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Conserved domains on  [gi|1952662956|ref|NP_001376527|]
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ubiquitin carboxyl-terminal hydrolase 19 isoform 20 [Homo sapiens]

Protein Classification

ubiquitin specific protease( domain architecture ID 12950357)

ubiquitin specific protease (such as USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
594-1316 7.14e-119

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 7.14e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  594 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 673
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  674 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 750
Cdd:COG5560    342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  751 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 829
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  830 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 909
Cdd:COG5560    487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  910 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 989
Cdd:COG5560    540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  990 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 1062
Cdd:COG5560    585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1063 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1142
Cdd:COG5560    639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1143 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1221
Cdd:COG5560    676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1222 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1301
Cdd:COG5560    737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                          730
                   ....*....|....*
gi 1952662956 1302 VVTRYAYVLFYRRRN 1316
Cdd:COG5560    809 SVTSSAYVLFYRRKS 823
USP19_linker super family cl24979
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
476-596 2.42e-54

Linker region of USP19 deubiquitinase; This region is generally located between a CS domain pfam04969 and the enzymatic UCH domain pfam00582 of USP19 deubiquitinases. This region is predicted to be natively unstructured. Its precise functional role is not known.


The actual alignment was detected with superfamily member pfam16602:

Pssm-ID: 465191  Cd Length: 121  Bit Score: 185.12  E-value: 2.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  476 RQSQRWGGLEAPAAR--VGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 553
Cdd:pfam16602    1 RHSQRWGGLEAPATQgaVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1952662956  554 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 596
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
389-485 4.55e-21

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


:

Pssm-ID: 107223  Cd Length: 84  Bit Score: 88.80  E-value: 4.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  389 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 468
Cdd:cd06466      1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                           90
                   ....*....|....*..
gi 1952662956  469 IDICLRKRQSQRWGGLE 485
Cdd:cd06466     68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
120-202 2.77e-06

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


:

Pssm-ID: 107220  Cd Length: 84  Bit Score: 46.51  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  120 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 194
Cdd:cd06463      1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                   ....*...
gi 1952662956  195 MLTWPSLL 202
Cdd:cd06463     77 GEWWPRLE 84
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
594-1316 7.14e-119

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 7.14e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  594 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 673
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  674 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 750
Cdd:COG5560    342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  751 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 829
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  830 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 909
Cdd:COG5560    487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  910 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 989
Cdd:COG5560    540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  990 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 1062
Cdd:COG5560    585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1063 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1142
Cdd:COG5560    639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1143 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1221
Cdd:COG5560    676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1222 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1301
Cdd:COG5560    737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                          730
                   ....*....|....*
gi 1952662956 1302 VVTRYAYVLFYRRRN 1316
Cdd:COG5560    809 SVTSSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1156-1313 5.96e-56

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 194.04  E-value: 5.96e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1156 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1235
Cdd:cd02674     81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952662956 1236 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1313
Cdd:cd02674    160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
476-596 2.42e-54

Linker region of USP19 deubiquitinase; This region is generally located between a CS domain pfam04969 and the enzymatic UCH domain pfam00582 of USP19 deubiquitinases. This region is predicted to be natively unstructured. Its precise functional role is not known.


Pssm-ID: 465191  Cd Length: 121  Bit Score: 185.12  E-value: 2.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  476 RQSQRWGGLEAPAAR--VGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 553
Cdd:pfam16602    1 RHSQRWGGLEAPATQgaVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1952662956  554 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 596
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
598-785 3.08e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 3.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  598 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHH-AFQPSKLKAIVA 676
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  677 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 756
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 1952662956  757 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 785
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
389-485 4.55e-21

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 88.80  E-value: 4.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  389 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 468
Cdd:cd06466      1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                           90
                   ....*....|....*..
gi 1952662956  469 IDICLRKRQSQRWGGLE 485
Cdd:cd06466     68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
120-202 2.77e-06

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 46.51  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  120 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 194
Cdd:cd06463      1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                   ....*...
gi 1952662956  195 MLTWPSLL 202
Cdd:cd06463     77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
386-475 5.81e-06

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 45.33  E-value: 5.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  386 VKNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHpgcgphttfrwqvKLRNLIEPEQCTFCFT 465
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELIDG-------------ELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 1952662956  466 ASRIDICLRK 475
Cdd:pfam04969   67 GKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
357-533 1.50e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 49.01  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  357 DDCAKEEM---------AVAADAATLVDEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFT 422
Cdd:PLN03088   114 DEKIAEEEkdlvqpvpsDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  423 LIFQTrdgnflrlhPGCGPhttFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEApaarvgGAKVAVPTGP 502
Cdd:PLN03088   193 VVIEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEY------GKGPAVLPKP 254
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1952662956  503 TpldsTPPGGAPHPLTGQEEARAVEKDKSKA 533
Cdd:PLN03088   255 N----VSSEVSQRPAYPSSKKKKDDWDKLEA 281
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
119-191 7.40e-03

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 36.85  E-value: 7.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952662956  119 DWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAKVqTRKGSLLHLTLPK 191
Cdd:pfam04969    4 DWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELiDGELFHPIDPEESSW-TIEGKKVEITLKK 76
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
594-1316 7.14e-119

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 7.14e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  594 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 673
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  674 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 750
Cdd:COG5560    342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  751 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 829
Cdd:COG5560    422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  830 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 909
Cdd:COG5560    487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  910 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 989
Cdd:COG5560    540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  990 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 1062
Cdd:COG5560    585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1063 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1142
Cdd:COG5560    639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1143 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1221
Cdd:COG5560    676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1222 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1301
Cdd:COG5560    737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                          730
                   ....*....|....*
gi 1952662956 1302 VVTRYAYVLFYRRRN 1316
Cdd:COG5560    809 SVTSSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1156-1313 5.96e-56

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 194.04  E-value: 5.96e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1156 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1235
Cdd:cd02674     81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952662956 1236 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1313
Cdd:cd02674    160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
476-596 2.42e-54

Linker region of USP19 deubiquitinase; This region is generally located between a CS domain pfam04969 and the enzymatic UCH domain pfam00582 of USP19 deubiquitinases. This region is predicted to be natively unstructured. Its precise functional role is not known.


Pssm-ID: 465191  Cd Length: 121  Bit Score: 185.12  E-value: 2.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  476 RQSQRWGGLEAPAAR--VGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 553
Cdd:pfam16602    1 RHSQRWGGLEAPATQgaVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1952662956  554 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 596
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
598-785 3.08e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 3.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  598 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHH-AFQPSKLKAIVA 676
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  677 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 756
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 1952662956  757 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 785
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1161-1312 1.47e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 169.93  E-value: 1.47e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1161 LDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWrDKINDLVEFPvRNLDLSKFCI 1240
Cdd:pfam00443  164 LQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFP-LELDLSRYLA 241
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952662956 1241 G---QKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDES-QVVTRYAYVLFY 1312
Cdd:pfam00443  242 EelkPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNR-------WYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1160-1313 1.82e-40

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 150.33  E-value: 1.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1160 TLDQCLNLFTRPEVLAPEEAWYCPqCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPvRNLDLSKFC 1239
Cdd:cd02257    100 SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFP-LELDLSPYL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1240 IGQKEEQLPS-----YDLYAVINHYGGMI-GGHYTACARlpnDRSSQRsdvgWRLFDDSTVTTVDESQVVTRY-----AY 1308
Cdd:cd02257    178 SEGEKDSDSDngsykYELVAVVVHSGTSAdSGHYVAYVK---DPSDGK----WYKFNDDKVTEVSEEEVLEFGslsssAY 250

                   ....*
gi 1952662956 1309 VLFYR 1313
Cdd:cd02257    251 ILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1148-1312 2.59e-35

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 137.89  E-value: 2.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1148 GSAGEAARAGHFTLDQCLNLFTRPEVLAPEeAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVE 1227
Cdd:cd02660    165 WALGESGVSGTPTLSDCLDRFTRPEKLGDF-AYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1228 FPVRnLDLSKFCIGQKEEQLPS--------YDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDE 1299
Cdd:cd02660    244 FPLE-LNMTPYTSSSIGDTQDSnsldpdytYDLFAVVVHKGTLDTGHYTAYCRQGDGQ--------WFKFDDAMITRVSE 314
                          170
                   ....*....|...
gi 1952662956 1300 SQVVTRYAYVLFY 1312
Cdd:cd02660    315 EEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1160-1312 2.99e-33

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 131.24  E-value: 2.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1160 TLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFsfrSFIWRDKINDLVEFPVRnLDLSKFc 1239
Cdd:cd02661    163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF---SNFRGGKINKQISFPET-LDLSPY- 237
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952662956 1240 IGQKEEQLPSYDLYAVINHYGGMI-GGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFY 1312
Cdd:cd02661    238 MSQPNDGPLKYKLYAVLVHSGFSPhSGHYYCYVKSSNGK--------WYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1159-1313 2.34e-29

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 119.03  E-value: 2.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1159 FTLDQCLNLFTRPEVLAPEEAWYCPQCKqhrEASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnLDLSKF 1238
Cdd:cd02667    111 CSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEI-LDLAPF 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1239 C----IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARL--PNDRSS-------QRSDVG-----WRLFDDSTVTTVDES 1300
Cdd:cd02667    187 CdpkcNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrpPQQRLSdltkskpAADEAGpgsgqWYYISDSDVREVSLE 266
                          170
                   ....*....|...
gi 1952662956 1301 QVVTRYAYVLFYR 1313
Cdd:cd02667    267 EVLKSEAYLLFYE 279
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-785 4.83e-26

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 108.14  E-value: 4.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthhafqpsklkaivask 678
Cdd:cd02674      1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  679 asqftgyaQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVCP 758
Cdd:cd02674     22 --------QQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                          170       180
                   ....*....|....*....|....*..
gi 1952662956  759 VCAKVSITFDPFLYLPVPLPQKQKVLP 785
Cdd:cd02674     56 TCGKTSTTFEPFTYLSLPIPSGSGDAP 82
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1165-1316 8.74e-25

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 107.34  E-value: 8.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1165 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfiW----RDKINDLVEFPVRnLDLSKFCI 1240
Cdd:cd02659    157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD---FetmmRIKINDRFEFPLE-LDMEPYTE 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1241 ----------GQKEEQLPSYDLYAVINHYGGMIGGHYTACARlpndrssQRSDVGWRLFDDSTVTTVDESQVVTRY---- 1306
Cdd:cd02659    233 kglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK-------DRDDGKWYKFNDDVVTPFDPNDAEEECfgge 305
                          170       180
                   ....*....|....*....|....*...
gi 1952662956 1307 ------------------AYVLFYRRRN 1316
Cdd:cd02659    306 etqktydsgprafkrttnAYMLFYERKS 333
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1158-1312 6.05e-22

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 98.15  E-value: 6.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1158 HFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWR-DKINDLVEFPvrnLDLS 1236
Cdd:cd02663    146 NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP---LELR 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1237 KF-CIGQKEEQLPSYDLYAVINHYGGMIG-GHYTacarlpndrSSQRSDVGWRLFDDSTVTTVDESQVVTRY-------- 1306
Cdd:cd02663    223 LFnTTDDAENPDRLYELVAVVVHIGGGPNhGHYV---------SIVKSHGGWLLFDDETVEKIDENAVEEFFgdspnqat 293

                   ....*.
gi 1952662956 1307 AYVLFY 1312
Cdd:cd02663    294 AYVLFY 299
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
599-782 2.45e-21

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 95.24  E-value: 2.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthhafqpsklkaivask 678
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  679 asqftgyaQHDAQEFMAFLLDGLHEDLNRIQNKpytetvdsdgrpdevvaeeawQRHKMRNDSFIVDLFQGQYKSKLVCP 758
Cdd:cd02257     22 --------QQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                          170       180
                   ....*....|....*....|....
gi 1952662956  759 VCAKVSITFDPFLYLPVPLPQKQK 782
Cdd:cd02257     73 ECGHESVSTEPELFLSLPLPVKGL 96
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
389-485 4.55e-21

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 88.80  E-value: 4.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  389 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 468
Cdd:cd06466      1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                           90
                   ....*....|....*..
gi 1952662956  469 IDICLRKRQSQRWGGLE 485
Cdd:cd06466     68 VEITLKKAEPGSWPSLE 84
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
598-775 6.78e-21

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 95.04  E-value: 6.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  598 TGLVNLGNTCFMNSVIQSLSNTRELRDFFhdRSFEAEINYNNPlgtggrlaiGFAVLL-------RALW---KGTHHAFQ 667
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYL--LSREHSKDCCNE---------GFCMMCaleahveRALAssgPGSAPRIF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  668 PSKLKAIvaskASQFTGYAQHDAQEFMAFLLDGLHED-LNRiqNKPYTETVDSDgrpdevvaeeawqrhkmRNDSFIVDL 746
Cdd:cd02661     71 SSNLKQI----SKHFRIGRQEDAHEFLRYLLDAMQKAcLDR--FKKLKAVDPSS-----------------QETTLVQQI 127
                          170       180
                   ....*....|....*....|....*....
gi 1952662956  747 FQGQYKSKLVCPVCAKVSITFDPFLYLPV 775
Cdd:cd02661    128 FGGYLRSQVKCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-780 4.03e-20

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 93.21  E-value: 4.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTRELRDFF----HDR-----------SFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTH 663
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFlsdrHSCtclscspnsclSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  664 HafqpsklkaivaskasqFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYtetvdsdgrpdevvaeeawqrHKMRNDSFI 743
Cdd:cd02660     82 N-----------------LAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAN---------------------DESHCNCII 123
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1952662956  744 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQK 780
Cdd:cd02660    124 HQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK 160
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1156-1313 3.11e-19

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 90.56  E-value: 3.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1156 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDKINDLVEFPvRNLD 1234
Cdd:cd02668    153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNASISFP-EILD 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1235 LSKFCIGQKeEQLPSYDLYAVINHYG-GMIGGHYTAcarlpNDRSSQRSDvgWRLFDDSTVTTVDESQV----------- 1302
Cdd:cd02668    232 MGEYLAESD-EGSYVYELSGVLIHQGvSAYSGHYIA-----HIKDEQTGE--WYKFNDEDVEEMPGKPLklgnsedpakp 303
                          170       180
                   ....*....|....*....|.
gi 1952662956 1303 ----------VTRYAYVLFYR 1313
Cdd:cd02668    304 rkseikkgthSSRTAYMLVYK 324
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1165-1313 1.77e-16

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 82.15  E-value: 1.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1165 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDK------INDLVEFPVRNLDLSK 1237
Cdd:cd02664    140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYdQKTHVREKimdnvsINEVLSLPVRVESKSS 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1238 FCIGQKEE-----------QLPSYDLYAVINHYG-GMIGGHYTACAR-------------LPNDRSSQRSDVGWRLFDDS 1292
Cdd:cd02664    220 ESPLEKKEeesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARdqtdadstgqecpEPKDAEENDESKNWYLFNDS 299
                          170       180
                   ....*....|....*....|....*...
gi 1952662956 1293 TVTTVD--ESQVVTRY-----AYVLFYR 1313
Cdd:cd02664    300 RVTFSSfeSVQNVTSRfpkdtPYILFYE 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-784 2.94e-16

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 80.89  E-value: 2.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRsfeaeinynnplgtggrlaigfavllralwkgthhafqPSKLKAIVASK 678
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  679 ASQFTGYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrnDSFIVDLFQGQYKSKLVCP 758
Cdd:cd02667     43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                          170       180
                   ....*....|....*....|....*.
gi 1952662956  759 VCAKVSITFDPFLYLPVPLPQKQKVL 784
Cdd:cd02667     85 SCGTVSLVYEPFLDLSLPRSDEIKSE 110
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-792 1.43e-15

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 79.46  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLsntrelrdfFHDRSFEAEINYNNPLGTGGRLAIGFA-VLLRALWKGTHHAFQPSKLKAIVAS 677
Cdd:cd02664      1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKlQLLQAHLMHTQRRAEAPPDYFLEAS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  678 KASQFTGYAQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVC 757
Cdd:cd02664     72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1952662956  758 PVCAKVSITFDPFLYLPVPLPQKQKVLPvFYFARE 792
Cdd:cd02664    114 LNCNSTSARTERFRDLDLSFPSVQDLLN-YFLSPE 147
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1128-1313 5.90e-15

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 77.63  E-value: 5.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1128 ERLQEF----VLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNV 1203
Cdd:cd02671    145 ERREDFqdisVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1204 LIVQLKRFSFRSFIWR-----DKINDLVEFPvrnLDLSKFCIGQKeEQLPSYDLYAVINHYGGMIG-GHYTACARlpndr 1277
Cdd:cd02671    225 ITIHLKCFAANGSEFDcygglSKVNTPLLTP---LKLSLEEWSTK-PKNDVYRLFAVVMHSGATISsGHYTAYVR----- 295
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1952662956 1278 ssqrsdvgWRLFDDSTVTTVDE---------SQVVTRYAYVLFYR 1313
Cdd:cd02671    296 --------WLLFDDSEVKVTEEkdflealspNTSSTSTPYLLFYK 332
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
594-780 4.02e-14

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 76.59  E-value: 4.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  594 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFhdrsfeaeINYNNPLGTGGR---LAIGFAVLLRALWkgTHHAFQ--- 667
Cdd:cd02669    116 LPGFVGLNNIKNNDYANVIIQALSHVKPIRNFF--------LLYENYENIKDRkseLVKRLSELIRKIW--NPRNFKghv 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  668 -PSK-LKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiQNKPYTETVDS--DG------RPDEVVAEEAWQRHKM 737
Cdd:cd02669    186 sPHElLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHDcfQGkvqietQKIKPHAEEEGSKDKF 264
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1952662956  738 RNDSFivdlfqgQYKSKLVcpvcakvsitfdPFLYLPVPLPQK 780
Cdd:cd02669    265 FKDSR-------VKKTSVS------------PFLLLTLDLPPP 288
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1188-1313 3.35e-12

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 68.90  E-value: 3.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1188 HREA--SKQLLLWRLPNVLIVQLKRFSFRSFI-WRDKINDLVEFPVrNLDLSKFCIgqkeeqlPS--YDLYAVINHYG-G 1261
Cdd:cd02657    182 GRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIqKKAKILRKVKFPF-ELDLYELCT-------PSgyYELVAVITHQGrS 253
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952662956 1262 MIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQVVT-------RYAYVLFYR 1313
Cdd:cd02657    254 ADSGHYVAWVRRKNDGK-------WIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
zf-MYND pfam01753
MYND finger;
892-934 6.01e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.28  E-value: 6.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1952662956  892 CAACQRkqqsEDEKLKRCTRCYRVGYCNQLCQKTHWPDHKGLC 934
Cdd:pfam01753    1 CAVCGK----EALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
599-723 7.85e-12

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.52  E-value: 7.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLS------NTRELRDFFHDRSFEAEINYNNPLGTgGRLAIGFavlLRALWKGTHHAFqpsklk 672
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlylpklDELLDDLSKELKVLKNVIRKPEPDLN-QEEALKL---FTALWSSKEHKV------ 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952662956  673 aivaskASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRP 723
Cdd:COG5533     71 ------GWIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKT 115
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1160-1314 1.16e-11

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1160 TLDQCLNLFtrpEVLAPE---------EAWYCpQCKQHREASKQlllwRLPNVLIVQLKRFSFRsfIWRDKINDLVEFPV 1230
Cdd:COG5533    138 TLQEFIDNM---EELVDDetgvkakenEELEV-QAKQEYEVSFV----KLPKILTIQLKRFANL--GGNQKIDTEVDEKF 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1231 rNLDLSKFCIGQKEEQLpSYDLYAVINHYGGMIGGHYTACARLPNDrssqrsdvgWRLFDDSTVTTVDESQVVT---RYA 1307
Cdd:COG5533    208 -ELPVKHDQILNIVKET-YYDLVGFVLHQGSLEGGHYIAYVKKGGK---------WEKANDSDVTPVSEEEAINekaKNA 276

                   ....*..
gi 1952662956 1308 YVLFYRR 1314
Cdd:COG5533    277 YLYFYER 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1160-1302 1.33e-11

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 69.51  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1160 TLDQCLNLFTRPEVLAPEEAWYCpQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfIWRD---KINDLVEFPVrNLDLS 1236
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNA-EKHGLQDAKKGVIFESLPPVLHLQLKRFEYD--FERDmmvKINDRYEFPL-EIDLL 414
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952662956 1237 KFC---IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQV 1302
Cdd:COG5077    415 PFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGR-------WYKFDDTRVTRATEKEV 476
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-779 3.02e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 66.18  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNT---RELRDFFHDRSfeaeinyNNPLGTGgrlaigfavllralwkgthhAFQPSKLKAIV 675
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYFEnllTCLKDLFESIS-------EQKKRTG--------------------VISPKKFITRL 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  676 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEvvaeeaWQRhkmrndSFIVDLFQGQYKSKL 755
Cdd:cd02663     54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAE------PQP------TWVHEIFQGILTNET 121
                          170       180
                   ....*....|....*....|....
gi 1952662956  756 VCPVCAKVSITFDPFLYLPVPLPQ 779
Cdd:cd02663    122 RCLTCETVSSRDETFLDLSIDVEQ 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1160-1312 4.96e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 64.31  E-value: 4.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1160 TLDQCLNLFTRPEVLapeEAWYCPQCkqhreaskQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnldLSKfc 1239
Cdd:cd02662     97 TLEHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPER---LPK-- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1240 igqkeeqlPSYDLYAVINHYGGMIGGHYTACARLP-----NDRSSQRSDVG---------WRLfDDSTVTTVDESQVVTR 1305
Cdd:cd02662    161 --------VLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdKEPGSFVRMREgpsstshpwWRI-SDTTVKEVSESEVLEQ 231

                   ....*...
gi 1952662956 1306 -YAYVLFY 1312
Cdd:cd02662    232 kSAYMLFY 239
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-757 7.80e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 65.04  E-value: 7.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTRELRDffhdrsfeAEINYNNPLGTGGRLAIGFAVLLRALWK---GTHHAFQPSKLKAIV 675
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRD--------ALKNYNPARRGANQSSDNLTNALRDLFDtmdKKQEPVPPIEFLQLL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  676 ASKASQFT------GYAQHDAQEFMAFLLDGLHEDLnriqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQG 749
Cdd:cd02657     73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGI 124

                   ....*...
gi 1952662956  750 QYKSKLVC 757
Cdd:cd02657    125 ELETKMKC 132
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-777 4.87e-10

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 62.34  E-value: 4.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNP----------LGTG---GRLAIgfAVLLRALWKGTHHA 665
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLADGllsGRYSK--PASLKSENDPYQVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  666 FQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTetvdsdgrpdevvaeeawqrhkmrndsfivD 745
Cdd:cd02658     79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPN------------------------------D 128
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1952662956  746 LFQGQYKSKLVCPVCAKVSITFDP--FLYLPVPL 777
Cdd:cd02658    129 LFKFMIEDRLECLSCKKVKYTSELseILSLPVPK 162
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1160-1313 1.20e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 61.18  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1160 TLDQCLNLFTRPEVLapEEawYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFiWRD-KINDLVEFPvrnldlskf 1238
Cdd:cd02658    179 PLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPkKLDVPIDVP--------- 244
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952662956 1239 cigqkEEQLPS-YDLYAVINHYGGMI-GGHYTACARLPNDRSSQrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFYR 1313
Cdd:cd02658    245 -----EELGPGkYELIAFISHKGTSVhSGHYVAHIKKEIDGEGK-----WVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
395-485 2.66e-09

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 55.37  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  395 PDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASRIDICLR 474
Cdd:cd06463      5 LDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGK------------EYLLEGELFGPIDPEESKWTVEDRKIEITLK 72
                           90
                   ....*....|..
gi 1952662956  475 KRQ-SQRWGGLE 485
Cdd:cd06463     73 KKEpGEWWPRLE 84
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
570-703 2.43e-07

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 54.51  E-value: 2.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  570 PPMPHSPVSgdsveeeeeEEKKVCLPGFTGLVNLGNTCFMNSVIQSLsntRELRDFFHDRSFEAEINynnplGTGGRLAI 649
Cdd:cd02671      6 APQPSSATS---------CEKRENLLPFVGLNNLGNTCYLNSVLQVL---YFCPGFKHGLKHLVSLI-----SSVEQLQS 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952662956  650 GFaVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHE 703
Cdd:cd02671     69 SF-LLNPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
596-775 2.90e-07

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 54.19  E-value: 2.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  596 GFTGLVNLGNTCFMNSVIQSLSNTRELRD----FFHDRSFEAEINYNNPLgtggRLAIGFAvllralwkgthhafQPSKL 671
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNavysIPPTEDDDDNKSVPLAL----QRLFLFL--------------QLSES 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  672 KAIVAS-KASQFT-------GYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaEEAWQrhKMRNDSFI 743
Cdd:cd02659     63 PVKTTElTDKTRSfgwdslnTFEQHDVQEFFRVLFDKL---------------------------EEKLK--GTGQEGLI 113
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1952662956  744 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPV 775
Cdd:cd02659    114 KNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
599-625 9.57e-07

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 51.60  E-value: 9.57e-07
                           10        20
                   ....*....|....*....|....*..
gi 1952662956  599 GLVNLGNTCFMNSVIQSLSNTRELRDF 625
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
120-202 2.77e-06

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 46.51  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  120 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 194
Cdd:cd06463      1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                   ....*...
gi 1952662956  195 MLTWPSLL 202
Cdd:cd06463     77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
386-475 5.81e-06

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 45.33  E-value: 5.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  386 VKNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHpgcgphttfrwqvKLRNLIEPEQCTFCFT 465
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELIDG-------------ELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 1952662956  466 ASRIDICLRK 475
Cdd:pfam04969   67 GKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
357-533 1.50e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 49.01  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  357 DDCAKEEM---------AVAADAATLVDEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFT 422
Cdd:PLN03088   114 DEKIAEEEkdlvqpvpsDLPSSVTAPPVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  423 LIFQTrdgnflrlhPGCGPhttFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEApaarvgGAKVAVPTGP 502
Cdd:PLN03088   193 VVIEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEY------GKGPAVLPKP 254
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1952662956  503 TpldsTPPGGAPHPLTGQEEARAVEKDKSKA 533
Cdd:PLN03088   255 N----VSSEVSQRPAYPSSKKKKDDWDKLEA 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1200-1312 1.84e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 47.55  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1200 LPNVLIVQLKRFSFRSFIwRDKINDLVEFPvrnldlskfcigQKEEQLPsYDLYAVINHYGGMIGGHYTAcarLPNDRSS 1279
Cdd:cd02665    128 LPPVLTFELSRFEFNQGR-PEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWA---YIYKQSR 190
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1952662956 1280 QRsdvgWRLFDDSTVTTVDESQVVTR--------YAYVLFY 1312
Cdd:cd02665    191 QE----WEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1182-1312 6.18e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 46.37  E-value: 6.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1182 CPQCKqHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRD-KINDLVefpvrnldLSKFCIgqkeeQLPSYDLYAVINHYG 1260
Cdd:cd02673    129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYlKKNEEI--------MKKYCG-----TDAKYSLVAVICHLG 194
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952662956 1261 -GMIGGHYTACARLPNDRSSqrsdvgWRLFDDSTVTTVDESQV---VTRYAYVLFY 1312
Cdd:cd02673    195 eSPYDGHYIAYTKELYNGSS------WLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1190-1261 1.14e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 46.16  E-value: 1.14e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952662956 1190 EASKQLLLWRLPNVLIVQLKRFSFRSFIwRDKINDLVEFPVRNLDLSKFCIGQKEEQLPS--YDLYAVINHYGG 1261
Cdd:cd02669    322 DSLKRYLISRLPKYLIFHIKRFSKNNFF-KEKNPTIVNFPIKNLDLSDYVHFDKPSLNLStkYNLVANIVHEGT 394
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
598-798 1.25e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 45.95  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  598 TGLVNLGNTCFMNSVIQSLSNTRELRDF---FHDRSFEAEINYNNPLGTGGR--------LAIGFAVLLRALWkgthHAF 666
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnFDESKAELASDYPTERRIGGRevsrselqRSNQFVYELRSLF----NDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  667 QPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGrpdEVVAEeawqrhkmrndsfIVDL 746
Cdd:cd02666     78 IHSNTRSVTPSKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDK---EQSDL-------------IKRL 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952662956  747 FQGQYKSKLV---CPVCAKVSITFDPFLYLPVPLPQKQKVLPVfyfarEPHSKPI 798
Cdd:cd02666    142 FSGKTKQQLVpesMGNQPSVRTKTERFLSLLVDVGKKGREIVV-----LLEPKDL 191
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
596-701 3.07e-04

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 45.25  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  596 GFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeaEINYNNPlgtGGRLAIGFAvlLRALWKGTHHAFQP-SKLKAI 674
Cdd:COG5077    192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY------GIPTDHP---RGRDSVALA--LQRLFYNLQTGEEPvDTTELT 260
                           90       100
                   ....*....|....*....|....*..
gi 1952662956  675 VASKASQFTGYAQHDAQEFMAFLLDGL 701
Cdd:COG5077    261 RSFGWDSDDSFMQHDIQEFNRVLQDNL 287
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
398-485 3.33e-04

p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup.


Pssm-ID: 107239  Cd Length: 84  Bit Score: 40.82  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  398 VVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLhpgcgphttfrwQVKLRNLIEPEQCTFCFTASRIDICLRKRQ 477
Cdd:cd06489      9 VVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSL------------KLHLLHPIVPEQSSYKILSTKIEIKLKKTE 76

                   ....*...
gi 1952662956  478 SQRWGGLE 485
Cdd:cd06489     77 AIRWSKLE 84
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
769-858 3.91e-04

Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.


Pssm-ID: 464201  Cd Length: 204  Bit Score: 43.24  E-value: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  769 PFLY--LPVPLPQKQKVLPV-FYFAREPHSKPIKFLVSVSKeNSTASEVLDSLSQSVHVKPE---NLRLAEVIKNRFHRV 842
Cdd:pfam14533    1 ALYYevLDISLSELENKKSIkVTWLSPGLKKEEELELLVPK-NGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKE 79
                           90
                   ....*....|....*.
gi 1952662956  843 FLPSHSLDTVSPSDTL 858
Cdd:pfam14533   80 LSEDEPIDSLNDYLTL 95
p23_NUDC_like cd06467
p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) ...
120-202 4.82e-04

p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) NUDC is needed for nuclear movement. AnNUDC is localized at the hyphal cortex, and binds NUDF at spindle pole bodies (SPBs) and in the cytoplasm at different stages in the cell cycle. At the SPBs it is part of the dynein molecular motor/NUDF complex that regulates microtubule dynamics. Mammalian(m) NUDC associates both with the dynein complex and also with an anti-inflammatory enzyme, platelet activating factor acetylhydrolase I, PAF-AH(I) complex, through binding mNUDF, the regulatory beta subunit of PAF-AH(I). mNUDC is important for cell proliferation both in normal and tumor tissues. Its expression is elevated in various cell types undergoing mitosis or stimulated to proliferate, with high expression levels observed in leukemic cells and tumors. For a leukemic cell line, human NUDC was shown to activate the thrombopoietin (TPO) receptor (Mpl) by binding to its extracellular domain, and promoting cell proliferation and differentiation. This group also includes the human broadly immunogenic tumor associated antigen, CML66, which is highly expressed in a variety of solid tumors and in leukemias. In normal tissues high expression of CML66 is limited to testis and heart.


Pssm-ID: 107224  Cd Length: 85  Bit Score: 40.22  E-value: 4.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  120 WRQSAEEVIVKLRVGVGpLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAkVQTR-KGSLLHLTLPKKVPMLT 197
Cdd:cd06467      3 WTQTLDEVTVTIPLPEG-TKSKDVKVEITPKHLKVGVKGGEPLlDGELYAKVKVDES-TWTLeDGKLLEITLEKRNEGEW 80

                   ....*
gi 1952662956  198 WPSLL 202
Cdd:cd06467     81 WPSLV 85
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
397-485 5.34e-04

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


Pssm-ID: 107238  Cd Length: 87  Bit Score: 40.36  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956  397 SVVVHVYVKEICRDTSRVLFREQDFT--LIFqtrDGNFlrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASRIDICLR 474
Cdd:cd06488     11 HVVVSVYAKNSNPELSVVEANSTVLTihIVF---EGNK-----------EFQLDIELWGVIDVEKSSVNMLPTKVEIKLR 76
                           90
                   ....*....|.
gi 1952662956  475 KRQSQRWGGLE 485
Cdd:cd06488     77 KAEPGSWAKLE 87
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1163-1312 5.93e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 40.19  E-value: 5.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1163 QCLNLFTRPEVLAPEeawYCPQCKQHREASKQLLLWRLPN----VLIVQLKRF-SFRSFIWRDKI-----NDLVEFPVRN 1232
Cdd:cd02672    121 QLLKRSLDLEKVTKA---WCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTnGEFDDINVVLPsgkvmQNKVSPKAID 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952662956 1233 LDLSKFCIGQKEeqLPSYDLYAVINHY-GGMIGGHYTACARLPNDRSSQRsdvGWRLFDDSTVTTVDESqvvtryAYVLF 1311
Cdd:cd02672    198 HDKLVKNRGQES--IYKYELVGYVCEInDSSRGQHNVVFVIKVNEESTHG---RWYLFNDFLVTPVSEL------AYILL 266

                   .
gi 1952662956 1312 Y 1312
Cdd:cd02672    267 Y 267
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
119-191 7.40e-03

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 36.85  E-value: 7.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952662956  119 DWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAKVqTRKGSLLHLTLPK 191
Cdd:pfam04969    4 DWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELiDGELFHPIDPEESSW-TIEGKKVEITLKK 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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