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Conserved domains on  [gi|530371803|ref|XP_005264884|]
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ubiquitin carboxyl-terminal hydrolase 19 isoform X4 [Homo sapiens]

Protein Classification

ubiquitin specific protease( domain architecture ID 12950362)

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];
583-1305 1.01e-118

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: 1.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  583 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 662
Cdd:COG5560   262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  663 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 739
Cdd:COG5560   342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  740 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 818
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  819 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 898
Cdd:COG5560   487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  899 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 978
Cdd:COG5560   540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  979 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 1051
Cdd:COG5560   585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1052 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1131
Cdd:COG5560   639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1132 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1210
Cdd:COG5560   676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1211 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1290
Cdd:COG5560   737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                         730
                  ....*....|....*
gi 530371803 1291 VVTRYAYVLFYRRRN 1305
Cdd:COG5560   809 SVTSSAYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
463-585 3.82e-58

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: 195.90  E-value: 3.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   463 RQSQRWGGLEAPAARGAVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 542
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530371803   543 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 585
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 ...
376-472 4.64e-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: 4.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  376 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 455
Cdd:cd06466     1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                          90
                  ....*....|....*..
gi 530371803  456 IDICLRKRQSQRWGGLE 472
Cdd:cd06466    68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
105-187 2.82e-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: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  105 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 179
Cdd:cd06463     1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                  ....*...
gi 530371803  180 MLTWPSLL 187
Cdd:cd06463    77 GEWWPRLE 84
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
583-1305 1.01e-118

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 1.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  583 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 662
Cdd:COG5560   262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  663 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 739
Cdd:COG5560   342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  740 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 818
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  819 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 898
Cdd:COG5560   487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  899 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 978
Cdd:COG5560   540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  979 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 1051
Cdd:COG5560   585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1052 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1131
Cdd:COG5560   639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1132 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1210
Cdd:COG5560   676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1211 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1290
Cdd:COG5560   737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                         730
                  ....*....|....*
gi 530371803 1291 VVTRYAYVLFYRRRN 1305
Cdd:COG5560   809 SVTSSAYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
463-585 3.82e-58

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: 195.90  E-value: 3.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   463 RQSQRWGGLEAPAARGAVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 542
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530371803   543 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 585
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1145-1302 6.08e-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: 6.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1145 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1224
Cdd:cd02674    81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530371803 1225 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1302
Cdd:cd02674   160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
587-774 3.15e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   587 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHH-AFQPSKLKAIVA 665
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   666 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 745
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 530371803   746 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 774
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 ...
376-472 4.64e-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: 4.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  376 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 455
Cdd:cd06466     1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                          90
                  ....*....|....*..
gi 530371803  456 IDICLRKRQSQRWGGLE 472
Cdd:cd06466    68 VEITLKKAEPGSWPSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
105-187 2.82e-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: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  105 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 179
Cdd:cd06463     1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                  ....*...
gi 530371803  180 MLTWPSLL 187
Cdd:cd06463    77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
373-462 5.92e-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: 5.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   373 VKNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHpgcgphttfrwqvKLRNLIEPEQCTFCFT 452
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELIDG-------------ELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 530371803   453 ASRIDICLRK 462
Cdd:pfam04969   67 GKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
342-522 9.78e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 46.32  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  342 DDCAKEEM--AVAADAATLVDG-----KEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFT 409
Cdd:PLN03088  114 DEKIAEEEkdLVQPVPSDLPSSvtappVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILS 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  410 LIFQTrdgnflrlhPGCGPhttFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEApaargavgGAKVAVPT 489
Cdd:PLN03088  193 VVIEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEY--------GKGPAVLP 252
                         170       180       190
                  ....*....|....*....|....*....|...
gi 530371803  490 GPTpldsTPPGGAPHPLTGQEEARAVEKDKSKA 522
Cdd:PLN03088  253 KPN----VSSEVSQRPAYPSSKKKKDDWDKLEA 281
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
104-176 7.54e-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: 7.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371803   104 DWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAKVqTRKGSLLHLTLPK 176
Cdd:pfam04969    4 DWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELiDGELFHPIDPEESSW-TIEGKKVEITLKK 76
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
583-1305 1.01e-118

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 391.55  E-value: 1.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  583 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKA 662
Cdd:COG5560   262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKK 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  663 IVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVD-SDGRPDEV--VAEEAWQRHKMRNDSFIVDLFQGQ 739
Cdd:COG5560   342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGM 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  740 YKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKvlpvfyfarepHSKPIKFLvsvsKENSTASEV-LDSLSQSVHVKPENL 818
Cdd:COG5560   422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV-----------WKHTIVVF----PESGRRQPLkIELDASSTIRGLKKL 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  819 RLAEviknrfhrvflpshsldtvspSDTLLCFELLSSELAKERVVVlEVQQRPQVPSVPISKCAACQRKQQSEDEklkrc 898
Cdd:COG5560   487 VDAE---------------------YGKLGCFEIKVMCIYYGGNYN-MLEPADKVLLQDIPQTDFVYLYETNDNG----- 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  899 trcyrVGYCnqlcqKTHWPDHKGLCRPENIGYPFLvsvpasrltyarlaqllegyarySVSVFQPPFqpGRMALESQSPG 978
Cdd:COG5560   540 -----IEVP-----VVHLRIEKGYKSKRLFGDPFL-----------------------QLNVLIKAS--IYDKLVKEFEE 584
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  979 CTTLLSTGSLEAG-DSERDPIQPPE------LQLVTpmaEGDTglPRVWAAPDRGPVPStsgissemlasgpievgslpa 1051
Cdd:COG5560   585 LLVLVEMKKTDVDlVSEQVRLLREEsspsswLKLET---EIDT--KREEQVEEEGQMNF--------------------- 638
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1052 gervsrPEAAVPGYQHPSEAMNahtpqfFIYKIDSSNREQRLEDKGDTPlelgddcslalvwrnnerlqefvlvaskele 1131
Cdd:COG5560   639 ------NDAVVISCEWEEKRYL------SLFSYDPLWTIREIGAAERTI------------------------------- 675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1132 caedpgsageaaraghfTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFiwRDK 1210
Cdd:COG5560   676 -----------------TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvRSF--RDK 736
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1211 INDLVEFPVRNLDLSKFcIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPndrssqrSDVGWRLFDDSTVTTVDESQ 1290
Cdd:COG5560   737 IDDLVEYPIDDLDLSGV-EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNF-------ANNGWYLFDDSRITEVDPED 808
                         730
                  ....*....|....*
gi 530371803 1291 VVTRYAYVLFYRRRN 1305
Cdd:COG5560   809 SVTSSAYVLFYRRKS 823
USP19_linker pfam16602
Linker region of USP19 deubiquitinase; This region is generally located between a CS domain ...
463-585 3.82e-58

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: 195.90  E-value: 3.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   463 RQSQRWGGLEAPAARGAVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVT 542
Cdd:pfam16602    1 RHSQRWGGLEAPATQGAVGGAKVAVPTGPTPLDKSQPGSSQHSLPSKEEPRVGEKEKPKTRVEDSGLDSVAPRTVSEHVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530371803   543 PKPETHLASPKPTCMVPPMPHSPVSGDSVeeEEEEEKKVCLPG 585
Cdd:pfam16602   81 IKQEPLLTSPKPTCMVPPMTHSPVSSESV--EEEEEKKVCLPG 121
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1145-1302 6.08e-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: 6.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1145 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFrSFIWRDKINDLVEFPVRNLDL 1224
Cdd:cd02674    81 APKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF-SRGSTRKLTTPVTFPLNDLDL 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530371803 1225 SKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvGWRLFDDSTVTTVDESQVVTRYAYVLFYR 1302
Cdd:cd02674   160 TPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETN-------DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
587-774 3.15e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   587 TGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTggrLAIGFAVLLRALWKGTHH-AFQPSKLKAIVA 665
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNSKSsSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   666 SKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQGQYKSKLV 745
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                          170       180
                   ....*....|....*....|....*....
gi 530371803   746 CPVCAKVSITFDPFLYLPVPLPQKQKVLP 774
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELK 160
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1150-1301 1.50e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 169.93  E-value: 1.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  1150 LDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWrDKINDLVEFPvRNLDLSKFCI 1229
Cdd:pfam00443  164 LQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFP-LELDLSRYLA 241
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371803  1230 G---QKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDES-QVVTRYAYVLFY 1301
Cdd:pfam00443  242 EelkPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNR-------WYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1149-1302 1.86e-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: 1.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1149 TLDQCLNLFTRPEVLAPEEAWYCPqCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPvRNLDLSKFC 1228
Cdd:cd02257   100 SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFP-LELDLSPYL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1229 IGQKEEQLPS-----YDLYAVINHYGGMI-GGHYTACARlpnDRSSQRsdvgWRLFDDSTVTTVDESQVVTRY-----AY 1297
Cdd:cd02257   178 SEGEKDSDSDngsykYELVAVVVHSGTSAdSGHYVAYVK---DPSDGK----WYKFNDDKVTEVSEEEVLEFGslsssAY 250

                  ....*
gi 530371803 1298 VLFYR 1302
Cdd:cd02257   251 ILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1137-1301 2.65e-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: 2.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1137 GSAGEAARAGHFTLDQCLNLFTRPEVLAPEeAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVE 1216
Cdd:cd02660   165 WALGESGVSGTPTLSDCLDRFTRPEKLGDF-AYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1217 FPVRnLDLSKFCIGQKEEQLPS--------YDLYAVINHYGGMIGGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDE 1288
Cdd:cd02660   244 FPLE-LNMTPYTSSSIGDTQDSnsldpdytYDLFAVVVHKGTLDTGHYTAYCRQGDGQ--------WFKFDDAMITRVSE 314
                         170
                  ....*....|...
gi 530371803 1289 SQVVTRYAYVLFY 1301
Cdd:cd02660   315 EEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1149-1301 3.06e-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: 3.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1149 TLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFsfrSFIWRDKINDLVEFPVRnLDLSKFc 1228
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF---SNFRGGKINKQISFPET-LDLSPY- 237
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371803 1229 IGQKEEQLPSYDLYAVINHYGGMI-GGHYTACARLPNDRssqrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFY 1301
Cdd:cd02661   238 MSQPNDGPLKYKLYAVLVHSGFSPhSGHYYCYVKSSNGK--------WYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1148-1302 2.48e-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: 2.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1148 FTLDQCLNLFTRPEVLAPEEAWYCPQCKqhrEASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnLDLSKF 1227
Cdd:cd02667   111 CSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEI-LDLAPF 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1228 C----IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARL--PNDRSS-------QRSDVG-----WRLFDDSTVTTVDES 1289
Cdd:cd02667   187 CdpkcNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrpPQQRLSdltkskpAADEAGpgsgqWYYISDSDVREVSLE 266
                         170
                  ....*....|...
gi 530371803 1290 QVVTRYAYVLFYR 1302
Cdd:cd02667   267 EVLKSEAYLLFYE 279
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-774 4.94e-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: 4.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthhafqpsklkaivask 667
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  668 asqftgyaQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVCP 747
Cdd:cd02674    22 --------QQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180
                  ....*....|....*....|....*..
gi 530371803  748 VCAKVSITFDPFLYLPVPLPQKQKVLP 774
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSGDAP 82
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1154-1305 8.94e-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: 8.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1154 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfiW----RDKINDLVEFPVRnLDLSKFCI 1229
Cdd:cd02659   157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFD---FetmmRIKINDRFEFPLE-LDMEPYTE 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1230 ----------GQKEEQLPSYDLYAVINHYGGMIGGHYTACARlpndrssQRSDVGWRLFDDSTVTTVDESQVVTRY---- 1295
Cdd:cd02659   233 kglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK-------DRDDGKWYKFNDDVVTPFDPNDAEEECfgge 305
                         170       180
                  ....*....|....*....|....*...
gi 530371803 1296 ------------------AYVLFYRRRN 1305
Cdd:cd02659   306 etqktydsgprafkrttnAYMLFYERKS 333
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1147-1301 6.18e-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: 6.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1147 HFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWR-DKINDLVEFPvrnLDLS 1225
Cdd:cd02663   146 NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP---LELR 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1226 KF-CIGQKEEQLPSYDLYAVINHYGGMIG-GHYTacarlpndrSSQRSDVGWRLFDDSTVTTVDESQVVTRY-------- 1295
Cdd:cd02663   223 LFnTTDDAENPDRLYELVAVVVHIGGGPNhGHYV---------SIVKSHGGWLLFDDETVEKIDENAVEEFFgdspnqat 293

                  ....*.
gi 530371803 1296 AYVLFY 1301
Cdd:cd02663   294 AYVLFY 299
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
588-771 2.51e-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: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTrelrdffhdrsfeaeinynnplgtggrlaigfavllralwkgthhafqpsklkaivask 667
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  668 asqftgyaQHDAQEFMAFLLDGLHEDLNRIQNKpytetvdsdgrpdevvaeeawQRHKMRNDSFIVDLFQGQYKSKLVCP 747
Cdd:cd02257    22 --------QQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                         170       180
                  ....*....|....*....|....
gi 530371803  748 VCAKVSITFDPFLYLPVPLPQKQK 771
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 ...
376-472 4.64e-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: 4.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  376 DSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASR 455
Cdd:cd06466     1 DWYQT-DTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGS------------EYQLELDLFGPIDPEQSKVSVLPTK 67
                          90
                  ....*....|....*..
gi 530371803  456 IDICLRKRQSQRWGGLE 472
Cdd:cd06466    68 VEITLKKAEPGSWPSLE 84
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
587-764 6.93e-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: 6.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  587 TGLVNLGNTCFMNSVIQSLSNTRELRDFFhdRSFEAEINYNNPlgtggrlaiGFAVLL-------RALW---KGTHHAFQ 656
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYL--LSREHSKDCCNE---------GFCMMCaleahveRALAssgPGSAPRIF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  657 PSKLKAIvaskASQFTGYAQHDAQEFMAFLLDGLHED-LNRiqNKPYTETVDSDgrpdevvaeeawqrhkmRNDSFIVDL 735
Cdd:cd02661    71 SSNLKQI----SKHFRIGRQEDAHEFLRYLLDAMQKAcLDR--FKKLKAVDPSS-----------------QETTLVQQI 127
                         170       180
                  ....*....|....*....|....*....
gi 530371803  736 FQGQYKSKLVCPVCAKVSITFDPFLYLPV 764
Cdd:cd02661   128 FGGYLRSQVKCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-769 4.13e-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: 4.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTRELRDFF----HDR-----------SFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTH 652
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFlsdrHSCtclscspnsclSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  653 HafqpsklkaivaskasqFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYtetvdsdgrpdevvaeeawqrHKMRNDSFI 732
Cdd:cd02660    82 N-----------------LAGYSQQDAHEFFQFLLDQLHTHYGGDKNEAN---------------------DESHCNCII 123
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530371803  733 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQK 769
Cdd:cd02660   124 HQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK 160
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1145-1302 3.18e-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: 3.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1145 AGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDKINDLVEFPvRNLD 1223
Cdd:cd02668   153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNASISFP-EILD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1224 LSKFCIGQKeEQLPSYDLYAVINHYG-GMIGGHYTAcarlpNDRSSQRSDvgWRLFDDSTVTTVDESQV----------- 1291
Cdd:cd02668   232 MGEYLAESD-EGSYVYELSGVLIHQGvSAYSGHYIA-----HIKDEQTGE--WYKFNDEDVEEMPGKPLklgnsedpakp 303
                         170       180
                  ....*....|....*....|.
gi 530371803 1292 ----------VTRYAYVLFYR 1302
Cdd:cd02668   304 rkseikkgthSSRTAYMLVYK 324
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1154-1302 1.81e-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: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1154 LNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSF-RSFIWRDK------INDLVEFPVRNLDLSK 1226
Cdd:cd02664   140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYdQKTHVREKimdnvsINEVLSLPVRVESKSS 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1227 FCIGQKEE-----------QLPSYDLYAVINHYG-GMIGGHYTACAR-------------LPNDRSSQRSDVGWRLFDDS 1281
Cdd:cd02664   220 ESPLEKKEeesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARdqtdadstgqecpEPKDAEENDESKNWYLFNDS 299
                         170       180
                  ....*....|....*....|....*...
gi 530371803 1282 TVTTVD--ESQVVTRY-----AYVLFYR 1302
Cdd:cd02664   300 RVTFSSfeSVQNVTSRfpkdtPYILFYE 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-773 3.04e-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: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRsfeaeinynnplgtggrlaigfavllralwkgthhafqPSKLKAIVASK 667
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  668 ASQFTGYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrnDSFIVDLFQGQYKSKLVCP 747
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                         170       180
                  ....*....|....*....|....*.
gi 530371803  748 VCAKVSITFDPFLYLPVPLPQKQKVL 773
Cdd:cd02667    85 SCGTVSLVYEPFLDLSLPRSDEIKSE 110
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-781 1.46e-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: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLsntrelrdfFHDRSFEAEINYNNPLGTGGRLAIGFA-VLLRALWKGTHHAFQPSKLKAIVAS 666
Cdd:cd02664     1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKlQLLQAHLMHTQRRAEAPPDYFLEAS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  667 KASQFTGYAQHDAQEFMAFLLDGLHedlnriqnkpytetvdsdgrpdevvaeeawqrhkmrndSFIVDLFQGQYKSKLVC 746
Cdd:cd02664    72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530371803  747 PVCAKVSITFDPFLYLPVPLPQKQKVLPvFYFARE 781
Cdd:cd02664   114 LNCNSTSARTERFRDLDLSFPSVQDLLN-YFLSPE 147
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1117-1302 4.59e-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: 78.01  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1117 ERLQEF----VLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNV 1192
Cdd:cd02671   145 ERREDFqdisVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1193 LIVQLKRFSFRSFIWR-----DKINDLVEFPvrnLDLSKFCIGQKeEQLPSYDLYAVINHYGGMIG-GHYTACARlpndr 1266
Cdd:cd02671   225 ITIHLKCFAANGSEFDcygglSKVNTPLLTP---LKLSLEEWSTK-PKNDVYRLFAVVMHSGATISsGHYTAYVR----- 295
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 530371803 1267 ssqrsdvgWRLFDDSTVTTVDE---------SQVVTRYAYVLFYR 1302
Cdd:cd02671   296 --------WLLFDDSEVKVTEEkdflealspNTSSTSTPYLLFYK 332
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
583-769 4.11e-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: 4.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  583 LPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFhdrsfeaeINYNNPLGTGGR---LAIGFAVLLRALWkgTHHAFQ--- 656
Cdd:cd02669   116 LPGFVGLNNIKNNDYANVIIQALSHVKPIRNFF--------LLYENYENIKDRkseLVKRLSELIRKIW--NPRNFKghv 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  657 -PSK-LKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRiQNKPYTETVDS--DG------RPDEVVAEEAWQRHKM 726
Cdd:cd02669   186 sPHElLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHDcfQGkvqietQKIKPHAEEEGSKDKF 264
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 530371803  727 RNDSFivdlfqgQYKSKLVcpvcakvsitfdPFLYLPVPLPQK 769
Cdd:cd02669   265 FKDSR-------VKKTSVS------------PFLLLTLDLPPP 288
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1177-1302 3.42e-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: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1177 HREA--SKQLLLWRLPNVLIVQLKRFSFRSFI-WRDKINDLVEFPVrNLDLSKFCIgqkeeqlPS--YDLYAVINHYG-G 1250
Cdd:cd02657   182 GRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIqKKAKILRKVKFPF-ELDLYELCT-------PSgyYELVAVITHQGrS 253
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530371803 1251 MIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQVVT-------RYAYVLFYR 1302
Cdd:cd02657   254 ADSGHYVAWVRRKNDGK-------WIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
zf-MYND pfam01753
MYND finger;
881-923 5.72e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.28  E-value: 5.72e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 530371803   881 CAACQRkqqsEDEKLKRCTRCYRVGYCNQLCQKTHWPDHKGLC 923
Cdd:pfam01753    1 CAVCGK----EALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
588-712 8.02e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.52  E-value: 8.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLS------NTRELRDFFHDRSFEAEINYNNPLGTgGRLAIGFavlLRALWKGTHHAFqpsklk 661
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlylpklDELLDDLSKELKVLKNVIRKPEPDLN-QEEALKL---FTALWSSKEHKV------ 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530371803  662 aivaskASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRP 712
Cdd:COG5533    71 ------GWIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKT 115
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1149-1303 1.18e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1149 TLDQCLNLFtrpEVLAPE---------EAWYCpQCKQHREASKQlllwRLPNVLIVQLKRFSFRsfIWRDKINDLVEFPV 1219
Cdd:COG5533   138 TLQEFIDNM---EELVDDetgvkakenEELEV-QAKQEYEVSFV----KLPKILTIQLKRFANL--GGNQKIDTEVDEKF 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1220 rNLDLSKFCIGQKEEQLpSYDLYAVINHYGGMIGGHYTACARLPNDrssqrsdvgWRLFDDSTVTTVDESQVVT---RYA 1296
Cdd:COG5533   208 -ELPVKHDQILNIVKET-YYDLVGFVLHQGSLEGGHYIAYVKKGGK---------WEKANDSDVTPVSEEEAINekaKNA 276

                  ....*..
gi 530371803 1297 YVLFYRR 1303
Cdd:COG5533   277 YLYFYER 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1149-1291 1.36e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 69.51  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1149 TLDQCLNLFTRPEVLAPEEAWYCpQCKQHREASKQLLLWRLPNVLIVQLKRFSFRsfIWRD---KINDLVEFPVrNLDLS 1225
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNA-EKHGLQDAKKGVIFESLPPVLHLQLKRFEYD--FERDmmvKINDRYEFPL-EIDLL 414
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530371803 1226 KFC---IGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSsqrsdvgWRLFDDSTVTTVDESQV 1291
Cdd:COG5077   415 PFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGR-------WYKFDDTRVTRATEKEV 476
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-768 3.09e-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: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNT---RELRDFFHDRSfeaeinyNNPLGTGgrlaigfavllralwkgthhAFQPSKLKAIV 664
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFEnllTCLKDLFESIS-------EQKKRTG--------------------VISPKKFITRL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  665 ASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEvvaeeaWQRhkmrndSFIVDLFQGQYKSKL 744
Cdd:cd02663    54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAE------PQP------TWVHEIFQGILTNET 121
                         170       180
                  ....*....|....*....|....
gi 530371803  745 VCPVCAKVSITFDPFLYLPVPLPQ 768
Cdd:cd02663   122 RCLTCETVSSRDETFLDLSIDVEQ 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1149-1301 5.06e-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: 5.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1149 TLDQCLNLFTRPEVLapeEAWYCPQCkqhreaskQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRnldLSKfc 1228
Cdd:cd02662    97 TLEHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPER---LPK-- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1229 igqkeeqlPSYDLYAVINHYGGMIGGHYTACARLP-----NDRSSQRSDVG---------WRLfDDSTVTTVDESQVVTR 1294
Cdd:cd02662   161 --------VLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdKEPGSFVRMREgpsstshpwWRI-SDTTVKEVSESEVLEQ 231

                  ....*...
gi 530371803 1295 -YAYVLFY 1301
Cdd:cd02662   232 kSAYMLFY 239
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-746 7.97e-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: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTRELRDffhdrsfeAEINYNNPLGTGGRLAIGFAVLLRALWK---GTHHAFQPSKLKAIV 664
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRD--------ALKNYNPARRGANQSSDNLTNALRDLFDtmdKKQEPVPPIEFLQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  665 ASKASQFT------GYAQHDAQEFMAFLLDGLHEDLnriqnkpytetvdsdgrpdevvaeeawqRHKMRNDSFIVDLFQG 738
Cdd:cd02657    73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGI 124

                  ....*...
gi 530371803  739 QYKSKLVC 746
Cdd:cd02657   125 ELETKMKC 132
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-766 4.97e-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: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNP----------LGTG---GRLAIgfAVLLRALWKGTHHA 654
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLADGllsGRYSK--PASLKSENDPYQVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  655 FQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTetvdsdgrpdevvaeeawqrhkmrndsfivD 734
Cdd:cd02658    79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPN------------------------------D 128
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530371803  735 LFQGQYKSKLVCPVCAKVSITFDP--FLYLPVPL 766
Cdd:cd02658   129 LFKFMIEDRLECLSCKKVKYTSELseILSLPVPK 162
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1149-1302 1.23e-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: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1149 TLDQCLNLFTRPEVLapEEawYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFiWRD-KINDLVEFPvrnldlskf 1227
Cdd:cd02658   179 PLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPkKLDVPIDVP--------- 244
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530371803 1228 cigqkEEQLPS-YDLYAVINHYGGMI-GGHYTACARLPNDRSSQrsdvgWRLFDDSTVTTVDESQVVTRYAYVLFYR 1302
Cdd:cd02658   245 -----EELGPGkYELIAFISHKGTSVhSGHYVAHIKKEIDGEGK-----WVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
382-472 2.71e-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: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  382 PDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNflrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASRIDICLR 461
Cdd:cd06463     5 LDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGK------------EYLLEGELFGPIDPEESKWTVEDRKIEITLK 72
                          90
                  ....*....|..
gi 530371803  462 KRQ-SQRWGGLE 472
Cdd:cd06463    73 KKEpGEWWPRLE 84
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
559-692 2.21e-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: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  559 PPMPHSPVSgdsveeeeeEEKKVCLPGFTGLVNLGNTCFMNSVIQSLsntRELRDFFHDRSFEAEINynnplGTGGRLAI 638
Cdd:cd02671     6 APQPSSATS---------CEKRENLLPFVGLNNLGNTCYLNSVLQVL---YFCPGFKHGLKHLVSLI-----SSVEQLQS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371803  639 GFaVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHE 692
Cdd:cd02671    69 SF-LLNPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
585-764 2.96e-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: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  585 GFTGLVNLGNTCFMNSVIQSLSNTRELRD----FFHDRSFEAEINYNNPLgtggRLAIGFAvllralwkgthhafQPSKL 660
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNavysIPPTEDDDDNKSVPLAL----QRLFLFL--------------QLSES 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  661 KAIVAS-KASQFT-------GYAQHDAQEFMAFLLDGLhedlnriqnkpytetvdsdgrpdevvaEEAWQrhKMRNDSFI 732
Cdd:cd02659    63 PVKTTElTDKTRSfgwdslnTFEQHDVQEFFRVLFDKL---------------------------EEKLK--GTGQEGLI 113
                         170       180       190
                  ....*....|....*....|....*....|..
gi 530371803  733 VDLFQGQYKSKLVCPVCAKVSITFDPFLYLPV 764
Cdd:cd02659   114 KNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
588-614 9.77e-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: 9.77e-07
                          10        20
                  ....*....|....*....|....*..
gi 530371803  588 GLVNLGNTCFMNSVIQSLSNTRELRDF 614
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
105-187 2.82e-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: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  105 WRQSAEEVIVKLRV-GVGPlqlEDVDAAFTDT--DCVVRFAGGQ--QWGGVFYAEIKSSCAKVqTRKGSLLHLTLPKKVP 179
Cdd:cd06463     1 WYQTLDEVTITIPLkDVTK---KDVKVEFTPKslTVSVKGGGGKeyLLEGELFGPIDPEESKW-TVEDRKIEITLKKKEP 76

                  ....*...
gi 530371803  180 MLTWPSLL 187
Cdd:cd06463    77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
373-462 5.92e-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: 5.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   373 VKNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHpgcgphttfrwqvKLRNLIEPEQCTFCFT 452
Cdd:pfam04969    1 PRYDWYQT-LDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYELIDG-------------ELFHPIDPEESSWTIE 66
                           90
                   ....*....|
gi 530371803   453 ASRIDICLRK 462
Cdd:pfam04969   67 GKKVEITLKK 76
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1189-1301 1.87e-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: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1189 LPNVLIVQLKRFSFRSFIwRDKINDLVEFPvrnldlskfcigQKEEQLPsYDLYAVINHYGGMIGGHYTAcarLPNDRSS 1268
Cdd:cd02665   128 LPPVLTFELSRFEFNQGR-PEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWA---YIYKQSR 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530371803 1269 QRsdvgWRLFDDSTVTTVDESQVVTR--------YAYVLFY 1301
Cdd:cd02665   191 QE----WEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1171-1301 6.31e-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: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1171 CPQCKqHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRD-KINDLVefpvrnldLSKFCIgqkeeQLPSYDLYAVINHYG 1249
Cdd:cd02673   129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYlKKNEEI--------MKKYCG-----TDAKYSLVAVICHLG 194
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371803 1250 -GMIGGHYTACARLPNDRSSqrsdvgWRLFDDSTVTTVDESQV---VTRYAYVLFY 1301
Cdd:cd02673   195 eSPYDGHYIAYTKELYNGSS------WLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
342-522 9.78e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 46.32  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  342 DDCAKEEM--AVAADAATLVDG-----KEPESMVNLAFV-----KNDSYEKgPDSVVVHVYVKEICRDTSRVLFREQDFT 409
Cdd:PLN03088  114 DEKIAEEEkdLVQPVPSDLPSSvtappVEEADATPVVPPskpkyRHEFYQK-PEEVVVTVFAKGVPAENVNVDFGEQILS 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  410 LIFQTrdgnflrlhPGCGPhttFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEApaargavgGAKVAVPT 489
Cdd:PLN03088  193 VVIEV---------PGEDA---YHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEY--------GKGPAVLP 252
                         170       180       190
                  ....*....|....*....|....*....|...
gi 530371803  490 GPTpldsTPPGGAPHPLTGQEEARAVEKDKSKA 522
Cdd:PLN03088  253 KPN----VSSEVSQRPAYPSSKKKKDDWDKLEA 281
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1179-1250 1.17e-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: 1.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371803 1179 EASKQLLLWRLPNVLIVQLKRFSFRSFIwRDKINDLVEFPVRNLDLSKFCIGQKEEQLPS--YDLYAVINHYGG 1250
Cdd:cd02669   322 DSLKRYLISRLPKYLIFHIKRFSKNNFF-KEKNPTIVNFPIKNLDLSDYVHFDKPSLNLStkYNLVANIVHEGT 394
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
587-787 1.28e-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: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  587 TGLVNLGNTCFMNSVIQSLSNTRELRDF---FHDRSFEAEINYNNPLGTGGR--------LAIGFAVLLRALWkgthHAF 655
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnFDESKAELASDYPTERRIGGRevsrselqRSNQFVYELRSLF----NDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  656 QPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGrpdEVVAEeawqrhkmrndsfIVDL 735
Cdd:cd02666    78 IHSNTRSVTPSKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDK---EQSDL-------------IKRL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530371803  736 FQGQYKSKLV---CPVCAKVSITFDPFLYLPVPLPQKQKVLPVfyfarEPHSKPI 787
Cdd:cd02666   142 FSGKTKQQLVpesMGNQPSVRTKTERFLSLLVDVGKKGREIVV-----LLEPKDL 191
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
585-690 3.13e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 45.25  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  585 GFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHdrsfeaEINYNNPlgtGGRLAIGFAvlLRALWKGTHHAFQP-SKLKAI 663
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY------GIPTDHP---RGRDSVALA--LQRLFYNLQTGEEPvDTTELT 260
                          90       100
                  ....*....|....*....|....*..
gi 530371803  664 VASKASQFTGYAQHDAQEFMAFLLDGL 690
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 ...
385-472 3.39e-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: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  385 VVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLhpgcgphttfrwQVKLRNLIEPEQCTFCFTASRIDICLRKRQ 464
Cdd:cd06489     9 VVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSL------------KLHLLHPIVPEQSSYKILSTKIEIKLKKTE 76

                  ....*...
gi 530371803  465 SQRWGGLE 472
Cdd:cd06489    77 AIRWSKLE 84
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
758-847 3.99e-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: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803   758 PFLY--LPVPLPQKQKVLPV-FYFAREPHSKPIKFLVSVSKeNSTASEVLDSLSQSVHVKPE---NLRLAEVIKNRFHRV 831
Cdd:pfam14533    1 ALYYevLDISLSELENKKSIkVTWLSPGLKKEEELELLVPK-NGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKE 79
                           90
                   ....*....|....*.
gi 530371803   832 FLPSHSLDTVSPSDTL 847
Cdd:pfam14533   80 LSEDEPIDSLNDYLTL 95
p23_NUDC_like cd06467
p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) ...
105-187 4.91e-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: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  105 WRQSAEEVIVKLRVGVGpLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAkVQTR-KGSLLHLTLPKKVPMLT 182
Cdd:cd06467     3 WTQTLDEVTVTIPLPEG-TKSKDVKVEITPKHLKVGVKGGEPLlDGELYAKVKVDES-TWTLeDGKLLEITLEKRNEGEW 80

                  ....*
gi 530371803  183 WPSLL 187
Cdd:cd06467    81 WPSLV 85
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
384-472 5.44e-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: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803  384 SVVVHVYVKEICRDTSRVLFREQDFT--LIFqtrDGNFlrlhpgcgphtTFRWQVKLRNLIEPEQCTFCFTASRIDICLR 461
Cdd:cd06488    11 HVVVSVYAKNSNPELSVVEANSTVLTihIVF---EGNK-----------EFQLDIELWGVIDVEKSSVNMLPTKVEIKLR 76
                          90
                  ....*....|.
gi 530371803  462 KRQSQRWGGLE 472
Cdd:cd06488    77 KAEPGSWAKLE 87
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1152-1301 6.05e-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: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1152 QCLNLFTRPEVLAPEeawYCPQCKQHREASKQLLLWRLPN----VLIVQLKRF-SFRSFIWRDKI-----NDLVEFPVRN 1221
Cdd:cd02672   121 QLLKRSLDLEKVTKA---WCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTnGEFDDINVVLPsgkvmQNKVSPKAID 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371803 1222 LDLSKFCIGQKEeqLPSYDLYAVINHY-GGMIGGHYTACARLPNDRSSQRsdvGWRLFDDSTVTTVDESqvvtryAYVLF 1300
Cdd:cd02672   198 HDKLVKNRGQES--IYKYELVGYVCEInDSSRGQHNVVFVIKVNEESTHG---RWYLFNDFLVTPVSEL------AYILL 266

                  .
gi 530371803 1301 Y 1301
Cdd:cd02672   267 Y 267
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
104-176 7.54e-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: 7.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371803   104 DWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQW-GGVFYAEIKSSCAKVqTRKGSLLHLTLPK 176
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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