|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
903-1055 |
7.54e-79 |
|
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor C, RFC1. RFC complexes hydrolyse ATP and load sliding clamps such as PCNA (proliferating cell nuclear antigen) onto double-stranded DNA. RFC1 is essential for RFC function in vivo.
Pssm-ID: 462507 Cd Length: 158 Bit Score: 255.20 E-value: 7.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 903 ICDGDIVDRQIRSKQNWNLLPTQAIYASVLPGELMRGYMSQFPVFPSWLGKFSSTGKHDRIIQELAMHMSLRTQTCKRTV 982
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006366332 983 NMEYLSYLRDALVQPLKDFGADGVQQAIACMDSYCLMKEDVENIMEISTWG----GKPSPFSKLDPKVKAAFTRAYN 1055
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYN 157
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
574-991 |
1.04e-55 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 201.69 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 574 RLLWVDKYKPVSLKAIIGQQGEQscaNKLLRWLRNWhkntlEDGQAKpsktgskddgtgfKAALLSGPPGVGKTTTAALV 653
Cdd:PRK04195 1 MMPWVEKYRPKTLSDVVGNEKAK---EQLREWIESW-----LKGKPK-------------KALLLYGPPGVGKTSLAHAL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 654 CKELGYSYVELNASDTRSKNSLKEVVAESLNNTSIkdfccgassSVSRKHVLIMDEVDGMAGNEDRGGIQELIGLIRHTK 733
Cdd:PRK04195 60 ANDYGWEVIELNASDQRTADVIERVAGEAATSGSL---------FGARRKLILLDEVDGIHGNEDRGGARAILELIKKAK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 734 IPIICMCNDRNHPKMRSLVHYCLDLRFQRPRLEQIKGAMMSIAFKEGLKIPPPAMQEIILAANQDIRQVLHNLNMWCAKD 813
Cdd:PRK04195 131 QPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAEGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 814 KSLTYDEAKTDASRakkDIKLGPFDVVRKVFAT--GEEA--ARMSLIDKSDLFFHdyslaplFVQEN--YVHVKPAAagg 887
Cdd:PRK04195 211 GKLTLEDVKTLGRR---DREESIFDALDAVFKArnADQAleASYDVDEDPDDLIE-------WIDENipKEYDDPED--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 888 nlkkhlvlLSKAADSICDGDIVDRQIRSKQNWNLLPtqaiYASvlpgELM------------RG---YMsqfpvFPSWLG 952
Cdd:PRK04195 278 --------IARAYDALSRADIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGftrYQ-----PPSYWR 336
|
410 420 430
....*....|....*....|....*....|....*....
gi 2006366332 953 KFSSTGKHDRIIQELAMHMSLRTQTCKRTVNMEYLSYLR 991
Cdd:PRK04195 337 LLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
392-470 |
4.08e-48 |
|
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349383 [Multi-domain] Cd Length: 79 Bit Score: 165.46 E-value: 4.08e-48
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006366332 392 GAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSKCEKASTLGTKIIDEDGLFDLIR 470
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
388-469 |
2.08e-26 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 116.28 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 388 EIPQGAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGqSKCEKASTLGTKIIDEDGLFD 467
Cdd:COG0272 587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665
|
..
gi 2006366332 468 LI 469
Cdd:COG0272 666 LL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
382-469 |
8.59e-24 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 107.90 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 382 KALGSKEIPQGAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGqSKCEKASTLGTKIID 461
Cdd:PRK07956 576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654
|
....*...
gi 2006366332 462 EDGLFDLI 469
Cdd:PRK07956 655 EEEFLRLL 662
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
637-742 |
7.48e-16 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 75.32 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 637 LLSGPPGVGKTTTAALVCKELGYSYVELNASDTRSKnslkeVVAESLNNtsIKDFCCGASSsvSRKHVLIMDEVDGMAGN 716
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEAAKK--LAPCVIFIDEIDALAGS 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 2006366332 717 EDRGGIQELIGLI------------RHTKIPIICMCND 742
Cdd:pfam00004 73 RGSGGDSESRRVVnqllteldgftsSNSKVIVIAATNR 110
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
394-469 |
3.26e-15 |
|
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.
Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 71.56 E-value: 3.26e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 394 ENCLEGLTFVITGvLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMgrDCGQSKCEKASTLGTKIIDEDGLFDLI 469
Cdd:pfam00533 3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
394-469 |
3.77e-15 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 71.25 E-value: 3.77e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006366332 394 ENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSKCE--KASTLGTKIIDEDGLFDLI 469
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDCL 78
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
633-760 |
6.19e-15 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 73.33 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 633 FKAALLSGPPGVGKTTTAALVCKEL---GYSYVELNASDTRSKNSLKEVVAESLNNTSIKDFccgassSVSRKHVLIMDE 709
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELA------EKAKPGVLFIDE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2006366332 710 VDGMAGNEDRGGIQEL----IGLIRHTKIPIICMCNDRNHPKMRSLVHYCLDLRF 760
Cdd:cd00009 93 IDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
637-766 |
1.04e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 637 LLSGPPGVGKTTTAALVCKEL---GYSYVELNASDTRSKNSLKEVVAESLNNTS-------IKDFCCGASSSVSRkhVLI 706
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgelrLRLALALARKLKPD--VLI 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 707 MDEVDGMAGNEDRGGIQE------LIGLIRHTKIPIICMCNDRNHPKMRSLVHyCLDLRFQRPRLE 766
Cdd:smart00382 84 LDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
510-875 |
1.65e-08 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129690 [Multi-domain] Cd Length: 637 Bit Score: 58.81 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 510 PFKREANNKKYkSTPEKGDTVRSvkkeTTAVRK----LTDFKRQTVEEKEASKPKGNLVSEVNEDGTErlLWVDKYKPvs 585
Cdd:TIGR00602 10 SFDDFLLSSLI-STITKWSLSRP----TSSHRRknspSTDIHARKRGFLSLEQDTGLELSSENLDGNE--PWVEKYKP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 586 lkaiiGQQGEQSCANKLLRWLRNWHKNTLEDGQAKpsktgskddgtgfKAALLSGPPGVGKTTTAALVCKELGYSYVE-L 664
Cdd:TIGR00602 81 -----ETQHELAVHKKKIEEVETWLKAQVLENAPK-------------RILLITGPSGCGKSTTIKILSKELGIQVQEwS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 665 NASDTRS-KNSLKEVVA--ESLNN-----TSIKDFCCGASSSV--------SRKHVLIMDEVDGMAgNEDRGGIQELI-- 726
Cdd:TIGR00602 143 NPTLPDFqKNDHKVTLSleSCFSNfqsqiEVFSEFLLRATNKLqmlgddlmTDKKIILVEDLPNQF-YRDTRALHEILrw 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 727 GLIRHTKIPII-----CMCNDRNHPKMR-SLVHYCLDLRFQRPRLEQIK------GAMM----SIAFKEGLKIPP----P 786
Cdd:TIGR00602 222 KYVSIGRCPLVfiiteSLEGDNNQRRLLfPAETIMNKEILEEPRVSNISfnpiapTIMKkflnRIVTIEAKKNGEkikvP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 787 AMQEIILAANQ---DIRQVLHNLNMWCAKDKSLTYDE---AKTDASRAKKDIKLGPF-----DVVRKVFATGEEA----- 850
Cdd:TIGR00602 302 KKTSVELLCQGcsgDIRSAINSLQFSSSKSGSLPIKKrmsTKSDAHASKSKIKGKHSsnnenQEIQALGGKDVSLflfra 381
|
410 420
....*....|....*....|....*.
gi 2006366332 851 -ARMSLIDKSDLFFHDYSLAPLFVQE 875
Cdd:TIGR00602 382 lGKILYCKRATLNELDSPRLPSHLSE 407
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
634-721 |
2.30e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 54.53 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 634 KAALLSGPPGVGKTTTAALVCKELGYSYVELNASDTRSK------NSLKEVV--AESLNNTsikdfccgasssvsrkhVL 705
Cdd:COG0464 192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFdkARGLAPC-----------------VL 254
|
90
....*....|....*.
gi 2006366332 706 IMDEVDGMAGNEDRGG 721
Cdd:COG0464 255 FIDEADALAGKRGEVG 270
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
469-651 |
4.65e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 43.48 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 469 IRTMPGKKSKYELAA-----EAEAKKVEPKPKKTPQKAEAGKRNFSPFKREANnKKYKSTPEKGDTVRSVKKETTAVRKL 543
Cdd:TIGR03499 34 VRKGLFGKKFVEVTAaideeEAAAASAEEEASKALEQADPKPLSATAEPLELP-APQEEPAAPAAQAAEPLLPEEELRKE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 544 TDFKRQTVEEKEASKPKGNLvSEVNEDGTERLLWVDkYKPVSLKAIIGQQGEQSCANKLLRWLRNWHKNTLedgqakPSK 623
Cdd:TIGR03499 113 LEALRELLERLLAGLAWLQR-PPERAKLYERLLEAG-VSEELARELLEKLPEDADAEDAWRWLREALEGML------PVK 184
|
170 180
....*....|....*....|....*...
gi 2006366332 624 TGSKDDGTGFKAALLSGPPGVGKTTTAA 651
Cdd:TIGR03499 185 PEEDPILEQGGVIALVGPTGVGKTTTLA 212
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-373 |
5.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 183 VQRSEKKLVASKRKEPSESRDSTLDDEAIARQLQLEEDSELERQLHEDEEFARTLAMLDETPRKKKARRDAEGEQTVLST 262
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 263 TSSPNSTAGYKQSETVKATNSAGTARNYSAKPQTKSEQLKGSHLspqssdgKKEEiaEKERGAQNSLSREKAASGKEEKT 342
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-------KKAE--EDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190
....*....|....*....|....*....|.
gi 2006366332 343 PpKKEKVSPKKSESISPEDSEKKRNNYQAYR 373
Cdd:PTZ00121 1708 K-KKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
903-1055 |
7.54e-79 |
|
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor C, RFC1. RFC complexes hydrolyse ATP and load sliding clamps such as PCNA (proliferating cell nuclear antigen) onto double-stranded DNA. RFC1 is essential for RFC function in vivo.
Pssm-ID: 462507 Cd Length: 158 Bit Score: 255.20 E-value: 7.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 903 ICDGDIVDRQIRSKQNWNLLPTQAIYASVLPGELMRGYMSQFPVFPSWLGKFSSTGKHDRIIQELAMHMSLRTQTCKRTV 982
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006366332 983 NMEYLSYLRDALVQPLKDFGADGVQQAIACMDSYCLMKEDVENIMEISTWG----GKPSPFSKLDPKVKAAFTRAYN 1055
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYN 157
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
574-991 |
1.04e-55 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 201.69 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 574 RLLWVDKYKPVSLKAIIGQQGEQscaNKLLRWLRNWhkntlEDGQAKpsktgskddgtgfKAALLSGPPGVGKTTTAALV 653
Cdd:PRK04195 1 MMPWVEKYRPKTLSDVVGNEKAK---EQLREWIESW-----LKGKPK-------------KALLLYGPPGVGKTSLAHAL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 654 CKELGYSYVELNASDTRSKNSLKEVVAESLNNTSIkdfccgassSVSRKHVLIMDEVDGMAGNEDRGGIQELIGLIRHTK 733
Cdd:PRK04195 60 ANDYGWEVIELNASDQRTADVIERVAGEAATSGSL---------FGARRKLILLDEVDGIHGNEDRGGARAILELIKKAK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 734 IPIICMCNDRNHPKMRSLVHYCLDLRFQRPRLEQIKGAMMSIAFKEGLKIPPPAMQEIILAANQDIRQVLHNLNMWCAKD 813
Cdd:PRK04195 131 QPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAEGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 814 KSLTYDEAKTDASRakkDIKLGPFDVVRKVFAT--GEEA--ARMSLIDKSDLFFHdyslaplFVQEN--YVHVKPAAagg 887
Cdd:PRK04195 211 GKLTLEDVKTLGRR---DREESIFDALDAVFKArnADQAleASYDVDEDPDDLIE-------WIDENipKEYDDPED--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 888 nlkkhlvlLSKAADSICDGDIVDRQIRSKQNWNLLPtqaiYASvlpgELM------------RG---YMsqfpvFPSWLG 952
Cdd:PRK04195 278 --------IARAYDALSRADIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGftrYQ-----PPSYWR 336
|
410 420 430
....*....|....*....|....*....|....*....
gi 2006366332 953 KFSSTGKHDRIIQELAMHMSLRTQTCKRTVNMEYLSYLR 991
Cdd:PRK04195 337 LLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
392-470 |
4.08e-48 |
|
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349383 [Multi-domain] Cd Length: 79 Bit Score: 165.46 E-value: 4.08e-48
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006366332 392 GAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSKCEKASTLGTKIIDEDGLFDLIR 470
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
388-469 |
2.08e-26 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 116.28 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 388 EIPQGAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGqSKCEKASTLGTKIIDEDGLFD 467
Cdd:COG0272 587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665
|
..
gi 2006366332 468 LI 469
Cdd:COG0272 666 LL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
382-469 |
8.59e-24 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 107.90 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 382 KALGSKEIPQGAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGqSKCEKASTLGTKIID 461
Cdd:PRK07956 576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654
|
....*...
gi 2006366332 462 EDGLFDLI 469
Cdd:PRK07956 655 EEEFLRLL 662
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
397-468 |
1.16e-23 |
|
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349379 [Multi-domain] Cd Length: 76 Bit Score: 95.63 E-value: 1.16e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 397 LEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSK----CEKASTLGTKIIDEDGLFDL 468
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLkkgeELKAKGLGIKIISEEEFLDL 76
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
637-742 |
7.48e-16 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 75.32 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 637 LLSGPPGVGKTTTAALVCKELGYSYVELNASDTRSKnslkeVVAESLNNtsIKDFCCGASSsvSRKHVLIMDEVDGMAGN 716
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEAAKK--LAPCVIFIDEIDALAGS 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 2006366332 717 EDRGGIQELIGLI------------RHTKIPIICMCND 742
Cdd:pfam00004 73 RGSGGDSESRRVVnqllteldgftsSNSKVIVIAATNR 110
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
394-469 |
3.26e-15 |
|
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.
Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 71.56 E-value: 3.26e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 394 ENCLEGLTFVITGvLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMgrDCGQSKCEKASTLGTKIIDEDGLFDLI 469
Cdd:pfam00533 3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
394-469 |
3.77e-15 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 71.25 E-value: 3.77e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006366332 394 ENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSKCE--KASTLGTKIIDEDGLFDLI 469
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDCL 78
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
633-760 |
6.19e-15 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 73.33 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 633 FKAALLSGPPGVGKTTTAALVCKEL---GYSYVELNASDTRSKNSLKEVVAESLNNTSIKDFccgassSVSRKHVLIMDE 709
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELA------EKAKPGVLFIDE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2006366332 710 VDGMAGNEDRGGIQEL----IGLIRHTKIPIICMCNDRNHPKMRSLVHYCLDLRF 760
Cdd:cd00009 93 IDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
390-463 |
8.77e-15 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 79.03 E-value: 8.77e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006366332 390 PQGAE----NCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSKCEKASTLGTKIIDED 463
Cdd:PRK14351 599 PQPAEseggDALDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVGENPGQSKRDDAEANDVPTLDEE 676
|
|
| PLN03025 |
PLN03025 |
replication factor C subunit; Provisional |
577-806 |
4.81e-11 |
|
replication factor C subunit; Provisional
Pssm-ID: 178596 [Multi-domain] Cd Length: 319 Bit Score: 65.52 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 577 WVDKYKPVSLKAIIGQQgeqscankllrwlrnwhkNTLEDGQAKPSktgskddgTGFKAAL-LSGPPGVGKTTTA-ALVC 654
Cdd:PLN03025 3 WVEKYRPTKLDDIVGNE------------------DAVSRLQVIAR--------DGNMPNLiLSGPPGTGKTTSIlALAH 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 655 KELGYSY----VELNASDTRSknslKEVVaeslnNTSIKDFccgASSSVS----RKHVLIMDEVDGMAGnedrGGIQELI 726
Cdd:PLN03025 57 ELLGPNYkeavLELNASDDRG----IDVV-----RNKIKMF---AQKKVTlppgRHKIVILDEADSMTS----GAQQALR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 727 GLIR----HTKIPIICMCNDRNHPKMRSlvhYCLDLRFQRPRLEQIKGAMMSIAFKEGLKIPPPAMQEIILAANQDIRQV 802
Cdd:PLN03025 121 RTMEiysnTTRFALACNTSSKIIEPIQS---RCAIVRFSRLSDQEILGRLMKVVEAEKVPYVPEGLEAIIFTADGDMRQA 197
|
....
gi 2006366332 803 LHNL 806
Cdd:PLN03025 198 LNNL 201
|
|
| HLD_clamp_RFC |
cd18140 |
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ... |
763-819 |
3.70e-10 |
|
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein clamp loader complex that forms a stable ATP-dependent complex with the sliding clamp, PCNA, which binds specifically to primed DNA. RFC subunits belong to the clamp loader clade of the AAA+ superfamily.
Pssm-ID: 350842 [Multi-domain] Cd Length: 63 Bit Score: 56.77 E-value: 3.70e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006366332 763 PRLEQIKGAMMSIAFKEGLKIPPPAMQEIILAANQDIRQVLHNLNMWCAKDKSLTYD 819
Cdd:cd18140 1 LSKEQIVKRLREICKKEGVKIDEEALEAIAEKSEGDMRKAINDLQAAAAGGGVITEE 57
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
579-710 |
4.76e-09 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 59.71 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 579 DKYKPVSLKAIIGQQ---GEqscaNKLLRwlrnwhkNTLEDGQAkPSktgskddgtgfkaALLSGPPGVGKTTTAALVCK 655
Cdd:PRK13342 4 ERMRPKTLDEVVGQEhllGP----GKPLR-------RMIEAGRL-SS-------------MILWGPPGTGKTTLARIIAG 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2006366332 656 ELGYSYVELNASDTrSKNSLKEVVAESLNNTSIkdfccgasssvSRKHVLIMDEV 710
Cdd:PRK13342 59 ATDAPFEALSAVTS-GVKDLREVIEEARQRRSA-----------GRRTILFIDEI 101
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
400-467 |
6.58e-09 |
|
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.
Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 53.52 E-value: 6.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006366332 400 LTFVITGvLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQSKCEKASTLGTKIIDEDGLFD 467
Cdd:cd00027 1 LVICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLD 67
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
573-713 |
7.54e-09 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 58.73 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 573 ERLLWVDKYKPVSLKAIIGQQgeqSCANKLLRWLRNwhKNTledgqakPSktgskddgtgfkaALLSGPPGVGKTTTAAL 652
Cdd:PRK00440 3 MEEIWVEKYRPRTLDEIVGQE---EIVERLKSYVKE--KNM-------PH-------------LLFAGPPGTGKTTAALA 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 653 VCKEL-GYSY----VELNASDTRSKNslkeVVaeslnNTSIKDFCCGASSSVSRKHVLIMDEVDGM 713
Cdd:PRK00440 58 LARELyGEDWrenfLELNASDERGID----VI-----RNKIKEFARTAPVGGAPFKIIFLDEADNL 114
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
637-766 |
1.04e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 637 LLSGPPGVGKTTTAALVCKEL---GYSYVELNASDTRSKNSLKEVVAESLNNTS-------IKDFCCGASSSVSRkhVLI 706
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgelrLRLALALARKLKPD--VLI 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 707 MDEVDGMAGNEDRGGIQE------LIGLIRHTKIPIICMCNDRNHPKMRSLVHyCLDLRFQRPRLE 766
Cdd:smart00382 84 LDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
510-875 |
1.65e-08 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129690 [Multi-domain] Cd Length: 637 Bit Score: 58.81 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 510 PFKREANNKKYkSTPEKGDTVRSvkkeTTAVRK----LTDFKRQTVEEKEASKPKGNLVSEVNEDGTErlLWVDKYKPvs 585
Cdd:TIGR00602 10 SFDDFLLSSLI-STITKWSLSRP----TSSHRRknspSTDIHARKRGFLSLEQDTGLELSSENLDGNE--PWVEKYKP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 586 lkaiiGQQGEQSCANKLLRWLRNWHKNTLEDGQAKpsktgskddgtgfKAALLSGPPGVGKTTTAALVCKELGYSYVE-L 664
Cdd:TIGR00602 81 -----ETQHELAVHKKKIEEVETWLKAQVLENAPK-------------RILLITGPSGCGKSTTIKILSKELGIQVQEwS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 665 NASDTRS-KNSLKEVVA--ESLNN-----TSIKDFCCGASSSV--------SRKHVLIMDEVDGMAgNEDRGGIQELI-- 726
Cdd:TIGR00602 143 NPTLPDFqKNDHKVTLSleSCFSNfqsqiEVFSEFLLRATNKLqmlgddlmTDKKIILVEDLPNQF-YRDTRALHEILrw 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 727 GLIRHTKIPII-----CMCNDRNHPKMR-SLVHYCLDLRFQRPRLEQIK------GAMM----SIAFKEGLKIPP----P 786
Cdd:TIGR00602 222 KYVSIGRCPLVfiiteSLEGDNNQRRLLfPAETIMNKEILEEPRVSNISfnpiapTIMKkflnRIVTIEAKKNGEkikvP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 787 AMQEIILAANQ---DIRQVLHNLNMWCAKDKSLTYDE---AKTDASRAKKDIKLGPF-----DVVRKVFATGEEA----- 850
Cdd:TIGR00602 302 KKTSVELLCQGcsgDIRSAINSLQFSSSKSGSLPIKKrmsTKSDAHASKSKIKGKHSsnnenQEIQALGGKDVSLflfra 381
|
410 420
....*....|....*....|....*.
gi 2006366332 851 -ARMSLIDKSDLFFHDYSLAPLFVQE 875
Cdd:TIGR00602 382 lGKILYCKRATLNELDSPRLPSHLSE 407
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
575-806 |
7.65e-08 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 55.38 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 575 LLWVDKYKPVSLKAIIGQQGEqscankllrwlRNWHKNTLEDGQAkPSKTgskddgtgfkaaLLSGPPGVGKTTTAALVC 654
Cdd:PHA02544 9 FMWEQKYRPSTIDECILPAAD-----------KETFKSIVKKGRI-PNML------------LHSPSPGTGKTTVAKALC 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 655 KELGYSYVELNASDTRSknslkEVVaeslnNTSIKDFCCGASSSVSRKhVLIMDEVD--GMAGNED--RGGIQELiglir 730
Cdd:PHA02544 65 NEVGAEVLFVNGSDCRI-----DFV-----RNRLTRFASTVSLTGGGK-VIIIDEFDrlGLADAQRhlRSFMEAY----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 731 HTKIPIICMCNDRN--HPKMRSlvhYCLDLRFQRP-RLEQI--KGAM----MSIAFKEGLKIPPPAMQEIILAANQDIRQ 801
Cdd:PHA02544 129 SKNCSFIITANNKNgiIEPLRS---RCRVIDFGVPtKEEQIemMKQMivrcKGILEAEGVEVDMKVLAALVKKNFPDFRR 205
|
....*
gi 2006366332 802 VLHNL 806
Cdd:PHA02544 206 TINEL 210
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
634-768 |
9.39e-08 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 52.67 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 634 KAALLSGPPGVGKTTTAALVCKELGYSYVELNASDTRSKnSLKEVVAEsLNNTsikdFccgassSVSRKH---VLIMDEV 710
Cdd:cd19481 27 KGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN-LRKI----F------ERARRLapcILFIDEI 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006366332 711 DGMAGNEDRGG------------IQELIGLIRHTKIPIICMCndrNHPKMrslvhycLDLRFQRP-RLEQI 768
Cdd:cd19481 95 DAIGRKRDSSGesgelrrvlnqlLTELDGVNSRSKVLVIAAT---NRPDL-------LDPALLRPgRFDEV 155
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
634-721 |
2.30e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 54.53 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 634 KAALLSGPPGVGKTTTAALVCKELGYSYVELNASDTRSK------NSLKEVV--AESLNNTsikdfccgasssvsrkhVL 705
Cdd:COG0464 192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFdkARGLAPC-----------------VL 254
|
90
....*....|....*.
gi 2006366332 706 IMDEVDGMAGNEDRGG 721
Cdd:COG0464 255 FIDEADALAGKRGEVG 270
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
635-840 |
2.75e-07 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 53.44 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 635 AALLSGPPGVGKTTTAALVCKELGYS-----------------------YVELNA---SDTRSKNSLKEVVaESLNNTSI 688
Cdd:COG0470 20 ALLLHGPPGIGKTTLALALARDLLCEnpeggkacgqchsrlmaagnhpdLLELNPeekSDQIGIDQIRELG-EFLSLTPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 689 kdfccgasssVSRKHVLIMDEVDGMAGNEDRGGIQELIGLIRHTkiPIICMCNDRNH--PKMRSLvhyCLDLRFQRPRLE 766
Cdd:COG0470 99 ----------EGGRKVVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---CQVIRFRPPSEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 767 QIKGAMmsiafkEGLKIPPPAMQEIILAANQDIRQVLHNLNMWCAKD-------KSLTYDEAKTDASRAKKDIKLGPFDV 839
Cdd:COG0470 164 EALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQALAGRKelledlaALLSRDRALELLDALLKAEALELLDW 237
|
.
gi 2006366332 840 V 840
Cdd:COG0470 238 L 238
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
397-470 |
2.88e-07 |
|
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.
Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 49.08 E-value: 2.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006366332 397 LEGLTFVITGvLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDCGQsKCEKASTLGT-KIIDEDGLFDLIR 470
Cdd:cd17731 3 FKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQ-KYEFARKWNSiHIVTPEWLYDSIE 75
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
397-469 |
9.78e-07 |
|
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.
Pssm-ID: 349378 [Multi-domain] Cd Length: 76 Bit Score: 47.52 E-value: 9.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 397 LEGLTFVITGVLEcIERDEAKSLIERYGGKVTGNVSKKTNYLV---MGRDCGQSKCEKASTLGTKIIDEDGLFDLI 469
Cdd:cd17747 1 LTGMKFALIGKLS-KSKDELKKLIEKLGGKVASKVTKKVTLCIstkAEVEKMSKKMKEAKEAGVPVVSEDFLEDCI 75
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
372-470 |
2.01e-06 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 50.93 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 372 YRSFLNREGPKAlgsKEIPQGAENCLEGLTFVITGVLECIERDEAKSLIERYGGKVTGNVSKKTNYLVMG--------RD 443
Cdd:PRK06195 199 KRSNRQAPRKKK---KIIESFGFTAFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnRE 275
|
90 100 110
....*....|....*....|....*....|..
gi 2006366332 444 CGQSKCEKASTL-----GTKIIDEDGLFDLIR 470
Cdd:PRK06195 276 EMSNKLKKAIDLkkkgqNIKFLNEEEFLQKCK 307
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
583-710 |
1.19e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 49.28 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 583 PVSLKAIIGQQ---GEqscaNKLLRwlrnwhkNTLEDGQAkPSktgskddgtgfkaALLSGPPGVGKTTTAALVCKELGY 659
Cdd:COG2256 21 PRTLDEVVGQEhllGP----GKPLR-------RAIEAGRL-SS-------------MILWGPPGTGKTTLARLIANATDA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2006366332 660 SYVELNASDTrSKNSLKEVVAESLNNTSIkdfccgasssvSRKHVLIMDEV 710
Cdd:COG2256 76 EFVALSAVTS-GVKDIREVIEEARERRAY-----------GRRTILFVDEI 114
|
|
| PRK04132 |
PRK04132 |
replication factor C small subunit; Provisional |
642-833 |
1.37e-05 |
|
replication factor C small subunit; Provisional
Pssm-ID: 235223 [Multi-domain] Cd Length: 846 Bit Score: 49.45 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 642 PGVGKTTTAAL-VCKEL-----GYSYVELNASDTRSKNSLKEVVAESLNNTSIKDfccgasssVSRKhVLIMDEVDGM-- 713
Cdd:PRK04132 574 PTVLHNTTAALaLARELfgenwRHNFLELNASDERGINVIREKVKEFARTKPIGG--------ASFK-IIFLDEADALtq 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 714 -AGNEDRGGIQELIGLIRhtkipIICMCN--DRNHPKMRSlvhYCLDLRFQRPRLEQIKGAMMSIAFKEGLKIPPPAMQE 790
Cdd:PRK04132 645 dAQQALRRTMEMFSSNVR-----FILSCNysSKIIEPIQS---RCAIFRFRPLRDEDIAKRLRYIAENEGLELTEEGLQA 716
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2006366332 791 IILAANQDIRQVLHNLNMWCAKDKSLTYDEAKTDASRAK-KDIK 833
Cdd:PRK04132 717 ILYIAEGDMRRAINILQAAAALDDKITDENVFLVASRARpEDIR 760
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
637-770 |
1.74e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 44.49 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 637 LLSGPPGVGKTTTAALVCKELGYSYVELNASdtrsknslkEVVAESLNNTSIK-----DFCCgasssvSRKHVLIMDEVD 711
Cdd:COG1223 39 LFYGPPGTGKTMLAEALAGELKLPLLTVRLD---------SLIGSYLGETARNlrklfDFAR------RAPCVIFFDEFD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006366332 712 GMAG----NEDRGGIQELIGLI------RHTKIPIICMCndrNHPKMrslvhycLD----------LRFQRPRLEQIKG 770
Cdd:COG1223 104 AIAKdrgdQNDVGEVKRVVNALlqeldgLPSGSVVIAAT---NHPEL-------LDsalwrrfdevIEFPLPDKEERKE 172
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
567-671 |
2.62e-04 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 43.41 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 567 VNEDGTErlLWVDKYKPvslkaiiGQQGEQSCANKLLRWLRNWHKNTLEDGQAKpsktgskddgtgfKAALLSGPPGVGK 646
Cdd:pfam03215 1 INDDGGE--QWYEKYKP-------NCLEQLAVHKRKIKDVQEWLDAMFLENAKH-------------RILLISGPSGCGK 58
|
90 100
....*....|....*....|....*.
gi 2006366332 647 TTTAALVCKELGYSYVE-LNASDTRS 671
Cdd:pfam03215 59 STVIKELSKELGPKYREwSNPTSFRS 84
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
469-651 |
4.65e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 43.48 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 469 IRTMPGKKSKYELAA-----EAEAKKVEPKPKKTPQKAEAGKRNFSPFKREANnKKYKSTPEKGDTVRSVKKETTAVRKL 543
Cdd:TIGR03499 34 VRKGLFGKKFVEVTAaideeEAAAASAEEEASKALEQADPKPLSATAEPLELP-APQEEPAAPAAQAAEPLLPEEELRKE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 544 TDFKRQTVEEKEASKPKGNLvSEVNEDGTERLLWVDkYKPVSLKAIIGQQGEQSCANKLLRWLRNWHKNTLedgqakPSK 623
Cdd:TIGR03499 113 LEALRELLERLLAGLAWLQR-PPERAKLYERLLEAG-VSEELARELLEKLPEDADAEDAWRWLREALEGML------PVK 184
|
170 180
....*....|....*....|....*...
gi 2006366332 624 TGSKDDGTGFKAALLSGPPGVGKTTTAA 651
Cdd:TIGR03499 185 PEEDPILEQGGVIALVGPTGVGKTTTLA 212
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
636-742 |
7.10e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 43.30 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 636 ALLSGPPGVGKTTTAALVCKELGY---------SYVELNASDTRSKNS-LKEVVAESLNNTSIkdfccgASSSVSRK--- 702
Cdd:COG1474 54 VLIYGPTGTGKTAVAKYVLEELEEeaeergvdvRVVYVNCRQASTRYRvLSRILEELGSGEDI------PSTGLSTDelf 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006366332 703 -------------HVLIMDEVDGMAGNEDRGGIQELIGL---IRHTKIPIICMCND 742
Cdd:COG1474 128 drlyealderdgvLVVVLDEIDYLVDDEGDDLLYQLLRAneeLEGARVGVIGISND 183
|
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
637-665 |
1.02e-03 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 41.34 E-value: 1.02e-03
10 20
....*....|....*....|....*....
gi 2006366332 637 LLSGPPGVGKTTTAALVCKELGYSYVELN 665
Cdd:COG1936 4 AITGTPGTGKTTVAKLLAERLGLEVIHLN 32
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
638-662 |
1.15e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 40.55 E-value: 1.15e-03
10 20
....*....|....*....|....*
gi 2006366332 638 LSGPPGVGKTTTAALVCKELGYSYV 662
Cdd:cd02020 4 IDGPAGSGKSTVAKLLAKKLGLPYL 28
|
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
637-658 |
2.86e-03 |
|
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.
Pssm-ID: 398900 [Multi-domain] Cd Length: 159 Bit Score: 39.79 E-value: 2.86e-03
|
| AAA_17 |
pfam13207 |
AAA domain; |
639-668 |
3.83e-03 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 38.76 E-value: 3.83e-03
10 20 30
....*....|....*....|....*....|
gi 2006366332 639 SGPPGVGKTTTAALVCKELGYSYVelNASD 668
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGFPHI--SAGD 28
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
638-688 |
4.13e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 39.40 E-value: 4.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006366332 638 LSGPPGVGKTTTAALVCKELGYSYVelNASDT-----RSKN-SLKEVVAESLNNTSI 688
Cdd:PRK04182 5 ISGPPGSGKTTVARLLAEKLGLKHV--SAGEIfrelaKERGmSLEEFNKYAEEDPEI 59
|
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
637-658 |
4.75e-03 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 40.50 E-value: 4.75e-03
|
| RuvB |
COG2255 |
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ... |
637-658 |
4.90e-03 |
|
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];
Pssm-ID: 441856 [Multi-domain] Cd Length: 337 Bit Score: 40.45 E-value: 4.90e-03
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-373 |
5.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 183 VQRSEKKLVASKRKEPSESRDSTLDDEAIARQLQLEEDSELERQLHEDEEFARTLAMLDETPRKKKARRDAEGEQTVLST 262
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 263 TSSPNSTAGYKQSETVKATNSAGTARNYSAKPQTKSEQLKGSHLspqssdgKKEEiaEKERGAQNSLSREKAASGKEEKT 342
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-------KKAE--EDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190
....*....|....*....|....*....|.
gi 2006366332 343 PpKKEKVSPKKSESISPEDSEKKRNNYQAYR 373
Cdd:PTZ00121 1708 K-KKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| PRK14970 |
PRK14970 |
DNA polymerase III subunits gamma and tau; Provisional |
580-803 |
7.65e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184934 [Multi-domain] Cd Length: 367 Bit Score: 39.86 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 580 KYKPVSLKAIIGQQGeqscankllrwLRNWHKNTLEDGQAKpsktgskddgtgfKAALLSGPPGVGKTTTAALVCKEL-- 657
Cdd:PRK14970 10 KYRPQTFDDVVGQSH-----------ITNTLLNAIENNHLA-------------QALLFCGPRGVGKTTCARILARKInq 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 658 -GYSYVELNAS------DTRSKNSLKEVvAESLNNTSIkdfccgaSSSVSRKHVLIMDEVDGMAGNEDRGGIQELIGLIR 730
Cdd:PRK14970 66 pGYDDPNEDFSfnifelDAASNNSVDDI-RNLIDQVRI-------PPQTGKYKIYIIDEVHMLSSAAFNAFLKTLEEPPA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006366332 731 HTkipIICMCNDRNHPKMRSLVHYCLDLRFQRPRLEQIKGAMMSIAFKEGLKIPPPAMQEIILAANQDIRQVL 803
Cdd:PRK14970 138 HA---IFILATTEKHKIIPTILSRCQIFDFKRITIKDIKEHLAGIAVKEGIKFEDDALHIIAQKADGALRDAL 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-570 |
7.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 193 SKRKEPSESRDSTLDDEAIARQLQLEEDSELERQLHEDE--EFARTLAMLD-ETPRKKKARRDAEGEQTVLSTTSSPNST 269
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARmaHFARRQAAIKaEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 270 AGYKQSETVKATNSAGTARNYSAKPQTKSEQLKG-SHLSPQSSDGKKEEIAEKERGAQNSLSREKAASGKEEKTPPKKEK 348
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 349 VSPKKSESISPEDSEKKRNNYQAYRSFLNREGPKALGSKEIPQGAENCLEGLTfVITGVLECIERDEAKSLIERygGKVT 428
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAKKADEAKKKAEE--AKKA 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006366332 429 GNVSKKTNYLVMGRDCGQSKCE--KASTLGTKIIDEDGLFDLIRTMPGKKSKYELAAEAEAKKVEPKPKKTPQKAEAGKR 506
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006366332 507 NFSPFKREANNKKYKSTPEKGDTVRSVKKETTAVRKLTDFKRQTVEEKEASKPKGNLVSEVNED 570
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
637-658 |
8.60e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 39.59 E-value: 8.60e-03
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
634-672 |
9.19e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 39.60 E-value: 9.19e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2006366332 634 KAALLSGPPGVGKTTTAALVCKELGYSYVELNASDTRSK 672
Cdd:COG1222 113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151
|
|
| |
