|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
888-1041 |
4.60e-78 |
|
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: 252.88 E-value: 4.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 888 ICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMRGYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTV 967
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249180 968 NMDYLSLLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWG----GKPSPFSKLDPKVKAAFTRAYNK 1041
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
558-976 |
7.13e-52 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 190.52 E-value: 7.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 558 LLWVDKYKPTSLKTIIGQQgdqSCANKLLRWLRNWQKsssedkkhakfgkfsgkddGSSFKAALLSGPPGVGKTTTASLV 637
Cdd:PRK04195 2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLK-------------------GKPKKALLLYGPPGVGKTSLAHAL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 638 CQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFysngaassvstKHALI-MDEVDGMAGNEDRGGIQELIGLIKH 716
Cdd:PRK04195 60 ANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA-----------RRKLIlLDEVDGIHGNEDRGGARAILELIKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 717 TKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCA 796
Cdd:PRK04195 129 AKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 797 RSKALTYDQAKAdshRAKKDIKMGPFDVARKVFA---AGEETAHMSLVDKS-DLFFHdysiaplFVQEN----YIHVKPV 868
Cdd:PRK04195 209 GYGKLTLEDVKT---LGRRDREESIFDALDAVFKarnADQALEASYDVDEDpDDLIE-------WIDENipkeYDDPEDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 869 AAGGDMkkhlmlLSRAadsicdgDLVDSQIRSKQNWSLLPaqaiYASvlpgELM------------RGYmTQFpTFPSWL 936
Cdd:PRK04195 279 ARAYDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGF-TRY-QPPSYW 335
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1390249180 937 GKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLSLLR 976
Cdd:PRK04195 336 RLLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
376-454 |
5.43e-46 |
|
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: 159.30 E-value: 5.43e-46
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249180 376 GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIR 454
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
372-453 |
9.34e-28 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 120.51 E-value: 9.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 372 EIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIIDEDGLLN 451
Cdd:COG0272 587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665
|
..
gi 1390249180 452 LI 453
Cdd:COG0272 666 LL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
366-453 |
1.45e-25 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 113.68 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 366 KALGSKEIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIID 445
Cdd:PRK07956 576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654
|
....*...
gi 1390249180 446 EDGLLNLI 453
Cdd:PRK07956 655 EEEFLRLL 662
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
621-749 |
5.41e-17 |
|
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: 78.40 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 621 LLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKsslkaIVAESLNNtsIKGFYSNgaASSVStKHALIMDEVDGMAG 700
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEA--AKKLA-PCVIFIDEIDALAG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249180 701 NEDRGGIQELIGLI------------KHTKIPIICMCNdrNHPKIRSLVHYCFDLRFQRPR 749
Cdd:pfam00004 72 SRGSGGDSESRRVVnqllteldgftsSNSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
378-453 |
5.21e-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: 70.79 E-value: 5.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249180 378 ENCLEGLIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMgrDSGQSKSDKAAALGTKIIDEDGLLNLI 453
Cdd:pfam00533 3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
616-745 |
2.95e-14 |
|
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: 71.41 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 616 SFKAALLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSksslKAIVAESLNNTSIKGFYSNGAASSVSTkhaLIM 692
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLE----GLVVAELFGHFLVRLLFELAEKAKPGV---LFI 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249180 693 DEVDGMAGNEDRGGIQEL----IGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRF 745
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
378-453 |
2.67e-13 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 66.24 E-value: 2.67e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249180 378 ENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAA--LGTKIIDEDGLLNLI 453
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAiaLGIPIVKEEWLLDCL 78
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
621-751 |
6.91e-09 |
|
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: 55.84 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 621 LLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFYSNGA-----ASSVSTKhALIM 692
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalARKLKPD-VLIL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249180 693 DEVDGMAGNEDRGGIQE------LIGLIKHTKIPIICMCNDRNHPKIRSLVHyCFDLRFQRPRVE 751
Cdd:smart00382 85 DEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
618-706 |
2.99e-06 |
|
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: 51.07 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 618 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK------SSLKAIVAESLnntsikgfysnGAASSVstkhaLI 691
Cdd:COG0464 192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFDKAR-----------GLAPCV-----LF 255
|
90
....*....|....*
gi 1390249180 692 MDEVDGMAGNEDRGG 706
Cdd:COG0464 256 IDEADALAGKRGEVG 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-378 |
3.04e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 14 KKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLP--- 90
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkka 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 91 --VSSKPGKISRQDPVTYISETDEEDDFMCKKA--ASKSKENGRSTNSHLGTSNMKKNEENTKTKNKplSPIKLTPTSVL 166
Cdd:PTZ00121 1408 deLKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 167 DYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEAiAKQLQLDEDAEARKDTEAGETFSSVQAN-LSKAE---KHKYPH 242
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEAKKAEEKKKADeLKKAEelkKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 243 KVKTAQVSDERKSYSPRKQS-----------------KYESSKESQQHSKSSADKIGEVSSPKASS---KLAIMKRKEES 302
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEeakkaeearieevmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKVEQLKKKEAE 1644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249180 303 SYKEIEPVASKRKENAIKLKGETKTPKKTKSspaKKESVSPEDSEKKRTNYQayrsyLNREGPKALGSKEIPKGAE 378
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEA-----LKKEAEEAKKAEELKKKEA 1712
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
511-647 |
1.75e-05 |
|
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: 48.80 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 511 SLAKTIKKETDVFWKSLDFKEQVAEETSGDSKARNLADD-------SSENKVENLLWVDKYKPTSlktiigqQGDQSCAN 583
Cdd:TIGR00602 18 SLISTITKWSLSRPTSSHRRKNSPSTDIHARKRGFLSLEqdtglelSSENLDGNEPWVEKYKPET-------QHELAVHK 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249180 584 KLLRWLRNWQKSSS-EDKKHakfgkfsgkddgssfKAALLSGPPGVGKTTTASLVCQELGYSYVE 647
Cdd:TIGR00602 91 KKIEEVETWLKAQVlENAPK---------------RILLITGPSGCGKSTTIKILSKELGIQVQE 140
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
888-1041 |
4.60e-78 |
|
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: 252.88 E-value: 4.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 888 ICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMRGYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTV 967
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249180 968 NMDYLSLLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWG----GKPSPFSKLDPKVKAAFTRAYNK 1041
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
558-976 |
7.13e-52 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 190.52 E-value: 7.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 558 LLWVDKYKPTSLKTIIGQQgdqSCANKLLRWLRNWQKsssedkkhakfgkfsgkddGSSFKAALLSGPPGVGKTTTASLV 637
Cdd:PRK04195 2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLK-------------------GKPKKALLLYGPPGVGKTSLAHAL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 638 CQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFysngaassvstKHALI-MDEVDGMAGNEDRGGIQELIGLIKH 716
Cdd:PRK04195 60 ANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA-----------RRKLIlLDEVDGIHGNEDRGGARAILELIKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 717 TKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCA 796
Cdd:PRK04195 129 AKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 797 RSKALTYDQAKAdshRAKKDIKMGPFDVARKVFA---AGEETAHMSLVDKS-DLFFHdysiaplFVQEN----YIHVKPV 868
Cdd:PRK04195 209 GYGKLTLEDVKT---LGRRDREESIFDALDAVFKarnADQALEASYDVDEDpDDLIE-------WIDENipkeYDDPEDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 869 AAGGDMkkhlmlLSRAadsicdgDLVDSQIRSKQNWSLLPaqaiYASvlpgELM------------RGYmTQFpTFPSWL 936
Cdd:PRK04195 279 ARAYDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGF-TRY-QPPSYW 335
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1390249180 937 GKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLSLLR 976
Cdd:PRK04195 336 RLLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
376-454 |
5.43e-46 |
|
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: 159.30 E-value: 5.43e-46
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249180 376 GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIR 454
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
372-453 |
9.34e-28 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 120.51 E-value: 9.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 372 EIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIIDEDGLLN 451
Cdd:COG0272 587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665
|
..
gi 1390249180 452 LI 453
Cdd:COG0272 666 LL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
366-453 |
1.45e-25 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 113.68 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 366 KALGSKEIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIID 445
Cdd:PRK07956 576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654
|
....*...
gi 1390249180 446 EDGLLNLI 453
Cdd:PRK07956 655 EEEFLRLL 662
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
381-452 |
5.63e-24 |
|
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: 96.40 E-value: 5.63e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249180 381 LEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSD----KAAALGTKIIDEDGLLNL 452
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKKgeelKAKGLGIKIISEEEFLDL 76
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
621-749 |
5.41e-17 |
|
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: 78.40 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 621 LLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKsslkaIVAESLNNtsIKGFYSNgaASSVStKHALIMDEVDGMAG 700
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEA--AKKLA-PCVIFIDEIDALAG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249180 701 NEDRGGIQELIGLI------------KHTKIPIICMCNdrNHPKIRSLVHYCFDLRFQRPR 749
Cdd:pfam00004 72 SRGSGGDSESRRVVnqllteldgftsSNSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
378-453 |
5.21e-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: 70.79 E-value: 5.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249180 378 ENCLEGLIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMgrDSGQSKSDKAAALGTKIIDEDGLLNLI 453
Cdd:pfam00533 3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
616-745 |
2.95e-14 |
|
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: 71.41 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 616 SFKAALLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSksslKAIVAESLNNTSIKGFYSNGAASSVSTkhaLIM 692
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLE----GLVVAELFGHFLVRLLFELAEKAKPGV---LFI 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249180 693 DEVDGMAGNEDRGGIQEL----IGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRF 745
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
378-453 |
2.67e-13 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 66.24 E-value: 2.67e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249180 378 ENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAA--LGTKIIDEDGLLNLI 453
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAiaLGIPIVKEEWLLDCL 78
|
|
| PLN03025 |
PLN03025 |
replication factor C subunit; Provisional |
560-791 |
3.15e-11 |
|
replication factor C subunit; Provisional
Pssm-ID: 178596 [Multi-domain] Cd Length: 319 Bit Score: 65.91 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 560 WVDKYKPTSLKTIIGQQGDQSCANKLLRwlrnwqksssedkkhakfgkfsgkdDGSsFKAALLSGPPGVGKTTTA-SLVC 638
Cdd:PLN03025 3 WVEKYRPTKLDDIVGNEDAVSRLQVIAR-------------------------DGN-MPNLILSGPPGTGKTTSIlALAH 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 639 QELGYSY----VELNASDTRSKSSLKaivaeslnnTSIKGFYSNGAASSVSTKHALIMDEVDGMAGnedrGGIQELIGLI 714
Cdd:PLN03025 57 ELLGPNYkeavLELNASDDRGIDVVR---------NKIKMFAQKKVTLPPGRHKIVILDEADSMTS----GAQQALRRTM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 715 K----HTKIPIICMCNDRNHPKIRSlvhYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHN 790
Cdd:PLN03025 124 EiysnTTRFALACNTSSKIIEPIQS---RCAIVRFSRLSDQEILGRLMKVVEAEKVPYVPEGLEAIIFTADGDMRQALNN 200
|
.
gi 1390249180 791 L 791
Cdd:PLN03025 201 L 201
|
|
| HLD_clamp_RFC |
cd18140 |
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ... |
748-804 |
2.04e-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: 57.54 E-value: 2.04e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249180 748 PRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCARSKALTYD 804
Cdd:cd18140 1 LSKEQIVKRLREICKKEGVKIDEEALEAIAEKSEGDMRKAINDLQAAAAGGGVITEE 57
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
621-751 |
6.91e-09 |
|
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: 55.84 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 621 LLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFYSNGA-----ASSVSTKhALIM 692
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalARKLKPD-VLIL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249180 693 DEVDGMAGNEDRGGIQE------LIGLIKHTKIPIICMCNDRNHPKIRSLVHyCFDLRFQRPRVE 751
Cdd:smart00382 85 DEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
384-447 |
8.66e-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: 53.13 E-value: 8.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249180 384 LIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDED 447
Cdd:cd00027 1 LVICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPE 63
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
300-454 |
2.29e-08 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 57.10 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 300 EESSYKEIEPVASKRKENAIKLKGETKTPKKTKSSPAKKESvsPEDSEKKRtnyqayrsylnregpkalgsKEIPKGAEN 379
Cdd:PRK06195 162 KELNSKDINEISKLLGVTLGYVNENGYKPSSRKGRILKRSN--RQAPRKKK--------------------KIIESFGFT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 380 CLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMG--------RDSGQSKSDKAAAL-----GTKIIDE 446
Cdd:PRK06195 220 AFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnREEMSNKLKKAIDLkkkgqNIKFLNE 299
|
....*...
gi 1390249180 447 DGLLNLIR 454
Cdd:PRK06195 300 EEFLQKCK 307
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
562-671 |
1.15e-07 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 55.48 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 562 DKYKPTSLKTIIGQQ---GdqscANKLLR-WLRNWQKSSSedkkhakfgkfsgkddgssfkaaLLSGPPGVGKTTTASLV 637
Cdd:PRK13342 4 ERMRPKTLDEVVGQEhllG----PGKPLRrMIEAGRLSSM-----------------------ILWGPPGTGKTTLARII 56
|
90 100 110
....*....|....*....|....*....|....
gi 1390249180 638 CQELGYSYVELNASDTrSKSSLKAIVAESLNNTS 671
Cdd:PRK13342 57 AGATDAPFEALSAVTS-GVKDLREVIEEARQRRS 89
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
558-791 |
2.68e-07 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 53.84 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 558 LLWVDKYKPTSLKTIIGQQGDqscankllrwlrnwqksssedkkHAKFGKFSgkDDGSSFKAALLSGPPGVGKTTTASLV 637
Cdd:PHA02544 9 FMWEQKYRPSTIDECILPAAD-----------------------KETFKSIV--KKGRIPNMLLHSPSPGTGKTTVAKAL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 638 CQELGYSYVELNASDTRsksslkaivAESLNNtSIKGFysngaASSVSTK---HALIMDEVD--GMAGNED--RGGIQEL 710
Cdd:PHA02544 64 CNEVGAEVLFVNGSDCR---------IDFVRN-RLTRF-----ASTVSLTgggKVIIIDEFDrlGLADAQRhlRSFMEAY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 711 iglikHTKIPIICMCNDRN--HPKIRSlvhYCFDLRFQRP-RVEQI--KGAM----MSIAFKEGLKIPPPAMNEIILGAN 781
Cdd:PHA02544 129 -----SKNCSFIITANNKNgiIEPLRS---RCRVIDFGVPtKEEQIemMKQMivrcKGILEAEGVEVDMKVLAALVKKNF 200
|
250
....*....|
gi 1390249180 782 QDIRQVLHNL 791
Cdd:PHA02544 201 PDFRRTINEL 210
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
554-654 |
8.76e-07 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 52.18 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 554 KVENLLWVDKYKPTSLKTIIGQQgdqscanKLLRWLRNWQKSssEDKKHAKFgkfsgkddgssfkaallSGPPGVGKTTT 633
Cdd:PRK00440 1 AMMEEIWVEKYRPRTLDEIVGQE-------EIVERLKSYVKE--KNMPHLLF-----------------AGPPGTGKTTA 54
|
90 100
....*....|....*....|....*.
gi 1390249180 634 ASLVCQEL-GYSY----VELNASDTR 654
Cdd:PRK00440 55 ALALARELyGEDWrenfLELNASDER 80
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
618-706 |
2.99e-06 |
|
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: 51.07 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 618 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK------SSLKAIVAESLnntsikgfysnGAASSVstkhaLI 691
Cdd:COG0464 192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFDKAR-----------GLAPCV-----LF 255
|
90
....*....|....*
gi 1390249180 692 MDEVDGMAGNEDRGG 706
Cdd:COG0464 256 IDEADALAGKRGEVG 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-378 |
3.04e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 14 KKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLP--- 90
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkka 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 91 --VSSKPGKISRQDPVTYISETDEEDDFMCKKA--ASKSKENGRSTNSHLGTSNMKKNEENTKTKNKplSPIKLTPTSVL 166
Cdd:PTZ00121 1408 deLKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 167 DYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEAiAKQLQLDEDAEARKDTEAGETFSSVQAN-LSKAE---KHKYPH 242
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEAKKAEEKKKADeLKKAEelkKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 243 KVKTAQVSDERKSYSPRKQS-----------------KYESSKESQQHSKSSADKIGEVSSPKASS---KLAIMKRKEES 302
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEeakkaeearieevmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKVEQLKKKEAE 1644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249180 303 SYKEIEPVASKRKENAIKLKGETKTPKKTKSspaKKESVSPEDSEKKRTNYQayrsyLNREGPKALGSKEIPKGAE 378
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEA-----LKKEAEEAKKAEELKKKEA 1712
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
619-797 |
3.84e-06 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 49.97 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 619 AALLSGPPGVGKTTTA-----SLVCQELGYS------------------YVELNA---SDTRSKSSLKAIVaESLNNTSI 672
Cdd:COG0470 20 ALLLHGPPGIGKTTLAlalarDLLCENPEGGkacgqchsrlmaagnhpdLLELNPeekSDQIGIDQIRELG-EFLSLTPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 673 KGFYSngaassvstkhALIMDEVDGMAGNEDRGGIQELIGLIKHTkiPIICMCNDRNH--PKIRSLvhyCFDLRFQRPRV 750
Cdd:COG0470 99 EGGRK-----------VVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---CQVIRFRPPSE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1390249180 751 EQIKGAMmsiafkEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCAR 797
Cdd:COG0470 163 EEALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQALAGR 203
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
381-447 |
7.51e-06 |
|
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: 44.83 E-value: 7.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 381 LEGLIFVITGVLeSIERDEAKSLIERYGGKVTGNVSKKTNYLV---MGRDSGQSKSDKAAALGTKIIDED 447
Cdd:cd17747 1 LTGMKFALIGKL-SKSKDELKKLIEKLGGKVASKVTKKVTLCIstkAEVEKMSKKMKEAKEAGVPVVSED 69
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-350 |
1.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 14 KKLVSETVKKNEKTKSDEETLKAKKGIKeiKVNSSRKEDDFKQKQPSKKK-----RIIYDSDSESEETLQVKNAKKPPEK 88
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKK--KAEEAKKADEAKKKAEEAKKadeakKKAEEAKKKADEAKKAAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 89 LPVSSKPGKISRQDPVTYISETDEEDDFMCKKAAS--KSKENGRSTNSHLGTSNMKKNEENTKTKNKPLSPIKLTPTSVL 166
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 167 DYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEAIAKQLQLDEDAEARKDTEAGETFSSVQANLSKAEkhkyphKVKT 246
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA------EEAK 1668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 247 AQVSDERKSYSPRKQSKYESSKESQQHSKSSADKigevsspkassKLAIMKRKEESSYKEIEPVASKRKENAIKLKgetK 326
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----------KAEELKKKEAEEKKKAEELKKAEEENKIKAE---E 1734
|
330 340
....*....|....*....|....
gi 1390249180 327 TPKKTKSSPAKKESVSPEDSEKKR 350
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKK 1758
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
566-665 |
1.48e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 48.90 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 566 PTSLKTIIGQQgdqscanKLL---RWLRNWQKSssedkkhakfGKFSgkddgsSFkaaLLSGPPGVGKTTTASLVCQELG 642
Cdd:COG2256 21 PRTLDEVVGQE-------HLLgpgKPLRRAIEA----------GRLS------SM---ILWGPPGTGKTTLARLIANATD 74
|
90 100
....*....|....*....|...
gi 1390249180 643 YSYVELNASDTrSKSSLKAIVAE 665
Cdd:COG2256 75 AEFVALSAVTS-GVKDIREVIEE 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-378 |
1.71e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 19 ETVKKNEKTKSDEEtlKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLPVSSKPGKI 98
Cdd:PTZ00121 1227 EAVKKAEEAKKDAE--EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 99 SRQDPVTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKTKnkplspikltptsvldyfgtgSVQRSN 178
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD---------------------EAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 179 KKMVASKRK--ELSQNTDESGLNDEAIAKQLQLDEDAEarKDTEAGETFSSVQANLSKAEKHKypHKVKTAQVSDERKSY 256
Cdd:PTZ00121 1364 EKAEAAEKKkeEAKKKADAAKKKAEEKKKADEAKKKAE--EDKKKADELKKAAAAKKKADEAK--KKAEEKKKADEAKKK 1439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 257 SPRKQSKYESSKESQQHSKS--SADKIGEVSSPKASSKLAIMKRKEESSYKEIEPvASKRKENAIKLKGETKTPKKTKSS 334
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE-AKKKADEAKKAAEAKKKADEAKKA 1518
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1390249180 335 PAKKESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAE 378
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
511-647 |
1.75e-05 |
|
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: 48.80 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 511 SLAKTIKKETDVFWKSLDFKEQVAEETSGDSKARNLADD-------SSENKVENLLWVDKYKPTSlktiigqQGDQSCAN 583
Cdd:TIGR00602 18 SLISTITKWSLSRPTSSHRRKNSPSTDIHARKRGFLSLEqdtglelSSENLDGNEPWVEKYKPET-------QHELAVHK 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249180 584 KLLRWLRNWQKSSS-EDKKHakfgkfsgkddgssfKAALLSGPPGVGKTTTASLVCQELGYSYVE 647
Cdd:TIGR00602 91 KKIEEVETWLKAQVlENAPK---------------RILLITGPSGCGKSTTIKILSKELGIQVQE 140
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
618-726 |
1.87e-05 |
|
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: 46.12 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 618 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKSS------LKAI--VAESLnntsikgfysngaASSVstkha 689
Cdd:cd19481 27 KGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgeseknLRKIfeRARRL-------------APCI----- 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1390249180 690 LIMDEVDGMAGNEDRGG------------IQELIGLIKHTKIPIICMCN 726
Cdd:cd19481 89 LFIDEIDAIGRKRDSSGesgelrrvlnqlLTELDGVNSRSKVLVIAATN 137
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
381-430 |
1.90e-05 |
|
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: 43.68 E-value: 1.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1390249180 381 LEGLIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQ 430
Cdd:cd17731 3 FKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQ 51
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-570 |
2.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 14 KKLVSETVKKNEKTKSDEEtlkAKKGIKEIKvnssRKEDDFKQKQPSKKKRiiyDSDSESEETLQVKNAKKPPEKLPVSS 93
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADE---AKKKAEEAK----KKADAAKKKAEEAKKA---AEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 94 KPgkisrqdpvtyISETDEEDDFMCKKAASKSKengrstnshlgTSNMKKNEENTKTKNKPLspikltptsvldyfgtgs 173
Cdd:PTZ00121 1371 KK-----------KEEAKKKADAAKKKAEEKKK-----------ADEAKKKAEEDKKKADEL------------------ 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 174 vqrsnKKMVASKRK--ELSQNTDESGLNDEAIAKQLQLDEDAEARKDTEAGEtfssvqanlsKAEKHKypHKVKTAQVSD 251
Cdd:PTZ00121 1411 -----KKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----------KAEEAK--KKAEEAKKAD 1473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 252 ERKSYSPRKQSKYESSKESQQHSKssadKIGEVSSPKASSKLAIMKRKEESSYKEIEpvaSKRKENAIKLKGETKTPKKT 331
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKK----KADEAKKAAEAKKKADEAKKAEEAKKADE---AKKAEEAKKADEAKKAEEKK 1546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 332 KSSPAKKESVSPEDSEKKRTNyQAYRSYLNREgpKALGSKEIPKGAEnclEGLIFVITGVLESIERDEAKSLIERYGGKV 411
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAE-EAKKAEEDKN--MALRKAEEAKKAE---EARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 412 TGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIRTMPGKKSKYEIAVETEMKKESKLERtpQKNVQGKRKI 491
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--KAAEALKKEA 1698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 492 SPSKKESESKKSRPTSKRDslAKTIKKETDV-FWKSLDFKEQVAEETSGDSKARnlADDSSENKVENLLWVDKYKPTSLK 570
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKK--AEELKKAEEEnKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
620-765 |
1.49e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 45.61 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 620 ALLSGPPGVGKTTTASLVCQELGY---------SYVELNASDTRSKSS-LKAIVAESLNNTSIkgfysngAASSVSTKHA 689
Cdd:COG1474 54 VLIYGPTGTGKTAVAKYVLEELEEeaeergvdvRVVYVNCRQASTRYRvLSRILEELGSGEDI-------PSTGLSTDEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 690 ----------------LIMDEVDGMAGNEDRGGIQELIGL---IKHTKIPIICMCND---RNH--PKIRSlVHYCFDLRF 745
Cdd:COG1474 127 fdrlyealderdgvlvVVLDEIDYLVDDEGDDLLYQLLRAneeLEGARVGVIGISNDlefLENldPRVKS-SLGEEEIVF 205
|
170 180
....*....|....*....|...
gi 1390249180 746 QRPRVEQIKGAMM---SIAFKEG 765
Cdd:COG1474 206 PPYDADELRDILEdraELAFYDG 228
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
552-657 |
2.09e-04 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 43.41 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 552 ENKVENLLWVDKYKPTSlktiigqQGDQSCANKLLRWLRNWQKSSS-EDKKHakfgkfsgkddgssfKAALLSGPPGVGK 630
Cdd:pfam03215 1 INDDGGEQWYEKYKPNC-------LEQLAVHKRKIKDVQEWLDAMFlENAKH---------------RILLISGPSGCGK 58
|
90 100
....*....|....*....|....*...
gi 1390249180 631 TTTASLVCQELGYSYVE-LNASDTRSKS 657
Cdd:pfam03215 59 STVIKELSKELGPKYREwSNPTSFRSPP 86
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-349 |
2.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 14 KKLVSETVKKNEKTKSDEETLKA---KKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDS--ESEETLQVKNAKKPPEK 88
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAeeaKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 89 LPVSSKPGKISRQDPVTYISETDEEDDFMCKKAASKSKengRSTNSHLGTSNMKKNEENTKtknkplspikltptsvldy 168
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK---KAEEAKIKAEELKKAEEEKK------------------- 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 169 fgtgSVQRSNKKMVASKRK--ELSQNTDESGLNDEAIAKQlqldEDAEARKDTEAgetfssvqanlSKAEKHKyphkvKT 246
Cdd:PTZ00121 1634 ----KVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKK----AEEDKKKAEEA-----------KKAEEDE-----KK 1689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 247 AQVSDERKSYSPRKQSKYESSKESQQHSKSSADKIGEVSSPKASSklaiMKRKEESSYKEIEPVASKRKENAIKLKGETK 326
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
330 340
....*....|....*....|...
gi 1390249180 327 TPKKTKSSPAKKESVSPEDSEKK 349
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-378 |
3.58e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 25 EKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRiiyDSDSESEETLQVKNAKKPPE-KLPVSSKPGKISRQDP 103
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA---EDARKAEEARKAEDARKAEEaRKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 104 VTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKTKNKPLSPIKLTPTSVLDYFGTGSVQRSNKKMVA 183
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 184 SKRKELSQNTDESGLNDEAIAKQLQLDEDA----EARKDTEAGETFSSVQAN-LSKAEKHK----YPHKVKTAQVSDERK 254
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAikaeEARKADELKKAEEKKKADeAKKAEEKKkadeAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 255 SYSPRKQSKYESSKESQQHSKsSADKIGEVSSPKASSKLAIMKRKEESSYKEIEpvASKRKENAIKLKGETK-----TPK 329
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE--EAKKKADAAKKKAEEKkkadeAKK 1398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1390249180 330 KTKSSPAKKESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAE 378
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
621-649 |
1.42e-03 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 40.95 E-value: 1.42e-03
10 20
....*....|....*....|....*....
gi 1390249180 621 LLSGPPGVGKTTTASLVCQELGYSYVELN 649
Cdd:COG1936 4 AITGTPGTGKTTVAKLLAERLGLEVIHLN 32
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
622-646 |
2.06e-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: 39.78 E-value: 2.06e-03
10 20
....*....|....*....|....*
gi 1390249180 622 LSGPPGVGKTTTASLVCQELGYSYV 646
Cdd:cd02020 4 IDGPAGSGKSTVAKLLAKKLGLPYL 28
|
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
621-642 |
2.07e-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: 40.18 E-value: 2.07e-03
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
621-651 |
2.18e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.02 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|.
gi 1390249180 621 LLSGPPGVGKTTTASLVCQELGYSYVELNAS 651
Cdd:COG1223 39 LFYGPPGTGKTMLAEALAGELKLPLLTVRLD 69
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
621-642 |
2.91e-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: 41.13 E-value: 2.91e-03
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
618-656 |
3.54e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 40.76 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1390249180 618 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK 656
Cdd:COG1222 113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151
|
|
| RuvB |
COG2255 |
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ... |
621-642 |
3.79e-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: 40.83 E-value: 3.79e-03
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
621-642 |
4.81e-03 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 40.50 E-value: 4.81e-03
|
| AAA_17 |
pfam13207 |
AAA domain; |
623-652 |
5.35e-03 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 38.37 E-value: 5.35e-03
10 20 30
....*....|....*....|....*....|
gi 1390249180 623 SGPPGVGKTTTASLVCQELGYSYVelNASD 652
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGFPHI--SAGD 28
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
14-348 |
6.71e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 14 KKLVSETVKKN-----EKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKK-----KRIIYDSDSESEETL--QVKN 81
Cdd:PTZ00108 1034 KDLVKELKKLGyvrfkDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllSMPIWSLTKEKVEKLnaELEK 1113
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 82 AKKPPEKLpVSSKPGKISRQDPVTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKTKNKPLSPIKLT 161
Cdd:PTZ00108 1114 KEKELEKL-KNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKA 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 162 PTSVldyfGTGSVQRSNKKMVASKRKELSQNTDESGLNDEAIAKQLQLDEDAEARKDTEAGETFSSVQANLSKAEKHKYP 241
Cdd:PTZ00108 1193 SVVG----NSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKE 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249180 242 HKVKTAQVSDERKSYSPRKQSKyESSKESQQHSKSSADKIGEVSSPKASSKLAIMKRKEEssyKEIEPVASKRKENAIKL 321
Cdd:PTZ00108 1269 GKPKNAPKRVSAVQYSPPPPSK-RPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKS---EKKTARKKKSKTRVKQA 1344
|
330 340
....*....|....*....|....*..
gi 1390249180 322 KGETKTPkkTKSSPAKKESVSPEDSEK 348
Cdd:PTZ00108 1345 SASQSSR--LLRRPRKKKSDSSSEDDD 1369
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