|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
898-1051 |
1.41e-74 |
|
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: 243.25 E-value: 1.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 898 ICDGDLVDNQIRSKQNWSLLPTQAIYASVVPGELMRGYMSQFPSFPSWLGKHSSTGKHDRTVQDLSLHMSLRTYSSKRTV 977
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677445 978 NMDYLSHIRDALVRPLTSQGVEGVQRVVTLMDTYYLVKEDFDNIMEVSSWG----GKPSTFSKLDPKVKAAFTRAYNK 1051
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
567-986 |
1.16e-52 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 192.83 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 567 LLWVDKYKPTSLKNIIGQQgdqSCANKLLRWLRNWHKSSPEekkhaakfgkvaskddgssfKAALLSGPPGVGKTTTASL 646
Cdd:PRK04195 2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLKGKPK--------------------KALLLYGPPGVGKTSLAHA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 647 VCQELGYSYVELNASDTRSKNSLKAIVAESLNNTSIKGfytsgaspsvSARHALIMDEVDGMAGNEDRGGIQELIGLIKH 726
Cdd:PRK04195 59 LANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFG----------ARRKLILLDEVDGIHGNEDRGGARAILELIKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 727 TKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVRQVLHNLSMWCA 806
Cdd:PRK04195 129 AKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 807 QSKVLTYDQAKADSQRakkDIRLGPFDVTRKVFAA-GEETAHMSLMDkSDLFFHDYSiapLFVQEN----YLHVKPVAAG 881
Cdd:PRK04195 209 GYGKLTLEDVKTLGRR---DREESIFDALDAVFKArNADQALEASYD-VDEDPDDLI---EWIDENipkeYDDPEDIARA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 882 GDMkkhlmlLSRAadsicdgDLVDNQIRSKQNWSLLPtqaiYASvvpgELMRG---YMSQFP-------SFPSWLGKHSS 951
Cdd:PRK04195 282 YDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMTAgvaLAKEKKkrgftryQPPSYWRLLSK 340
|
410 420 430
....*....|....*....|....*....|....*
gi 1958677445 952 TGKHDRTVQDLSLHMSLRTYSSKRTVNMDYLSHIR 986
Cdd:PRK04195 341 TKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
398-476 |
2.27e-47 |
|
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: 163.15 E-value: 2.27e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677445 398 GAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIR 476
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
394-475 |
2.39e-28 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 122.44 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 394 EIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGqSKSDKAAALGTKILDEDGLLD 473
Cdd:COG0272 587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665
|
..
gi 1958677445 474 LI 475
Cdd:COG0272 666 LL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
388-475 |
2.54e-25 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 112.91 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 388 KALGSKEIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGqSKSDKAAALGTKILD 467
Cdd:PRK07956 576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654
|
....*...
gi 1958677445 468 EDGLLDLI 475
Cdd:PRK07956 655 EEEFLRLL 662
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
631-759 |
3.27e-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: 79.17 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 631 LLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKnslkaIVAESLNNtsIKGFYT--SGASPSVsarhaLIMDEVDGM 708
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEaaKKLAPCV-----IFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958677445 709 AGNEDRGGIQELIGLI------------KHTKIPIICMCNdrNHPKIRSLVHYCFDLRFQRPR 759
Cdd:pfam00004 70 AGSRGSGGDSESRRVVnqllteldgftsSNSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
400-475 |
3.08e-16 |
|
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: 74.25 E-value: 3.08e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 400 ENCLEGLTFVITGvLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMgrDSGQSKSDKAAALGTKILDEDGLLDLI 475
Cdd:pfam00533 3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
617-755 |
5.46e-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: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 617 KVASKDDGSSFKAALLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKNSLKAIVAESLNNtsIKGFYTSGASPS 693
Cdd:cd00009 9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVR--LLFELAEKAKPG 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 694 VsarhaLIMDEVDGMAGNEDRGGIQEL----IGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRF 755
Cdd:cd00009 87 V-----LFIDEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
400-475 |
2.78e-14 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 68.94 E-value: 2.78e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677445 400 ENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAA--LGTKILDEDGLLDLI 475
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAiaLGIPIVKEEWLLDCL 78
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
631-761 |
2.25e-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: 57.38 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 631 LLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKNSLKAIVaesLNNTSIKGFYTSGASPSVSARHA-------L 700
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLL---IIVGGKKASGSGELRLRLALALArklkpdvL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958677445 701 IMDEVDGMAGNEDRGGIQE------LIGLIKHTKIPIICMCNDRNHPKIRSLVHyCFDLRFQRPRVE 761
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
312-476 |
4.68e-09 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 59.02 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 312 ASSKLALMKAQEENSYKETEL--LAAKRESAIEPKGEKttPRKTKGSPTKRESvsPEDSEKKRtnyqayrsylnregpka 389
Cdd:PRK06195 152 ACSNILLNISKELNSKDINEIskLLGVTLGYVNENGYK--PSSRKGRILKRSN--RQAPRKKK----------------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 390 lgsKEIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMG--------RDSGQSKSDKAAAL 461
Cdd:PRK06195 211 ---KIIESFGFTAFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnREEMSNKLKKAIDL 287
|
170 180
....*....|....*....|
gi 1958677445 462 -----GTKILDEDGLLDLIR 476
Cdd:PRK06195 288 kkkgqNIKFLNEEEFLQKCK 307
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-563 |
5.67e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 19 ETVKKNEKTKPSEGTVKGKKGVKEAKVNNPCKEDASRPKQHNKKKRIIYDSDSESEETVQVKN--AKKKSEKLPVSCKPG 96
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 97 KISRKDPvtyiSETDEDDDFLCKKAASKSKengvstnsylgASNVKKNEENTKTKSKPLSPIKLTPTSVLDyfGTESVQR 176
Cdd:PTZ00121 1367 EAAEKKK----EEAKKKADAAKKKAEEKKK-----------ADEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEE 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 177 SGKKMVASKKKESSQTPDDSRLNDEAIAKQLQLDEDAELERQLHEDEEFARTLALLDE-EPKTKKARKDSEEGESFSPAK 255
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAK 1509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 256 A---ELSKAAKQKSPANAEHFSIGRKTYSPAKYGKGRGSEGTK--QPCRSAHQKEACSSLKASSK---LALMKAQEENSY 327
Cdd:PTZ00121 1510 KkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKAEEAKKAEEdknMALRKAEEAKKA 1589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 328 KETELLAAKRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTnyqayrsylnrEGPKALGSKEIPKGaencleglt 407
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----------EQLKKKEAEEKKKA--------- 1649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 408 fvitgvlESIEREEAKSLIERYGGKVTGNVSKKTSYLVmgRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKKSKYEI 487
Cdd:PTZ00121 1650 -------EELKKAEEENKIKAAEEAKKAEEDKKKAEEA--KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677445 488 AAEAEmKKEKSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKHSPRKAV---KEEERVCPRGLDAKEPHGSHSASR 563
Cdd:PTZ00121 1721 LKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEeirKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
629-804 |
6.17e-07 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 52.28 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 629 AALLSGPPGVGKTTTA-----SLVCQELGYS------------------YVELNA---SDTRSKNSLKAIVaESLNNTSI 682
Cdd:COG0470 20 ALLLHGPPGIGKTTLAlalarDLLCENPEGGkacgqchsrlmaagnhpdLLELNPeekSDQIGIDQIRELG-EFLSLTPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 683 KGfytsgaspsvsARHALIMDEVDGMAGNEDRGGIQELIGLIKHTkiPIICMCNDRNH--PKIRSLvhyCFDLRFQRPRV 760
Cdd:COG0470 99 EG-----------GRKVVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---CQVIRFRPPSE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958677445 761 EQIKSAMlsiafkEGLKIPPPAMNEIILGANQDVRQVLHNLSMW 804
Cdd:COG0470 163 EEALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQAL 200
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
532-657 |
1.75e-04 |
|
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: 45.72 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 532 KHSPRKAVKEEERvcpRGLDAKEPHGSHSASREEC--LLWVDKYKPTSLKNIIgqqgdqscankllrwlrnWHKSSPEEK 609
Cdd:TIGR00602 38 KNSPSTDIHARKR---GFLSLEQDTGLELSSENLDgnEPWVEKYKPETQHELA------------------VHKKKIEEV 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958677445 610 KHA--AKFGKVASKddgssfKAALLSGPPGVGKTTTASLVCQELGYSYVE 657
Cdd:TIGR00602 97 ETWlkAQVLENAPK------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 ... |
898-1051 |
1.41e-74 |
|
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: 243.25 E-value: 1.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 898 ICDGDLVDNQIRSKQNWSLLPTQAIYASVVPGELMRGYMSQFPSFPSWLGKHSSTGKHDRTVQDLSLHMSLRTYSSKRTV 977
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677445 978 NMDYLSHIRDALVRPLTSQGVEGVQRVVTLMDTYYLVKEDFDNIMEVSSWG----GKPSTFSKLDPKVKAAFTRAYNK 1051
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
567-986 |
1.16e-52 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 192.83 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 567 LLWVDKYKPTSLKNIIGQQgdqSCANKLLRWLRNWHKSSPEekkhaakfgkvaskddgssfKAALLSGPPGVGKTTTASL 646
Cdd:PRK04195 2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLKGKPK--------------------KALLLYGPPGVGKTSLAHA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 647 VCQELGYSYVELNASDTRSKNSLKAIVAESLNNTSIKGfytsgaspsvSARHALIMDEVDGMAGNEDRGGIQELIGLIKH 726
Cdd:PRK04195 59 LANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFG----------ARRKLILLDEVDGIHGNEDRGGARAILELIKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 727 TKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVRQVLHNLSMWCA 806
Cdd:PRK04195 129 AKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 807 QSKVLTYDQAKADSQRakkDIRLGPFDVTRKVFAA-GEETAHMSLMDkSDLFFHDYSiapLFVQEN----YLHVKPVAAG 881
Cdd:PRK04195 209 GYGKLTLEDVKTLGRR---DREESIFDALDAVFKArNADQALEASYD-VDEDPDDLI---EWIDENipkeYDDPEDIARA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 882 GDMkkhlmlLSRAadsicdgDLVDNQIRSKQNWSLLPtqaiYASvvpgELMRG---YMSQFP-------SFPSWLGKHSS 951
Cdd:PRK04195 282 YDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMTAgvaLAKEKKkrgftryQPPSYWRLLSK 340
|
410 420 430
....*....|....*....|....*....|....*
gi 1958677445 952 TGKHDRTVQDLSLHMSLRTYSSKRTVNMDYLSHIR 986
Cdd:PRK04195 341 TKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
398-476 |
2.27e-47 |
|
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: 163.15 E-value: 2.27e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677445 398 GAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIR 476
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
394-475 |
2.39e-28 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 122.44 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 394 EIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGqSKSDKAAALGTKILDEDGLLD 473
Cdd:COG0272 587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665
|
..
gi 1958677445 474 LI 475
Cdd:COG0272 666 LL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
388-475 |
2.54e-25 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 112.91 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 388 KALGSKEIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGqSKSDKAAALGTKILD 467
Cdd:PRK07956 576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654
|
....*...
gi 1958677445 468 EDGLLDLI 475
Cdd:PRK07956 655 EEEFLRLL 662
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
403-474 |
2.63e-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: 97.17 E-value: 2.63e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 403 LEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSD----KAAALGTKILDEDGLLDL 474
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKKgeelKAKGLGIKIISEEEFLDL 76
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
631-759 |
3.27e-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: 79.17 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 631 LLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKnslkaIVAESLNNtsIKGFYT--SGASPSVsarhaLIMDEVDGM 708
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEaaKKLAPCV-----IFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958677445 709 AGNEDRGGIQELIGLI------------KHTKIPIICMCNdrNHPKIRSLVHYCFDLRFQRPR 759
Cdd:pfam00004 70 AGSRGSGGDSESRRVVnqllteldgftsSNSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
401-473 |
1.20e-16 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 85.19 E-value: 1.20e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 401 NCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAALGTKILDED---GLLD 473
Cdd:PRK14351 608 DALDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVGENPGQSKRDDAEANDVPTLDEEefeELLA 683
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
400-475 |
3.08e-16 |
|
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: 74.25 E-value: 3.08e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 400 ENCLEGLTFVITGvLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMgrDSGQSKSDKAAALGTKILDEDGLLDLI 475
Cdd:pfam00533 3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
617-755 |
5.46e-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: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 617 KVASKDDGSSFKAALLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKNSLKAIVAESLNNtsIKGFYTSGASPS 693
Cdd:cd00009 9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVR--LLFELAEKAKPG 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 694 VsarhaLIMDEVDGMAGNEDRGGIQEL----IGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRF 755
Cdd:cd00009 87 V-----LFIDEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
400-475 |
2.78e-14 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 68.94 E-value: 2.78e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677445 400 ENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAA--LGTKILDEDGLLDLI 475
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAiaLGIPIVKEEWLLDCL 78
|
|
| HLD_clamp_RFC |
cd18140 |
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ... |
758-814 |
3.69e-11 |
|
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: 59.46 E-value: 3.69e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958677445 758 PRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVRQVLHNLSMWCAQSKVLTYD 814
Cdd:cd18140 1 LSKEQIVKRLREICKKEGVKIDEEALEAIAEKSEGDMRKAINDLQAAAAGGGVITEE 57
|
|
| PLN03025 |
PLN03025 |
replication factor C subunit; Provisional |
569-801 |
4.76e-11 |
|
replication factor C subunit; Provisional
Pssm-ID: 178596 [Multi-domain] Cd Length: 319 Bit Score: 65.52 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 569 WVDKYKPTSLKNIIGQQgdqscankllrwlrnwhksspeekKHAAKFGKVASkdDGSsFKAALLSGPPGVGKTTTA-SLV 647
Cdd:PLN03025 3 WVEKYRPTKLDDIVGNE------------------------DAVSRLQVIAR--DGN-MPNLILSGPPGTGKTTSIlALA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 648 CQELGYSY----VELNASDTRSKNSLKaivaeslnnTSIKGFytsgASPSVS---ARHAL-IMDEVDGMAGnedrGGIQE 719
Cdd:PLN03025 56 HELLGPNYkeavLELNASDDRGIDVVR---------NKIKMF----AQKKVTlppGRHKIvILDEADSMTS----GAQQA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 720 LIGLIK----HTKIPIICMCNDRNHPKIRSlvhYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVR 795
Cdd:PLN03025 119 LRRTMEiysnTTRFALACNTSSKIIEPIQS---RCAIVRFSRLSDQEILGRLMKVVEAEKVPYVPEGLEAIIFTADGDMR 195
|
....*.
gi 1958677445 796 QVLHNL 801
Cdd:PLN03025 196 QALNNL 201
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
406-473 |
1.56e-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: 55.06 E-value: 1.56e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677445 406 LTFVITGvLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAALGTKILDEDGLLD 473
Cdd:cd00027 1 LVICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLD 67
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
631-761 |
2.25e-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: 57.38 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 631 LLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKNSLKAIVaesLNNTSIKGFYTSGASPSVSARHA-------L 700
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLL---IIVGGKKASGSGELRLRLALALArklkpdvL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958677445 701 IMDEVDGMAGNEDRGGIQE------LIGLIKHTKIPIICMCNDRNHPKIRSLVHyCFDLRFQRPRVE 761
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
312-476 |
4.68e-09 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 59.02 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 312 ASSKLALMKAQEENSYKETEL--LAAKRESAIEPKGEKttPRKTKGSPTKRESvsPEDSEKKRtnyqayrsylnregpka 389
Cdd:PRK06195 152 ACSNILLNISKELNSKDINEIskLLGVTLGYVNENGYK--PSSRKGRILKRSN--RQAPRKKK----------------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 390 lgsKEIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMG--------RDSGQSKSDKAAAL 461
Cdd:PRK06195 211 ---KIIESFGFTAFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnREEMSNKLKKAIDL 287
|
170 180
....*....|....*....|
gi 1958677445 462 -----GTKILDEDGLLDLIR 476
Cdd:PRK06195 288 kkkgqNIKFLNEEEFLQKCK 307
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-563 |
5.67e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 19 ETVKKNEKTKPSEGTVKGKKGVKEAKVNNPCKEDASRPKQHNKKKRIIYDSDSESEETVQVKN--AKKKSEKLPVSCKPG 96
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 97 KISRKDPvtyiSETDEDDDFLCKKAASKSKengvstnsylgASNVKKNEENTKTKSKPLSPIKLTPTSVLDyfGTESVQR 176
Cdd:PTZ00121 1367 EAAEKKK----EEAKKKADAAKKKAEEKKK-----------ADEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEE 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 177 SGKKMVASKKKESSQTPDDSRLNDEAIAKQLQLDEDAELERQLHEDEEFARTLALLDE-EPKTKKARKDSEEGESFSPAK 255
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAK 1509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 256 A---ELSKAAKQKSPANAEHFSIGRKTYSPAKYGKGRGSEGTK--QPCRSAHQKEACSSLKASSK---LALMKAQEENSY 327
Cdd:PTZ00121 1510 KkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKAEEAKKAEEdknMALRKAEEAKKA 1589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 328 KETELLAAKRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTnyqayrsylnrEGPKALGSKEIPKGaencleglt 407
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----------EQLKKKEAEEKKKA--------- 1649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 408 fvitgvlESIEREEAKSLIERYGGKVTGNVSKKTSYLVmgRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKKSKYEI 487
Cdd:PTZ00121 1650 -------EELKKAEEENKIKAAEEAKKAEEDKKKAEEA--KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677445 488 AAEAEmKKEKSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKHSPRKAV---KEEERVCPRGLDAKEPHGSHSASR 563
Cdd:PTZ00121 1721 LKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEeirKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
567-828 |
1.21e-08 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 57.96 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 567 LLWVDKYKPTSLKNIIGQQgdqscankllrwlrnwhksspEEKKHAAKFgkVASKDdgssFKAALLSGPPGVGKTTTASL 646
Cdd:PRK00440 5 EIWVEKYRPRTLDEIVGQE---------------------EIVERLKSY--VKEKN----MPHLLFAGPPGTGKTTAALA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 647 VCQEL-GYSY----VELNASDTRSKNSLKaivaeslnnTSIKGFytSGASPSVSARHALI-MDEVDGM---AGNEDRgGI 717
Cdd:PRK00440 58 LARELyGEDWrenfLELNASDERGIDVIR---------NKIKEF--ARTAPVGGAPFKIIfLDEADNLtsdAQQALR-RT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 718 QELIGliKHTKIPIICmcndrNHP-KI------RslvhyCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGA 790
Cdd:PRK00440 126 MEMYS--QNTRFILSC-----NYSsKIidpiqsR-----CAVFRFSPLKKEAVAERLRYIAENEGIEITDDALEAIYYVS 193
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958677445 791 NQDVRQVLHNLSMWCAQSKVLTYDQAKADSQRAK-KDIR 828
Cdd:PRK00440 194 EGDMRKAINALQAAAATGKEVTEEAVYKITGTARpEEIR 232
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
571-681 |
2.95e-08 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 57.40 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 571 DKYKPTSLKNIIGQQ---GdqscANKLLRwlrnwhksspeekkHAAKFGKVASkddgssfkaALLSGPPGVGKTTTASLV 647
Cdd:PRK13342 4 ERMRPKTLDEVVGQEhllG----PGKPLR--------------RMIEAGRLSS---------MILWGPPGTGKTTLARII 56
|
90 100 110
....*....|....*....|....*....|....
gi 1958677445 648 CQELGYSYVELNASDTrSKNSLKAIVAESLNNTS 681
Cdd:PRK13342 57 AGATDAPFEALSAVTS-GVKDLREVIEEARQRRS 89
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
567-745 |
3.27e-07 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 53.46 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 567 LLWVDKYKPTSLKNIIGQQGDQscankllrwlrnwhksspeekkhaAKFGKVASKddGSSFKAALLSGPPGVGKTTTASL 646
Cdd:PHA02544 9 FMWEQKYRPSTIDECILPAADK------------------------ETFKSIVKK--GRIPNMLLHSPSPGTGKTTVAKA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 647 VCQELGYSYVELNASDTR---SKNSLKAivaeslnntsikgfYTSGAspSVSARH-ALIMDEVD--GMAGNED--RGGIQ 718
Cdd:PHA02544 63 LCNEVGAEVLFVNGSDCRidfVRNRLTR--------------FASTV--SLTGGGkVIIIDEFDrlGLADAQRhlRSFME 126
|
170 180
....*....|....*....|....*....
gi 1958677445 719 ELiglikHTKIPIICMCNDRN--HPKIRS 745
Cdd:PHA02544 127 AY-----SKNCSFIITANNKNgiIEPLRS 150
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
403-475 |
4.06e-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: 48.30 E-value: 4.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 403 LEGLTFVITGVLeSIEREEAKSLIERYGGKVTGNVSKKTSYLV---MGRDSGQSKSDKAAALGTKILDEDGLLDLI 475
Cdd:cd17747 1 LTGMKFALIGKL-SKSKDELKKLIEKLGGKVASKVTKKVTLCIstkAEVEKMSKKMKEAKEAGVPVVSEDFLEDCI 75
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
629-804 |
6.17e-07 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 52.28 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 629 AALLSGPPGVGKTTTA-----SLVCQELGYS------------------YVELNA---SDTRSKNSLKAIVaESLNNTSI 682
Cdd:COG0470 20 ALLLHGPPGIGKTTLAlalarDLLCENPEGGkacgqchsrlmaagnhpdLLELNPeekSDQIGIDQIRELG-EFLSLTPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 683 KGfytsgaspsvsARHALIMDEVDGMAGNEDRGGIQELIGLIKHTkiPIICMCNDRNH--PKIRSLvhyCFDLRFQRPRV 760
Cdd:COG0470 99 EG-----------GRKVVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---CQVIRFRPPSE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958677445 761 EQIKSAMlsiafkEGLKIPPPAMNEIILGANQDVRQVLHNLSMW 804
Cdd:COG0470 163 EEALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQAL 200
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
628-716 |
6.64e-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: 52.99 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 628 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK------NSLKAIVAESLnntsikgfytsGASPSVsarhaLI 701
Cdd:COG0464 192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFDKAR-----------GLAPCV-----LF 255
|
90
....*....|....*
gi 1958677445 702 MDEVDGMAGNEDRGG 716
Cdd:COG0464 256 IDEADALAGKRGEVG 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-544 |
2.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 11 SSGKKPVNETVKKNEKTKPSEgtvKGKKGVKEAKVnnpcKEDASRPKQHNKKKRiiydsdseseETVQVKNAKKKSEKLP 90
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKK----KADAAKKKAEEAKKA----------AEAAKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 91 VSCKPGKISRKDPvtyiSETDEDDDFLCKKAASKSKengvstnsylgASNVKKNEENTKTKSKPLSPIKLTPTSVLDyfG 170
Cdd:PTZ00121 1361 AAEEKAEAAEKKK----EEAKKKADAAKKKAEEKKK-----------ADEAKKKAEEDKKKADELKKAAAAKKKADE--A 1423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 171 TESVQRSGKKMVASKKKESSQTPDDSRLNDEAIAKQLQLDEDAELERQLHEDEEFARTLALLDE-EPKTKKARKDSEEGE 249
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAK 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 250 SFSPAKA---ELSKAAKQKSPANAEHFSIGRKTYSPAKYGKGRGSEGTK--QPCRSAHQKEACSSLKASSK---LALMKA 321
Cdd:PTZ00121 1504 KAAEAKKkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKAEEAKKAEEdknMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 322 QEENSYKETELLAAKRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTnyqayrsylnrEGPKALGSKEIPKGaen 401
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----------EQLKKKEAEEKKKA--- 1649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 402 clegltfvitgvlESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAaalgtkildedglldLIRTMPGK 481
Cdd:PTZ00121 1650 -------------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA---------------LKKEAEEA 1701
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958677445 482 KSKYEIAAEAEmkKEKSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKhsprkaVKEEER 544
Cdd:PTZ00121 1702 KKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK------KDEEEK 1756
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
575-675 |
4.69e-06 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 50.44 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 575 PTSLKNIIGQQgdqscanKLL---RWLRNWHKSspeekkhaakfGKVASkddgssfkaALLSGPPGVGKTTTASLVCQEL 651
Cdd:COG2256 21 PRTLDEVVGQE-------HLLgpgKPLRRAIEA-----------GRLSS---------MILWGPPGTGKTTLARLIANAT 73
|
90 100
....*....|....*....|....
gi 1958677445 652 GYSYVELNASDTrSKNSLKAIVAE 675
Cdd:COG2256 74 DAEFVALSAVTS-GVKDIREVIEE 96
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
628-736 |
6.75e-06 |
|
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: 47.28 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 628 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKNS------LKAI--VAESLnntsikgfytsgaSPSVsarha 699
Cdd:cd19481 27 KGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgeseknLRKIfeRARRL-------------APCI----- 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958677445 700 LIMDEVDGMAGNEDRGG------------IQELIGLIKHTKIPIICMCN 736
Cdd:cd19481 89 LFIDEIDAIGRKRDSSGesgelrrvlnqlLTELDGVNSRSKVLVIAATN 137
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
403-476 |
1.11e-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: 44.45 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958677445 403 LEGLTFVITGvLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQsKSDKAAALGT-KILDEDGLLDLIR 476
Cdd:cd17731 3 FKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQ-KYEFARKWNSiHIVTPEWLYDSIE 75
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-565 |
3.74e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 19 ETVKKNEKTKPSEGtvKGKKGVKEAKVNNPCKEDASRPKQHNKKKRIIYDSDSESEETVQVKNAKKKSEKLpvsckpgki 98
Cdd:PTZ00121 1227 EAVKKAEEAKKDAE--EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA--------- 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 99 sRKdpvtyiSETDEDDDFLCKKAASKSKengvstnsylgASNVKKNEENTKTKSKPLSPiKLTPTSVLDYFGTESVQRSG 178
Cdd:PTZ00121 1296 -KK------AEEKKKADEAKKKAEEAKK-----------ADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 179 KKMVASKKKESS---QTPDDSRLNDEAIAKQLQLDEDAELERQLHEDEEFArtlallDEEPKTKKARKDSEEGESfspaK 255
Cdd:PTZ00121 1357 DEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA------DELKKAAAAKKKADEAKK----K 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 256 AELSKAAKQKSPANAEhfsiGRKTYSPAKygKGRGSEGTKQPCRSAHQKEACSSLKassKLALMKAQEENSYKETELLAA 335
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEE----AKKADEAKK--KAEEAKKAEEAKKKAEEAKKADEAK---KKAEEAKKADEAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 336 KRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAEnclegltfviTGVLE 415
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE----------KKKAE 1567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 416 SIEREEAKSLIERYGGKVTGNVSKKTSYLVMgRDSGQSKSDKAAALgTKILDEDGLLDLIRTMPGKKSKYEIAAEAEmKK 495
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEA-KKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AE 1644
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 496 EKSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKHSPRKAVKEEERVCPRGLDAKEPHGSHSASREE 565
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
578-661 |
1.22e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 44.87 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 578 LKNIIGQQgdqSCANKLLRWLRNWHKSspeekKHAAKFGKVASKDdgssfkaALLSGPPGVGKTTTASLVCQELGYSYVE 657
Cdd:COG1223 1 LDDVVGQE---EAKKKLKLIIKELRRR-----ENLRKFGLWPPRK-------ILFYGPPGTGKTMLAEALAGELKLPLLT 65
|
....
gi 1958677445 658 LNAS 661
Cdd:COG1223 66 VRLD 69
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
532-657 |
1.75e-04 |
|
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: 45.72 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 532 KHSPRKAVKEEERvcpRGLDAKEPHGSHSASREEC--LLWVDKYKPTSLKNIIgqqgdqscankllrwlrnWHKSSPEEK 609
Cdd:TIGR00602 38 KNSPSTDIHARKR---GFLSLEQDTGLELSSENLDgnEPWVEKYKPETQHELA------------------VHKKKIEEV 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958677445 610 KHA--AKFGKVASKddgssfKAALLSGPPGVGKTTTASLVCQELGYSYVE 657
Cdd:TIGR00602 97 ETWlkAQVLENAPK------RILLITGPSGCGKSTTIKILSKELGIQVQE 140
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-543 |
2.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 138 ASNVKKNEENTKTKSKPLSPIKLTPTSVLDYFGTESVQRSGKKMVASKKKESSQTPDDSRLNDEAIAKQLQLDEDAELER 217
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 218 QLHEDEEFARTLALLDEepKTKKARKDSEEGESFSPAKAELSKAAKQKSPANAEHFSIGRKTYSPAKYGKGRGSEGTKQP 297
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 298 CRSAHQKEACSSLKassklalmKAQEENSYKETEL--LAAKRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTNY 375
Cdd:PTZ00121 1384 KKKAEEKKKADEAK--------KKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 376 QAYRSYLNREGPKALGSKEIPKGAEnclegltfvitgvlESIEREEAKSLIERygGKVTGNVSKKTSYLVMGRDSGQSKS 455
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAE--------------EAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKKAE 1519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 456 DKAAALGTKILDEDGLLDLIRTMPGKKSKYEIAAEAEMKKEKSKLERTPQKNDQGKRKLSPTK----RELEPKKSKLTPL 531
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMK 1599
|
410
....*....|..
gi 1958677445 532 KHSPRKAVKEEE 543
Cdd:PTZ00121 1600 LYEEEKKMKAEE 1611
|
|
| PRK14970 |
PRK14970 |
DNA polymerase III subunits gamma and tau; Provisional |
572-816 |
4.17e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184934 [Multi-domain] Cd Length: 367 Bit Score: 44.09 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 572 KYKPTSLKNIIGQQgdqSCANKLLRWLRNWHKSSpeekkhaakfgkvaskddgssfkAALLSGPPGVGKTTTASLVCQEL 651
Cdd:PRK14970 10 KYRPQTFDDVVGQS---HITNTLLNAIENNHLAQ-----------------------ALLFCGPRGVGKTTCARILARKI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 652 ---GYSYVELNAS------DTRSKNSLkaivaESLNNTSIKGFYtsgaSPSVSARHALIMDEVDGMAGNEDRGGIQELIG 722
Cdd:PRK14970 64 nqpGYDDPNEDFSfnifelDAASNNSV-----DDIRNLIDQVRI----PPQTGKYKIYIIDEVHMLSSAAFNAFLKTLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 723 LIKHTkipIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIIL---GANQDVRQVLH 799
Cdd:PRK14970 135 PPAHA---IFILATTEKHKIIPTILSRCQIFDFKRITIKDIKEHLAGIAVKEGIKFEDDALHIIAQkadGALRDALSIFD 211
|
250
....*....|....*..
gi 1958677445 800 NLSMWCaqSKVLTYDQA 816
Cdd:PRK14970 212 RVVTFC--GKNITRQAV 226
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
416-480 |
4.44e-04 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 43.54 E-value: 4.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677445 416 SIEREEaksLIERY---GGKVTGNVSKKTSYLVMGR-DSGQSKSDKAAALGTKILDEDGLLDLIRTMPG 480
Cdd:PRK06063 245 SRTHEE---LVERIlhaGLAYSDSVDRDTSLVVCNDpAPEQGKGYHARQLGVPVLDEAAFLELLRAVVG 310
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
619-652 |
4.48e-04 |
|
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: 43.83 E-value: 4.48e-04
10 20 30
....*....|....*....|....*....|....
gi 1958677445 619 ASKDDGSSFKAALLSGPPGVGKTTTASLVCQELG 652
Cdd:TIGR00635 22 AAKMRQEALDHLLLYGPPGLGKTTLAHIIANEMG 55
|
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
631-659 |
1.30e-03 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 40.95 E-value: 1.30e-03
10 20
....*....|....*....|....*....
gi 1958677445 631 LLSGPPGVGKTTTASLVCQELGYSYVELN 659
Cdd:COG1936 4 AITGTPGTGKTTVAKLLAERLGLEVIHLN 32
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
632-656 |
1.57e-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: 40.16 E-value: 1.57e-03
10 20
....*....|....*....|....*
gi 1958677445 632 LSGPPGVGKTTTASLVCQELGYSYV 656
Cdd:cd02020 4 IDGPAGSGKSTVAKLLAKKLGLPYL 28
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
568-665 |
1.74e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 40.71 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 568 LWVDKYKPTSLKNIIgqqgdqscankllrwlrnWHKSSPEEKKHAAKFGKVASKDDgssfKAALLSGPPGVGKTTTASLV 647
Cdd:pfam03215 8 QWYEKYKPNCLEQLA------------------VHKRKIKDVQEWLDAMFLENAKH----RILLISGPSGCGKSTVIKEL 65
|
90
....*....|....*....
gi 1958677445 648 CQELGYSYVE-LNASDTRS 665
Cdd:pfam03215 66 SKELGPKYREwSNPTSFRS 84
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
31-554 |
1.92e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 31 EGTVKGKKGVKEAKVNNPCKEDASrpkqhnkkkriiYDSDSESEETVQVKNAKKKSEKlpvsckpgkiSRKDPVTYISET 110
Cdd:PTZ00121 1057 EGKAEAKAHVGQDEGLKPSYKDFD------------FDAKEDNRADEATEEAFGKAEE----------AKKTETGKAEEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 111 DEdddflcKKAASKSKENGVSTNSYLGASNVKKNEENTKTKSKPLSPIkltPTSVLDYFGTESVQRS--GKKMVASKKKE 188
Cdd:PTZ00121 1115 RK------AEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEI---ARKAEDARKAEEARKAedAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 189 SSQTPDDSRLNDEAiaKQLQLDEDAELERQL-----HEDEEFARTLALLDE-EPKTKKARKDSEEGESFSPAKAELSKAA 262
Cdd:PTZ00121 1186 EVRKAEELRKAEDA--RKAEAARKAEEERKAeearkAEDAKKAEAVKKAEEaKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 263 KQKSPANAEHFSIGRKTYSPAKYGKGRGSEGTKQPCRSAHQKEACSSLKASSKLALMKAQEENSYKETELLAAKRESAIE 342
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 343 PKGEKTTPRKTKGSPTKRESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAENclegltfvitgvlesiEREEA 422
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE----------------DKKKA 1407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 423 KSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSD---KAAALGTKILDEDGLLDLIRTMPGKKSKYEIAAEAEMKKE--- 496
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKade 1487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677445 497 -KSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKHSPRKAvkEEERVCPRGLDAKE 554
Cdd:PTZ00121 1488 aKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--EEAKKADEAKKAEE 1544
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
630-775 |
2.04e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 41.76 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 630 ALLSGPPGVGKTTTASLVCQELGY---------SYVELNASDTRSKNSLKAIVAESLNNTsiKGFYTSGASPSV------ 694
Cdd:COG1474 54 VLIYGPTGTGKTAVAKYVLEELEEeaeergvdvRVVYVNCRQASTRYRVLSRILEELGSG--EDIPSTGLSTDElfdrly 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 695 ------SARHALIMDEVDGMAGNEDRGGIQELIGL---IKHTKIPIICMCND---RNH--PKIRSlVHYCFDLRFQRPRV 760
Cdd:COG1474 132 ealderDGVLVVVLDEIDYLVDDEGDDLLYQLLRAneeLEGARVGVIGISNDlefLENldPRVKS-SLGEEEIVFPPYDA 210
|
170
....*....|....*...
gi 1958677445 761 EQIKSAML---SIAFKEG 775
Cdd:COG1474 211 DELRDILEdraELAFYDG 228
|
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
631-652 |
2.09e-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: 2.09e-03
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
628-666 |
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 1958677445 628 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK 666
Cdd:COG1222 113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151
|
|
| RuvB |
COG2255 |
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ... |
631-652 |
3.83e-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: 3.83e-03
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
631-652 |
4.87e-03 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 40.50 E-value: 4.87e-03
|
| AAA_17 |
pfam13207 |
AAA domain; |
633-662 |
4.96e-03 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 38.37 E-value: 4.96e-03
10 20 30
....*....|....*....|....*....|
gi 1958677445 633 SGPPGVGKTTTASLVCQELGYSYVelNASD 662
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGFPHI--SAGD 28
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
628-709 |
5.11e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 39.20 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 628 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK------NSLKAIVAESlnntsikgfytSGASPSVsarhaLI 701
Cdd:cd19503 35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKylgeseKNLREIFEEA-----------RSHAPSI-----IF 98
|
....*...
gi 1958677445 702 MDEVDGMA 709
Cdd:cd19503 99 IDEIDALA 106
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
628-719 |
5.61e-03 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410919 [Multi-domain] Cd Length: 159 Bit Score: 38.80 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677445 628 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKnslkaIVAESLNNTSiKGFYTS-GASPSVsarhaLIMDEVD 706
Cdd:cd19511 28 KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK-----YVGESERAVR-EIFQKArQAAPCI-----IFFDEID 96
|
90
....*....|....*.
gi 1958677445 707 GMA---GNEDRGGIQE 719
Cdd:cd19511 97 SLAprrGQSDSSGVTD 112
|
|
| PRK14964 |
PRK14964 |
DNA polymerase III subunits gamma and tau; Provisional |
572-647 |
8.43e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237870 [Multi-domain] Cd Length: 491 Bit Score: 40.15 E-value: 8.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677445 572 KYKPTSLKNIIGQqgdqscaNKLLRWLRNwhksspeekkhAAKFGKVASkddgssfkAALLSGPPGVGKTTTASLV 647
Cdd:PRK14964 6 KYRPSSFKDLVGQ-------DVLVRILRN-----------AFTLNKIPQ--------SILLVGASGVGKTTCARII 55
|
|
| |
