|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
764-917 |
4.28e-71 |
|
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: 232.85 E-value: 4.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 764 LSLGDLVEKRIRANSAWSLLPTQAFFSSVLPGEHMCGHFTGQINFPGWLGKNSKSGKRARLAQELHDHTRVCTSGSRLSV 843
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 844 RLDYAPFLLDNIVRPLAKDGQEGVPAALDVMKDYHLLREDLDSLVELTSWP----GKKSPLDAVDGRVKAALTRSYNK 917
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
421-969 |
7.70e-48 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 178.19 E-value: 7.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 421 MAWVDKHKPTSIKEIVGQAgaasnvtnhnlklKAKQErvkvlhyfnfprLMNWLSKWyvnhdgnkkpqrpnpwaknDDGS 500
Cdd:PRK04195 2 MPWVEKYRPKTLSDVVGNE-------------KAKEQ------------LREWIESW-------------------LKGK 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 501 FYKAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEVSTLLSNKSLSGYftgqgqavsRKHVLIMDEVD 580
Cdd:PRK04195 38 PKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA---------RRKLILLDEVD 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 581 GMAGNEDRGGMQELIALIKDSSIPIICMCNDRNHPKIRSLVNYCYDLRFQRPRLEQIKGKIMSICFKEKVKISPAKVEEI 660
Cdd:PRK04195 109 GIHGNEDRGGARAILELIKKAKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 661 IAATNNDIRQSINHI-ALLSAKEDASQKSGQQVATKDLKLGPWEVVRKVFTADEHKH-----MSFADKSDLFFHdyslap 734
Cdd:PRK04195 189 AERSGGDLRSAINDLqAIAEGYGKLTLEDVKTLGRRDREESIFDALDAVFKARNADQaleasYDVDEDPDDLIE------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 735 lFVQQNylqvLPqgNKKDVLAKVAATADALSLGDLVEKRIRANSAWSLLPTqaFFSSVLPG-----EHMCGHFTgQINFP 809
Cdd:PRK04195 263 -WIDEN----IP--KEYDDPEDIARAYDALSRADIFLGRVKRTQNYDLWRY--ASDLMTAGvalakEKKKRGFT-RYQPP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 810 GWLGKNSKS----GKRARLAQEL--HDHTrvctsgSRLSVRLDYAPFLldnivRPLAKDGQEgVPAALDvmKDYHLlreD 883
Cdd:PRK04195 333 SYWRLLSKTkekrETRDSIAKKIaeKLHT------SKRKVRREVLPFL-----SIIFKHNPE-LAARLA--AFLEL---T 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 884 LDSLVELTswpGKKSPLDAVDGRVKAAlTRSYNKEVMAYSYSAQAGIKKKKSEAAGADDDylDEGPGEEDGAGGHLSSEE 963
Cdd:PRK04195 396 EEEIEFLT---GSKKATKKIKKIVEKA-EKKREEEKKEKKKKAFAGKKKEEEEEEEKEKK--EEEKEEEEEEAEEEKEEE 469
|
....*.
gi 62472391 964 DEDKDN 969
Cdd:PRK04195 470 EEKKKK 475
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
232-310 |
2.68e-40 |
|
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: 142.74 E-value: 2.68e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62472391 232 GSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAVAEELNIPILSEDGLFDLIR 310
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
222-309 |
3.95e-23 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 105.49 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 222 LNPGSKEIPKGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGpKKLAVAEELNIPILS 301
Cdd:COG0272 581 VNMEEEEAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILD 659
|
....*...
gi 62472391 302 EDGLFDLI 309
Cdd:COG0272 660 EAEFLELL 667
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
231-311 |
1.08e-18 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 91.34 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 231 KGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGpKKLAVAEELNIPILSEDGLFDLIR 310
Cdd:PRK07956 585 KGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLDEEEFLRLLG 663
|
.
gi 62472391 311 E 311
Cdd:PRK07956 664 E 664
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
232-309 |
3.49e-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: 73.87 E-value: 3.49e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 232 GSPDCLSGLTFVVTGvLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVgeEAGPKKLAVAEELNIPILSEDGLFDLI 309
Cdd:pfam00533 1 PKEKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
506-633 |
8.83e-16 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 74.94 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEvstllsnKSLSGYFTGQGQavSRKHVLIMDEVDGMAGN 585
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESE-------KRLRELFEAAKK--LAPCVIFIDEIDALAGS 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 586 EDRGG-------MQELIALIKD-----SSIPIICMCNdrNHPKIRSLVNYCYDLRFQRPR 633
Cdd:pfam00004 73 RGSGGdsesrrvVNQLLTELDGftssnSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
234-309 |
5.34e-14 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 67.79 E-value: 5.34e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 234 PDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLK-YLVVGEEAGPK-KLAVAEELNIPILSEDGLFDLI 309
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTtHVIVGSPEGGKlELLKAIALGIPIVKEEWLLDCL 78
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
502-629 |
5.43e-11 |
|
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: 61.78 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 502 YKAALLSGPPGIGKTTTATLVVKEL---GFDAVEFNASDTRSKrllkdevsTLLSNKSLSGYFTGQGQAVSRKH--VLIM 576
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEG--------LVVAELFGHFLVRLLFELAEKAKpgVLFI 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 62472391 577 DEVDGMAGNEDRGGMQEL----IALIKDSSIPIICMCNDRNHPKIRSLVNYCYDLRF 629
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
506-635 |
2.33e-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: 57.00 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKEL---GFDAVEFNASDTRSKRLLKDEVSTLLSNKSLSGYFTGQGQAVS--RKH---VLIMD 577
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAlaRKLkpdVLILD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472391 578 EVDGMAGNEDRGGMQELIAL------IKDSSIPIICMCNDRNHPkIRSLVNYCYDLRFQRPRLE 635
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELrlllllKSEKNLTVILTTNDEKDL-GPALLRRRFDRRIVLLLIL 148
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
493-712 |
1.40e-08 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 57.29 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 493 WAKNDDGSfyKAALLSGPPGIGKTTTATLVVKELG-----------------------FDAVEFNAsDTRSKRLLKDEVS 549
Cdd:COG0470 11 AAESGRLP--HALLLHGPPGIGKTTLALALARDLLcenpeggkacgqchsrlmaagnhPDLLELNP-EEKSDQIGIDQIR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 550 TL---LSNKSLSGyftgqgqavSRKhVLIMDEVDGMAGNEDRGGMQELIALIKDSsiPIICMCNDRNH--PKIRSLvnyC 624
Cdd:COG0470 88 ELgefLSLTPLEG---------GRK-VVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---C 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 625 YDLRFQRPRLEQIKGKImsicfkEKVKISPAKVEEIIAATNNDIRQSINHIALLSAKEDASQKSGQQVATKDlklgPWEV 704
Cdd:COG0470 153 QVIRFRPPSEEEALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQALAGRKELLEDLAALLSRDR----ALEL 222
|
....*...
gi 62472391 705 VRKVFTAD 712
Cdd:COG0470 223 LDALLKAE 230
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-434 |
7.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 12 LPAKAKSAEAENGETPSKAPKRRKAVIISSDEDEVVSPPETKKRKASKTASSEddvvAATPEPIAKKARNGQKPAlsKLK 91
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE----AKKKAEEAKKAEEAKKKA--EEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 92 RHVDPTELFGGETKRVIVPKPKTKAVLEfENEDIDRSLMEVDLDESIKEAAPEKKVHSITRSSPSPKRAKNSSPEPPKPK 171
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 172 STKSKATTPRVKKEKPAAdlESSVLTDEERHERKRASAVLYQKYKNRSSCLNPGSKEIPKGSPDCLSGltfvvtgvlESM 251
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK---------AEE 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 252 EREEAESVIKEyggkvmTVVGKKLKYLVVGEEAGPKKlavAEELNipilsEDGLFDLIREKSGIAKQVKEEKKSPKKEHS 331
Cdd:PTZ00121 1618 AKIKAEELKKA------EEEKKKVEQLKKKEAEEKKK---AEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 332 SEEKGKKEVKTSRRSSDKKEKEATKLKYGEKHDIAK--------HKVKEEHTSPKETKDKlndvpavtlkvKKEPSSQKE 403
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkaeeeNKIKAEEAKKEAEEDK-----------KKAEEAKKD 1752
|
410 420 430
....*....|....*....|....*....|.
gi 62472391 404 HPPSPRTADLKTLDVVGMAWVDKHKPTSIKE 434
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
25-223 |
1.01e-03 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 43.16 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 25 ETPSKAPKRRKAViissdEDEVVSPPETKKRKASKTASSEDDvvAATP-------EPIAKKARNGQ-KPALSKLKRHV-- 94
Cdd:NF033875 67 ETPKTAVSEEATV-----QKDTTSQPTKVEEVASEKNGAEQS--SATPndttnaqQPTVGAEKSAQeQPVVSPETTNEpl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 95 -DPTELFGGET---KRVIVPKpktkavlEFENEDIDRSLMEVDLDESIKEA-APEKKVHSITRSSPSPKRAKNSSPEPPK 169
Cdd:NF033875 140 gQPTEVAPAENeanKSTSIPK-------EFETPDVDKAVDEAKKDPNITVVeKPAEDLGNVSSKDLAAKEKEVDQLQKEQ 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 62472391 170 PKSTKSKATTPRVKKEKPA---ADLESSVLTDEERHERKRASavlYQKYKNRSSCLN 223
Cdd:NF033875 213 AKKIAQQAAELKAKNEKIAkenAEIAAKNKAEKERYEKEVAE---YNKHKNENGYVN 266
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RFC1 |
pfam08519 |
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ... |
764-917 |
4.28e-71 |
|
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: 232.85 E-value: 4.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 764 LSLGDLVEKRIRANSAWSLLPTQAFFSSVLPGEHMCGHFTGQINFPGWLGKNSKSGKRARLAQELHDHTRVCTSGSRLSV 843
Cdd:pfam08519 1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 844 RLDYAPFLLDNIVRPLAKDGQEGVPAALDVMKDYHLLREDLDSLVELTSWP----GKKSPLDAVDGRVKAALTRSYNK 917
Cdd:pfam08519 81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
421-969 |
7.70e-48 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 178.19 E-value: 7.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 421 MAWVDKHKPTSIKEIVGQAgaasnvtnhnlklKAKQErvkvlhyfnfprLMNWLSKWyvnhdgnkkpqrpnpwaknDDGS 500
Cdd:PRK04195 2 MPWVEKYRPKTLSDVVGNE-------------KAKEQ------------LREWIESW-------------------LKGK 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 501 FYKAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEVSTLLSNKSLSGYftgqgqavsRKHVLIMDEVD 580
Cdd:PRK04195 38 PKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA---------RRKLILLDEVD 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 581 GMAGNEDRGGMQELIALIKDSSIPIICMCNDRNHPKIRSLVNYCYDLRFQRPRLEQIKGKIMSICFKEKVKISPAKVEEI 660
Cdd:PRK04195 109 GIHGNEDRGGARAILELIKKAKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 661 IAATNNDIRQSINHI-ALLSAKEDASQKSGQQVATKDLKLGPWEVVRKVFTADEHKH-----MSFADKSDLFFHdyslap 734
Cdd:PRK04195 189 AERSGGDLRSAINDLqAIAEGYGKLTLEDVKTLGRRDREESIFDALDAVFKARNADQaleasYDVDEDPDDLIE------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 735 lFVQQNylqvLPqgNKKDVLAKVAATADALSLGDLVEKRIRANSAWSLLPTqaFFSSVLPG-----EHMCGHFTgQINFP 809
Cdd:PRK04195 263 -WIDEN----IP--KEYDDPEDIARAYDALSRADIFLGRVKRTQNYDLWRY--ASDLMTAGvalakEKKKRGFT-RYQPP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 810 GWLGKNSKS----GKRARLAQEL--HDHTrvctsgSRLSVRLDYAPFLldnivRPLAKDGQEgVPAALDvmKDYHLlreD 883
Cdd:PRK04195 333 SYWRLLSKTkekrETRDSIAKKIaeKLHT------SKRKVRREVLPFL-----SIIFKHNPE-LAARLA--AFLEL---T 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 884 LDSLVELTswpGKKSPLDAVDGRVKAAlTRSYNKEVMAYSYSAQAGIKKKKSEAAGADDDylDEGPGEEDGAGGHLSSEE 963
Cdd:PRK04195 396 EEEIEFLT---GSKKATKKIKKIVEKA-EKKREEEKKEKKKKAFAGKKKEEEEEEEKEKK--EEEKEEEEEEAEEEKEEE 469
|
....*.
gi 62472391 964 DEDKDN 969
Cdd:PRK04195 470 EEKKKK 475
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
232-310 |
2.68e-40 |
|
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: 142.74 E-value: 2.68e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62472391 232 GSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAVAEELNIPILSEDGLFDLIR 310
Cdd:cd17752 1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
222-309 |
3.95e-23 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 105.49 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 222 LNPGSKEIPKGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGpKKLAVAEELNIPILS 301
Cdd:COG0272 581 VNMEEEEAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILD 659
|
....*...
gi 62472391 302 EDGLFDLI 309
Cdd:COG0272 660 EAEFLELL 667
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
237-308 |
6.42e-22 |
|
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: 90.23 E-value: 6.42e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472391 237 LSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAV----AEELNIPILSEDGLFDL 308
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKKGeelkAKGLGIKIISEEEFLDL 76
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
231-311 |
1.08e-18 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 91.34 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 231 KGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGpKKLAVAEELNIPILSEDGLFDLIR 310
Cdd:PRK07956 585 KGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLDEEEFLRLLG 663
|
.
gi 62472391 311 E 311
Cdd:PRK07956 664 E 664
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
232-309 |
3.49e-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: 73.87 E-value: 3.49e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 232 GSPDCLSGLTFVVTGvLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVgeEAGPKKLAVAEELNIPILSEDGLFDLI 309
Cdd:pfam00533 1 PKEKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
506-633 |
8.83e-16 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 74.94 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEvstllsnKSLSGYFTGQGQavSRKHVLIMDEVDGMAGN 585
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESE-------KRLRELFEAAKK--LAPCVIFIDEIDALAGS 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 586 EDRGG-------MQELIALIKD-----SSIPIICMCNdrNHPKIRSLVNYCYDLRFQRPR 633
Cdd:pfam00004 73 RGSGGdsesrrvVNQLLTELDGftssnSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
234-309 |
5.34e-14 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 67.79 E-value: 5.34e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 234 PDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLK-YLVVGEEAGPK-KLAVAEELNIPILSEDGLFDLI 309
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTtHVIVGSPEGGKlELLKAIALGIPIVKEEWLLDCL 78
|
|
| PLN03025 |
PLN03025 |
replication factor C subunit; Provisional |
421-675 |
2.30e-13 |
|
replication factor C subunit; Provisional
Pssm-ID: 178596 [Multi-domain] Cd Length: 319 Bit Score: 72.45 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 421 MAWVDKHKPTSIKEIVGQAGAASnvtnhnlklkakqeRVKVlhyfnfprlmnwlskwyVNHDGNKkpqrPNpwaknddgs 500
Cdd:PLN03025 1 LPWVEKYRPTKLDDIVGNEDAVS--------------RLQV-----------------IARDGNM----PN--------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 501 fykaALLSGPPGIGKTTTATLVVKEL----GFDAV-EFNASDTRSKRLLKDEVSTLLSNK-SLsgyftgqgqAVSRKHVL 574
Cdd:PLN03025 37 ----LILSGPPGTGKTTSILALAHELlgpnYKEAVlELNASDDRGIDVVRNKIKMFAQKKvTL---------PPGRHKIV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 575 IMDEVDGM---AGNEDRGGMQelialIKDSSIPIICMCNdRNHPKIRSLVNYCYDLRFQRPRLEQIKGKIMSICFKEKVK 651
Cdd:PLN03025 104 ILDEADSMtsgAQQALRRTME-----IYSNTTRFALACN-TSSKIIEPIQSRCAIVRFSRLSDQEILGRLMKVVEAEKVP 177
|
250 260
....*....|....*....|....
gi 62472391 652 ISPAKVEEIIAATNNDIRQSINHI 675
Cdd:PLN03025 178 YVPEGLEAIIFTADGDMRQALNNL 201
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
502-629 |
5.43e-11 |
|
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: 61.78 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 502 YKAALLSGPPGIGKTTTATLVVKEL---GFDAVEFNASDTRSKrllkdevsTLLSNKSLSGYFTGQGQAVSRKH--VLIM 576
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEG--------LVVAELFGHFLVRLLFELAEKAKpgVLFI 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 62472391 577 DEVDGMAGNEDRGGMQEL----IALIKDSSIPIICMCNDRNHPKIRSLVNYCYDLRF 629
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
218-316 |
6.34e-11 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 66.32 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 218 RSSCLNPGSKEIPKGspDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAVAEELNI 297
Cdd:PRK14351 593 LDHGVDPQPAESEGG--DALDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVGENPGQSKRDDAEANDV 670
|
90
....*....|....*....
gi 62472391 298 PILSEDGLFDLIREkSGIA 316
Cdd:PRK14351 671 PTLDEEEFEELLAE-RGVA 688
|
|
| HLD_clamp_RFC |
cd18140 |
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ... |
632-683 |
1.69e-09 |
|
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: 54.84 E-value: 1.69e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 62472391 632 PRLEQIKGKIMSICFKEKVKISPAKVEEIIAATNNDIRQSINHIALLSAKED 683
Cdd:cd18140 1 LSKEQIVKRLREICKKEGVKIDEEALEAIAEKSEGDMRKAINDLQAAAAGGG 52
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
506-635 |
2.33e-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: 57.00 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKEL---GFDAVEFNASDTRSKRLLKDEVSTLLSNKSLSGYFTGQGQAVS--RKH---VLIMD 577
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAlaRKLkpdVLILD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472391 578 EVDGMAGNEDRGGMQELIAL------IKDSSIPIICMCNDRNHPkIRSLVNYCYDLRFQRPRLE 635
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELrlllllKSEKNLTVILTTNDEKDL-GPALLRRRFDRRIVLLLIL 148
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
506-673 |
1.25e-08 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 57.69 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKrLLKDEVSTLLSNKSLSGyftgqgqavsrKH-VLIMDEVD--GM 582
Cdd:PHA02544 47 LHSPSPGTGKTTVAKALCNEVGAEVLFVNGSDCRID-FVRNRLTRFASTVSLTG-----------GGkVIIIDEFDrlGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 583 AGNED--RGGMQELialikDSSIPIICMCNDRN--HPKIRSlvnYCYDLRFQRP----RLE---QIKGKIMSICFKEKVK 651
Cdd:PHA02544 115 ADAQRhlRSFMEAY-----SKNCSFIITANNKNgiIEPLRS---RCRVIDFGVPtkeeQIEmmkQMIVRCKGILEAEGVE 186
|
170 180
....*....|....*....|..
gi 62472391 652 ISPAKVEEIIAATNNDIRQSIN 673
Cdd:PHA02544 187 VDMKVLAALVKKNFPDFRRTIN 208
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
493-712 |
1.40e-08 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 57.29 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 493 WAKNDDGSfyKAALLSGPPGIGKTTTATLVVKELG-----------------------FDAVEFNAsDTRSKRLLKDEVS 549
Cdd:COG0470 11 AAESGRLP--HALLLHGPPGIGKTTLALALARDLLcenpeggkacgqchsrlmaagnhPDLLELNP-EEKSDQIGIDQIR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 550 TL---LSNKSLSGyftgqgqavSRKhVLIMDEVDGMAGNEDRGGMQELIALIKDSsiPIICMCNDRNH--PKIRSLvnyC 624
Cdd:COG0470 88 ELgefLSLTPLEG---------GRK-VVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---C 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 625 YDLRFQRPRLEQIKGKImsicfkEKVKISPAKVEEIIAATNNDIRQSINHIALLSAKEDASQKSGQQVATKDlklgPWEV 704
Cdd:COG0470 153 QVIRFRPPSEEEALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQALAGRKELLEDLAALLSRDR----ALEL 222
|
....*...
gi 62472391 705 VRKVFTAD 712
Cdd:COG0470 223 LDALLKAE 230
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
423-673 |
2.25e-08 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 56.80 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 423 WVDKHKPTSIKEIVGQagaasnvtnhnlklkakqERVKvlhyfnfPRLMNwlskwYVnhdgnKKPQRPNpwaknddgsfy 502
Cdd:PRK00440 7 WVEKYRPRTLDEIVGQ------------------EEIV-------ERLKS-----YV-----KEKNMPH----------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 503 kaALLSGPPGIGKTTTATLVVKELGFDA-----VEFNASDTRSKRLLKDEVSTLLSNKSLSGY-FtgqgqavsrkHVLIM 576
Cdd:PRK00440 41 --LLFAGPPGTGKTTAALALARELYGEDwrenfLELNASDERGIDVIRNKIKEFARTAPVGGApF----------KIIFL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 577 DEVDGM---AGNEDRGGMqELIA------LIKDSSIPIIcmcndrnhPKIRSlvnYCYDLRFQRPRLEQIKGKIMSICFK 647
Cdd:PRK00440 109 DEADNLtsdAQQALRRTM-EMYSqntrfiLSCNYSSKII--------DPIQS---RCAVFRFSPLKKEAVAERLRYIAEN 176
|
250 260
....*....|....*....|....*.
gi 62472391 648 EKVKISPAKVEEIIAATNNDIRQSIN 673
Cdd:PRK00440 177 EGIEITDDALEAIYYVSEGDMRKAIN 202
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
240-307 |
1.95e-07 |
|
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: 48.90 E-value: 1.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 240 LTFVVTGvLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAVAEELNIPILSEDGLFD 307
Cdd:cd00027 1 LVICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLD 67
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
237-309 |
3.78e-07 |
|
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.
Pssm-ID: 349378 [Multi-domain] Cd Length: 76 Bit Score: 48.30 E-value: 3.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472391 237 LSGLTFVVTGVLeSMEREEAESVIKEYGGKVMTVVGKKLKYLVVGE---EAGPKKLAVAEELNIPILSEDGLFDLI 309
Cdd:cd17747 1 LTGMKFALIGKL-SKSKDELKKLIEKLGGKVASKVTKKVTLCISTKaevEKMSKKMKEAKEAGVPVVSEDFLEDCI 75
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
227-312 |
5.26e-07 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 52.48 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 227 KEIPKGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVG--------EEAGPKKLAVAEEL--- 295
Cdd:PRK06195 211 KIIESFGFTAFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnREEMSNKLKKAIDLkkk 290
|
90
....*....|....*....
gi 62472391 296 --NIPILSEDGLFDLIREK 312
Cdd:PRK06195 291 gqNIKFLNEEEFLQKCKEK 309
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
503-697 |
8.89e-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: 49.14 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 503 KAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKrllkdevstllsnkslsgyFTGQ-GQAVSR---------KH 572
Cdd:COG0464 192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK-------------------YVGEtEKNLREvfdkarglaPC 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 573 VLIMDEVDGMAGNEDRGG---MQELIALI------KDSSIPIICMCNDRNH--PKIRSlvnycydlRFQR------PRLE 635
Cdd:COG0464 253 VLFIDEADALAGKRGEVGdgvGRRVVNTLltemeeLRSDVVVIAATNRPDLldPALLR--------RFDEiiffplPDAE 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472391 636 QIKgKIMSICFKEKVKISPAKVEEIIAATNN----DIRQsinhiALLSAKEDASQKSGQQVATKDL 697
Cdd:COG0464 325 ERL-EIFRIHLRKRPLDEDVDLEELAEATEGlsgaDIRN-----VVRRAALQALRLGREPVTTEDL 384
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
506-606 |
3.48e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 44.25 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKEL---GFDAVEFNASDTRS--------KRLLKDEVSTLLSNKSLSGYFTGQGQAVSRKHVL 574
Cdd:pfam13401 9 VLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdllralLRALGLPLSGRLSKEELLAALQQLLLALAVAVVL 88
|
90 100 110
....*....|....*....|....*....|....
gi 62472391 575 IMDEVDGMagneDRGGMQELIAL--IKDSSIPII 606
Cdd:pfam13401 89 IIDEAQHL----SLEALEELRDLlnLSSKLLQLI 118
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
503-610 |
1.19e-04 |
|
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: 43.43 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 503 KAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLlkDEVSTLLSNkslsgYFtgqgqAVSRKH---VLIMDEV 579
Cdd:cd19481 27 KGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV--GESEKNLRK-----IF-----ERARRLapcILFIDEI 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 62472391 580 DGMAGNEDRGGM------------QELIALIKDSSIPIICMCN 610
Cdd:cd19481 95 DAIGRKRDSSGEsgelrrvlnqllTELDGVNSRSKVLVIAATN 137
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
480-698 |
4.11e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 43.33 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 480 NHDGNKKPQRPNPWAKNDdgsfykaALLSGPPGIGKTTTATLVVKELGFDAVEFNASdtrskrllkdevstllsnkSLSG 559
Cdd:COG1223 20 ELRRRENLRKFGLWPPRK-------ILFYGPPGTGKTMLAEALAGELKLPLLTVRLD-------------------SLIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 560 YFTGQG---------QAVSRKHVLIMDEVDGMAG----NEDRGGMQELI-AL------IKDSSIpIICMCndrNHPKI-- 617
Cdd:COG1223 74 SYLGETarnlrklfdFARRAPCVIFFDEFDAIAKdrgdQNDVGEVKRVVnALlqeldgLPSGSV-VIAAT---NHPELld 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 618 RSLVNYC-YDLRFQRPRLEQIKgKIMSIC---FKEKVKISPAK-VEEIIAATNNDIRQsinhiALLSAKEDASQKSGQQV 692
Cdd:COG1223 150 SALWRRFdEVIEFPLPDKEERK-EILELNlkkFPLPFELDLKKlAKKLEGLSGADIEK-----VLKTALKKAILEDREKV 223
|
....*.
gi 62472391 693 ATKDLK 698
Cdd:COG1223 224 TKEDLE 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-434 |
7.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 12 LPAKAKSAEAENGETPSKAPKRRKAVIISSDEDEVVSPPETKKRKASKTASSEddvvAATPEPIAKKARNGQKPAlsKLK 91
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE----AKKKAEEAKKAEEAKKKA--EEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 92 RHVDPTELFGGETKRVIVPKPKTKAVLEfENEDIDRSLMEVDLDESIKEAAPEKKVHSITRSSPSPKRAKNSSPEPPKPK 171
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 172 STKSKATTPRVKKEKPAAdlESSVLTDEERHERKRASAVLYQKYKNRSSCLNPGSKEIPKGSPDCLSGltfvvtgvlESM 251
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK---------AEE 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 252 EREEAESVIKEyggkvmTVVGKKLKYLVVGEEAGPKKlavAEELNipilsEDGLFDLIREKSGIAKQVKEEKKSPKKEHS 331
Cdd:PTZ00121 1618 AKIKAEELKKA------EEEKKKVEQLKKKEAEEKKK---AEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 332 SEEKGKKEVKTSRRSSDKKEKEATKLKYGEKHDIAK--------HKVKEEHTSPKETKDKlndvpavtlkvKKEPSSQKE 403
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkaeeeNKIKAEEAKKEAEEDK-----------KKAEEAKKD 1752
|
410 420 430
....*....|....*....|....*....|.
gi 62472391 404 HPPSPRTADLKTLDVVGMAWVDKHKPTSIKE 434
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| BRCT_p53bp1_rpt1 |
cd17745 |
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ... |
236-313 |
7.47e-04 |
|
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1) , is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family also includes Schizosaccharomyces pombe Crb2, which is a checkpoint mediator required for the cellular response to DNA damage. This model corresponds to the first BRCT domain.
Pssm-ID: 349376 [Multi-domain] Cd Length: 99 Bit Score: 39.99 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 236 CLSGLTFVVTGVLES---MEREEAESVIKEYGGKVM------------------------------TVVGKKLKYLvvge 282
Cdd:cd17745 1 IFSGCAFLLTGAEETdkpFDKERLESQIEANGGTVLedfdeelfndgrsstrksrskdlrfvfliaDSPSRTPKYL---- 76
|
90 100 110
....*....|....*....|....*....|.
gi 62472391 283 eagpkkLAVAeeLNIPILSEDGLFDLIREKS 313
Cdd:cd17745 77 ------QALA--LGIPCVSHKWILDCIEAGK 99
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
498-611 |
8.84e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 42.91 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 498 DGSFYKAALLSGPPGIGKTTTATLVVKELGFDA---------VEFNASDTRSK-RLLKDEVSTLLSNKSLSgyFTGQG-- 565
Cdd:COG1474 47 RGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAeergvdvrvVYVNCRQASTRyRVLSRILEELGSGEDIP--STGLStd 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 62472391 566 -------QAVSRK---HVLIMDEVDGMAGNEDRGGMQELI---ALIKDSSIPIICMCND 611
Cdd:COG1474 125 elfdrlyEALDERdgvLVVVLDEIDYLVDDEGDDLLYQLLranEELEGARVGVIGISND 183
|
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
506-527 |
9.35e-04 |
|
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: 40.95 E-value: 9.35e-04
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
25-223 |
1.01e-03 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 43.16 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 25 ETPSKAPKRRKAViissdEDEVVSPPETKKRKASKTASSEDDvvAATP-------EPIAKKARNGQ-KPALSKLKRHV-- 94
Cdd:NF033875 67 ETPKTAVSEEATV-----QKDTTSQPTKVEEVASEKNGAEQS--SATPndttnaqQPTVGAEKSAQeQPVVSPETTNEpl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 95 -DPTELFGGET---KRVIVPKpktkavlEFENEDIDRSLMEVDLDESIKEA-APEKKVHSITRSSPSPKRAKNSSPEPPK 169
Cdd:NF033875 140 gQPTEVAPAENeanKSTSIPK-------EFETPDVDKAVDEAKKDPNITVVeKPAEDLGNVSSKDLAAKEKEVDQLQKEQ 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 62472391 170 PKSTKSKATTPRVKKEKPA---ADLESSVLTDEERHERKRASavlYQKYKNRSSCLN 223
Cdd:NF033875 213 AKKIAQQAAELKAKNEKIAkenAEIAAKNKAEKERYEKEVAE---YNKHKNENGYVN 266
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
506-579 |
1.02e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 42.76 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472391 506 LLSGPPGIGKTTTATLVVKELGFDAVEFNASDTrSKRLLKDEVSTLLSNKSLsgyftgqgqavSRKHVLIMDEV 579
Cdd:PRK13342 40 ILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-GVKDLREVIEEARQRRSA-----------GRRTILFIDEI 101
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
237-310 |
1.25e-03 |
|
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: 38.68 E-value: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62472391 237 LSGLTFVVTGvLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGpKKLAVAEELN-IPILSEDGLFDLIR 310
Cdd:cd17731 3 FKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSG-QKYEFARKWNsIHIVTPEWLYDSIE 75
|
|
| RuvB |
COG2255 |
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ... |
506-527 |
1.46e-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: 41.99 E-value: 1.46e-03
10 20
....*....|....*....|..
gi 62472391 506 LLSGPPGIGKTTTATLVVKELG 527
Cdd:COG2255 58 LLYGPPGLGKTTLAHIIANEMG 79
|
|
| BRCT_PARP4_like |
cd17726 |
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ... |
252-312 |
2.44e-03 |
|
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.
Pssm-ID: 349358 [Multi-domain] Cd Length: 85 Bit Score: 38.04 E-value: 2.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62472391 252 EREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAG--PKKLAVAEELNIPILSEDGLFDLIREK 312
Cdd:cd17726 19 EKKKLKKKITENGGIISYIINKKCTHVVVNNAKAlsSYKCRMAQKYGIPVVSLDYIWKCVEAG 81
|
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
506-527 |
2.52e-03 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 41.27 E-value: 2.52e-03
|
| TIP49 |
COG1224 |
DNA helicase TIP49, TBP-interacting protein [Transcription]; |
503-548 |
7.49e-03 |
|
DNA helicase TIP49, TBP-interacting protein [Transcription];
Pssm-ID: 440837 [Multi-domain] Cd Length: 452 Bit Score: 39.95 E-value: 7.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 62472391 503 KAALLSGPPGIGKTTTATLVVKELGFDA--VEFNASDTRSKRLLKDEV 548
Cdd:COG1224 65 KGILIVGPPGTGKTALAVAIARELGEDTpfVAISGSEIYSAELKKTEF 112
|
|
| HLD_clamp |
cd18133 |
helical lid domain of clamp loader-like AAA+ proteins; Clamp loader complexes are multisubunit ... |
635-692 |
7.80e-03 |
|
helical lid domain of clamp loader-like AAA+ proteins; Clamp loader complexes are multisubunit complexes that play an important role in DNA replication. They open sliding clamps for assembly and close them around DNA, specifically targeting them to sites where DNA synthesis is initiated and orienting them correctly for replication. The subunits belong to the clamp loader clade of AAA+ superfamily.
Pssm-ID: 350838 [Multi-domain] Cd Length: 65 Bit Score: 35.91 E-value: 7.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 62472391 635 EQIKGKIMSICFKEKVKISPAKVEEIIAATNNDIRQSINHIALLSAKEDASQKSGQQV 692
Cdd:cd18133 4 EQLKRRLAAIAEQEKLKLDDAALQALAYISEGDLRKALNALQRAAALGDDGKISLDRV 61
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
503-583 |
8.21e-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: 38.43 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 503 KAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEvstllsnKSLSGYFtgqgqAVSRKH---VLIMDEV 579
Cdd:cd19503 35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE-------KNLREIF-----EEARSHapsIIFIDEI 102
|
....
gi 62472391 580 DGMA 583
Cdd:cd19503 103 DALA 106
|
|
| RNA_helicase |
pfam00910 |
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ... |
506-616 |
8.38e-03 |
|
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
Pssm-ID: 459992 Cd Length: 102 Bit Score: 36.81 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 506 LLSGPPGIGKTTTATLVVKELGfdavefnasdtRSKRLLKDEVSTL-LSNKSLSGYfTGQGqavsrkhVLIMDEVDGMAG 584
Cdd:pfam00910 2 WLYGPPGCGKSTLAKYLARALL-----------KKLGLPKDSVYSRnPDDDFWDGY-TGQP-------VVIIDDFGQNPD 62
|
90 100 110
....*....|....*....|....*....|...
gi 62472391 585 NEDrggMQELIALIkdSSIPII-CMCNDRNHPK 616
Cdd:pfam00910 63 GPD---EAELIRLV--SSTPYPpPMAALEEKGT 90
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
505-617 |
8.98e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 38.31 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472391 505 ALLSGPPGIGKTTTATLVVK---ELGFDAVEFNASDTRSKRLLKD---EVSTLlsnKSLsGYFTGQGQAVSRKHVLIMDE 578
Cdd:pfam13604 21 AVLVGPAGTGKTTALKALREaweAAGYRVIGLAPTGRAAKVLGEElgiPADTI---AKL-LHRLGGRAGLDPGTLLIVDE 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 62472391 579 VdGMAGNEDrggMQELIALIKDSSIPIICMCNDRNHPKI 617
Cdd:pfam13604 97 A-GMVGTRQ---MARLLKLAEDAGARVILVGDPRQLPSV 131
|
|
| BRCT_Rad4_rpt4 |
cd17723 |
fourth BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ... |
239-312 |
9.76e-03 |
|
fourth BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system, which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the fourth one.
Pssm-ID: 349355 [Multi-domain] Cd Length: 74 Bit Score: 36.08 E-value: 9.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62472391 239 GLTFVVTGvLESMEREEAESVIKEYGGKVMTVVGKKLKYLVV-GEEAGPKKLAVAEELNIPILSEDGLFDLIREK 312
Cdd:cd17723 1 GLSISLTG-FSGVDLLHISKLIKLLGAKYHESLTKDRSLLIVnSTEKKSDKINFAKKWGIPVVSVEWLWDCLKEG 74
|
|
|