|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-824 |
0e+00 |
|
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. Enzymatically, it catalyzes the specific insertion of dCMP opposite abasic sites. Rev1 interacts with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7). Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 176455 [Multi-domain] Cd Length: 404 Bit Score: 640.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangidsvlsRAE 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP----------------------------------------------------NSE 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 508 IASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTP 587
Cdd:cd01701 86 IASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 588 DEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKT 667
Cdd:cd01701 166 EELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 668 CGD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEA 745
Cdd:cd01701 246 CGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEE 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7706681 746 TGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 824
Cdd:cd01701 326 SNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-821 |
2.15e-90 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 295.13 E-value: 2.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqang 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 idsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:COG0389 39 ---------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 ILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMES 658
Cdd:COG0389 110 SARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 659 KLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEE 738
Cdd:COG0389 189 KLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAER 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 739 IQRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVG 818
Cdd:COG0389 268 LAERLRRQGLGARTVTVKL---------RTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLG 332
|
...
gi 7706681 819 IHV 821
Cdd:COG0389 333 VRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-757 |
2.11e-72 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 245.41 E-value: 2.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkGKAADipdsslwenpdsaqangidsvl 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV------------------------------GGSPG---------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 504 SRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE----I 579
Cdd:PRK02406 29 RRGVISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcI 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 580 LAETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 659
Cdd:PRK02406 109 GSATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 660 LASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 739
Cdd:PRK02406 184 LHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKL 262
|
330 340
....*....|....*....|
gi 7706681 740 QRRLEATGM--KGKRLTLKI 757
Cdd:PRK02406 263 ERRLERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
4.96e-49 |
|
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.
Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 168.52 E-value: 4.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 7706681 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-622 |
6.57e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 158.89 E-value: 6.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangids 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 502 vlsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASY-THNIEAVSCDEALVDITEiL 580
Cdd:pfam00817 31 ---RGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-L 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 7706681 581 AETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 622
Cdd:pfam00817 107 EKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1157-1250 |
4.76e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 213388 Cd Length: 94 Bit Score: 148.96 E-value: 4.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 1157 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1236
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 7706681 1237 QVVLQQTYGSTLKV 1250
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1167-1248 |
5.27e-17 |
|
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein REV1. It interacts with REV7, POLN, POLK and POLI.
Pssm-ID: 465248 Cd Length: 91 Bit Score: 77.27 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 1167 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1237
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 7706681 1238 VVLQQTYGSTL 1248
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1005-1040 |
5.53e-16 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 72.64 E-value: 5.53e-16
10 20 30
....*....|....*....|....*....|....*.
gi 7706681 1005 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1040
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
929-962 |
1.72e-12 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 62.63 E-value: 1.72e-12
10 20 30
....*....|....*....|....*....|....
gi 7706681 929 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 962
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
45-129 |
5.05e-12 |
|
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.
Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 62.77 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 7706681 125 SYIPY 129
Cdd:pfam16589 80 PLENY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
46-118 |
7.57e-11 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 59.31 E-value: 7.57e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706681 46 STIFSGVAIYVNGYTD-PSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 1 PKLFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
1011-1042 |
3.21e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 36.33 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|..
gi 7706681 1011 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1042
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
933-954 |
7.79e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 35.17 E-value: 7.79e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-824 |
0e+00 |
|
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. Enzymatically, it catalyzes the specific insertion of dCMP opposite abasic sites. Rev1 interacts with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7). Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 176455 [Multi-domain] Cd Length: 404 Bit Score: 640.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangidsvlsRAE 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP----------------------------------------------------NSE 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 508 IASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTP 587
Cdd:cd01701 86 IASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 588 DEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKT 667
Cdd:cd01701 166 EELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 668 CGD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEA 745
Cdd:cd01701 246 CGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEE 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7706681 746 TGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 824
Cdd:cd01701 326 SNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
420-824 |
6.20e-92 |
|
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Known primarily as Pol IV in prokaryotes and Pol kappa in eukaryotes, this polymerase has a propensity for generating frameshift mutations. The eukaryotic Pol kappa differs from Pol IV and Dpo4 by an N-terminal extension of ~75 residues known as the "N-clasp" region. The structure of Pol kappa shows DNA that is almost totally encircled by Pol kappa, with the N-clasp region augmenting the interactions between DNA and the polymerase. Pol kappa is more resistant than Pol eta and Pol iota to bulky guanine adducts and is efficient at catalyzing the incorporation of dCTP. Bacterial pol IV has a higher error rate than other Y-family polymerases.
Pssm-ID: 176459 [Multi-domain] Cd Length: 334 Bit Score: 299.44 E-value: 6.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtGRAPLRpganpqlewqyyqnkilkgkaadipdsslwenpdsaqanGI 499
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAV------GGSSDR---------------------------------------GV 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 500 dsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 579
Cdd:cd03586 36 --------VSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPRFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDY 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 580 LAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 659
Cdd:cd03586 108 VRLFG-SATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 660 LASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 739
Cdd:cd03586 187 LKELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 740 QRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISdMRGVGI 819
Cdd:cd03586 266 AERLRKRGLKGRTVTVKL------------KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGV 329
|
....*
gi 7706681 820 HVNQL 824
Cdd:cd03586 330 RLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-821 |
2.15e-90 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 295.13 E-value: 2.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqang 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 idsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:COG0389 39 ---------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 ILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMES 658
Cdd:COG0389 110 SARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 659 KLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEE 738
Cdd:COG0389 189 KLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAER 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 739 IQRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVG 818
Cdd:COG0389 268 LAERLRRQGLGARTVTVKL---------RTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLG 332
|
...
gi 7706681 819 IHV 821
Cdd:COG0389 333 VRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-757 |
2.11e-72 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 245.41 E-value: 2.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkGKAADipdsslwenpdsaqangidsvl 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV------------------------------GGSPG---------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 504 SRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE----I 579
Cdd:PRK02406 29 RRGVISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcI 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 580 LAETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 659
Cdd:PRK02406 109 GSATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 660 LASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 739
Cdd:PRK02406 184 LHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKL 262
|
330 340
....*....|....*....|
gi 7706681 740 QRRLEATGM--KGKRLTLKI 757
Cdd:PRK02406 263 ERRLERAKPdkRIKTVGVKL 282
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
419-796 |
8.17e-55 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 198.23 E-value: 8.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqa 496
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 497 ngidsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAV-PYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVD 575
Cdd:PRK03348 43 -----------VAGASYEARVFGARSAMPMHQARRLVGNGAVVlPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 576 ITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHS 655
Cdd:PRK03348 112 PAELAGASAEEVEAFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 656 MESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSL 735
Cdd:PRK03348 192 TEEKLHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERI 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7706681 736 SEEIQRRLEATGMKGKRLTLKimVRKPGAPVETakfgghgicdniaRTVTLDQATDNAKII 796
Cdd:PRK03348 272 AEHAHRRLLKDGRGARTVTVK--LRKSDFSTLT-------------RSATLPYATDDAAVL 317
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
421-755 |
4.09e-54 |
|
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Most TLS polymerases are members of the Y-family, including Pol eta, Pol kappa/IV, Pol iota, Rev1, and Pol V, which is found exclusively in bacteria. In eukaryotes, the B-family polymerase Pol zeta also functions as a TLS polymerase. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention.
Pssm-ID: 176453 [Multi-domain] Cd Length: 343 Bit Score: 192.96 E-value: 4.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 421 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangid 500
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNS------------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 501 svlSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIl 580
Cdd:cd00424 33 ---DSTCVIACSYEARKYGVKRGMPVREARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 581 AETKLTPDEFANAVRMEIKDQTK-CAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 659
Cdd:cd00424 109 ARLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 660 LASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 739
Cdd:cd00424 189 LEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKL 268
|
330
....*....|....*.
gi 7706681 740 QRRLEATGMKGKRLTL 755
Cdd:cd00424 269 ARRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
419-774 |
4.01e-50 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 181.45 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqa 496
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGV-------------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 497 ngidsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDI 576
Cdd:PRK14133 41 -----------VSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDI 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 577 TEIlaetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSM 656
Cdd:PRK14133 110 TNI----KEEPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 657 ESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLS 736
Cdd:PRK14133 186 VEKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFS 264
|
330 340 350
....*....|....*....|....*....|....*...
gi 7706681 737 EEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFGGH 774
Cdd:PRK14133 265 NIISEELKKRNLYGKTVTVKI---------KTSDFQTH 293
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
4.96e-49 |
|
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.
Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 168.52 E-value: 4.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 7706681 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
419-804 |
6.44e-48 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 176.76 E-value: 6.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqanG 498
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVAGNEKERK-------------------------------------------G 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 IdsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:PRK01810 44 I--------IVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 ILAetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMES 658
Cdd:PRK01810 116 CYA--LGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 659 KLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLS 736
Cdd:PRK01810 194 KLKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLS 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706681 737 EEIQRRLEATGMKGKrlTLKIMVRkpgapveTAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMF 804
Cdd:PRK01810 273 KSVSKRLQKKTVVSY--NVQIMIR-------YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
419-826 |
4.34e-45 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 168.64 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSnrgtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpDSAQANG 498
Cdd:PRK03103 5 ILLVDMQSFYASVEKAANPELKGRPVIVSG-------------------------------------------DPERRSG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 IdsVLsraeiASCsYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:PRK03103 42 V--VL-----AAC-PLAKAYGVKTAERLWEAQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 ILaetKL--TPDEFANAVRMEIKDQTKCAASVGIGSNILLARMAT---RKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVG 653
Cdd:PRK03103 114 SQ---KLfgSPLEIAQKIQQRIMRETGVYARVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 654 HSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAF 731
Cdd:PRK03103 191 SRMEKHLRRMGIRTIGQLANTPLERLKKRWG-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 732 LLSLSEEIQRRLEATGMKGKrlTLKIMVRkpGAPVETAKfgghgicdNIARTVTLDQATDNAKIIGKAMLNMFHTMkLNI 811
Cdd:PRK03103 270 LLELCEEVCRRARAKGYMGR--TVSVSLR--GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDG 336
|
410
....*....|....*
gi 7706681 812 SDMRGVGIHVNQLVP 826
Cdd:PRK03103 337 KPVRRVGVTLSNLVS 351
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-622 |
6.57e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 158.89 E-value: 6.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangids 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 502 vlsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASY-THNIEAVSCDEALVDITEiL 580
Cdd:pfam00817 31 ---RGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-L 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 7706681 581 AETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 622
Cdd:pfam00817 107 EKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
412-801 |
8.69e-43 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 162.02 E-value: 8.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 412 SPR-------HQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGRaplrpganpqlewqyyqnkilkgkaadipd 484
Cdd:PRK02794 24 SPRlvrhpelYTLSIAHIDCDAFYASVEKRDNPELRDKPVII----GGGK------------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 485 sslwenpdsaqangidsvlsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNI 564
Cdd:PRK02794 70 --------------------RGVVSTACYIARIHGVRSAMPMFKALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 565 EAVSCDEALVDI--TEIL--AETKLTPDEFANAVRMEIKdqtkCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDF 640
Cdd:PRK02794 130 EPLSIDEAFLDLsgTERLhgAPPAVVLARFARRVEREIG----ITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 641 IRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGI 720
Cdd:PRK02794 206 LAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFET 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 721 RFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFGGHgicdniARTVTLDQATDNAKII---G 797
Cdd:PRK02794 285 DLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKL---------KTADFRLR------TRRRTLEDPTQLADRIfrtA 349
|
....
gi 7706681 798 KAML 801
Cdd:PRK02794 350 RELL 353
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1157-1250 |
4.76e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 213388 Cd Length: 94 Bit Score: 148.96 E-value: 4.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 1157 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1236
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 7706681 1237 QVVLQQTYGSTLKV 1250
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
419-757 |
6.06e-41 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 154.80 E-value: 6.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrGTGraplrpganpqlewqyyqnkilkgkaadipdsslwenpDSAQAng 498
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIVG---GNG--------------------------------------DPTEP-- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 idsvlsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVdite 578
Cdd:PRK03352 44 ------RKVVTCASYEARAFGVRAGMPLRTAARRCPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFL---- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 iLAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMES 658
Cdd:PRK03352 114 -GVDTD-DPEALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 659 KLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSE 737
Cdd:PRK03352 192 RLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELAR 271
|
330 340
....*....|....*....|
gi 7706681 738 EIQRRLEATGMKGKRLTLKI 757
Cdd:PRK03352 272 RVLDEVVAEGRPVTRVAVKV 291
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
419-791 |
2.06e-40 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 154.76 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqang 498
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIV----GGG--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 idSVLSraeiasCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:PRK03858 37 --VVLA------ASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 iLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMES 658
Cdd:PRK03858 109 -LRRISGTPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 659 KLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEE 738
Cdd:PRK03858 188 KLRAHGITTVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDR 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 7706681 739 IQRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHGicdNIARTVTLDQATD 791
Cdd:PRK03858 268 VARRMRAAGRTGRTVVLRL------------RFDDFT---RATRSHTLPRPTA 305
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
419-711 |
2.94e-34 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 135.30 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwENPDSAQang 498
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSG-------------------------------------RFEDSGA--- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 499 idsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:PRK01216 43 ---------VATANYEARKLGIKAGMPIVEAKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 ILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMES 658
Cdd:PRK01216 114 KVKNYQ-DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAE 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 7706681 659 KLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTeKERKS 711
Cdd:PRK01216 193 KLKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRA-RVRKS 244
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
420-757 |
2.29e-32 |
|
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion synthesis (TLS) polymerase that consists of the heterotrimer of one umuC and two umuD subunits. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Pol V, RecA, single stranded DNA-binding protein, beta sliding clamp, and gamma clamp loading complex are responsible for inducing the SOS response in bacteria to repair UV-induced DNA damage.
Pssm-ID: 176454 [Multi-domain] Cd Length: 344 Bit Score: 129.59 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgraplrpganpqlewqyyqnkilkgkaADIpdsslwenpdsaqangi 499
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSN------------------------------NDG----------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 500 dSVLSRaeiascSYEARQLGIKNGMFFGHAKQLCP--NLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDIT 577
Cdd:cd01700 34 -CVIAR------SPEAKALGIKMGSPYFKVPDLLErhGVAVFSSNYALYGDMSRRIMSILERFSPDVEVYSIDESFLDLT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 578 EILaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAK----PDGQYHLKPEEVDDFIRGQL-VTNLPGV 652
Cdd:cd01700 107 GSL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLANDLAKkknpYGGVVDLTDEEVRDKLLKILpVGDVWGI 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 653 GHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEAF 731
Cdd:cd01700 185 GRRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELNGIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQA 263
|
330 340
....*....|....*....|....*.
gi 7706681 732 LLSLSEEIQRRLEATGMKGKRLTLKI 757
Cdd:cd01700 264 LAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
421-806 |
3.33e-31 |
|
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Unlike other Y-family members, Pol eta can efficiently and accurately replicate DNA past UV-induced lesions. Its activity is initiated by two simultaneous interactions: the PIP box in pol eta interacting with PCNA, and the UBZ (ubiquitin-binding zinc finger) in pol eta interacting with monoubiquitin attached to PCNA. Pol eta is more efficient in copying damaged DNA than undamaged DNA and seems to recognize when a lesion has been passed, facilitating a lesion-dependent dissociation from the DNA.
Pssm-ID: 176456 [Multi-domain] Cd Length: 359 Bit Score: 126.66 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsAQANGID 500
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAV-----------------------------------------------VQWNSII 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 501 SVlsraeiascSYEARQLGIKNGMFFGHAKQLCPNLQ----------AVPYDFHA-------------YKEVAQTLYETL 557
Cdd:cd01702 35 AV---------SYAARAFGVTRFMTIDEAKKKCPDLIlahvatykkgEDEADYHEnpsparhkvsldpYRRASRKILNIL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 558 ASYTHNIEAVSCDEALVDITEILAETkltpdefanaVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEV 637
Cdd:cd01702 106 KRFGDVVEKASIDEAYLDLGSRIVEE----------IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 638 DDFIRGQLVTNLPGVGHSM-ESKLASLGIKTCGDLQYM--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSA 714
Cdd:cd01702 176 ASFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 715 EINY-GIRFTQPKEAEAFLLSLSEEIQRRLE----ATGMKGKRLTLKIMVRKPGAPVEtakfgghgICDNIARTVTLDQA 789
Cdd:cd01702 256 SKNFpGKTALSTEDVQHWLLVLASELNSRLEddryENNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYDAQKIV 327
|
410
....*....|....*..
gi 7706681 790 TDNAKIIGKAMLNMFHT 806
Cdd:cd01702 328 KDAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
421-762 |
5.69e-28 |
|
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Pol iota is thought to be one of the least efficient polymerases, particularly when opposite pyrimidines; it can incorporate the correct nucleotide opposite a purine much more efficiently than opposite a pyrimidine, and prefers to insert guanosine instead of adenosine opposite thymidine. Pol iota is believed to use Hoogsteen rather than Watson-Crick base pairing, which may explain the varying efficiency for different template nucleotides.
Pssm-ID: 176457 [Multi-domain] Cd Length: 379 Bit Score: 117.57 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyQNKILkgkaadipdsslwenpdsaqangid 500
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGI------------------------QQKYI------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 501 svlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVP-YDFHAYKEVAQTLYETLASYTHN--IEAVSCDEALVDIT 577
Cdd:cd01703 33 -------VVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNgEDLTPFRDMSKKVYRLLRSYSWNdrVERLGFDENFMDVT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 578 EIlaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFI--RGQL-VTNLPGVGH 654
Cdd:cd01703 106 EM---RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPPSCADLMdfMDLHdLRKIPGIGY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 655 SMESKLASLGIKTCGDLQ---------------YMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINY 718
Cdd:cd01703 183 KTAAKLEAHGISSVRDLQefsnrnrqtvgaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSY 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 7706681 719 G-IRFTQPKEAEAFLLSLSEEIQRRL------EATGMKGKRLTLKIMVRKP 762
Cdd:cd01703 263 KkCSLEEIREARNKIEELLASLLERMkqdlqeVKAGDGRRPHTLRLTLRRY 313
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
508-756 |
1.10e-24 |
|
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention.
Pssm-ID: 176458 [Multi-domain] Cd Length: 335 Bit Score: 106.70 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 508 IASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYD----FHAYKEVAQTLYEtlasYTHNIEAVSCDEALVDITeilAET 583
Cdd:cd03468 36 ILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDpeadARALQELALWLLR----FTPLVALDGPDGLLLDVT---GCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 584 KLTPDEFANAVRMEIKDQTKC-AASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLAS 662
Cdd:cd03468 109 HLFGGEDALAASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 663 LGIKTCGDLQYMTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQ 740
Cdd:cd03468 189 LGLRTLGDLAALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLC 265
|
250
....*....|....*.
gi 7706681 741 RRLEATGMKGKRLTLK 756
Cdd:cd03468 266 AFLALRGLGARRLSLT 281
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
410-757 |
2.66e-23 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 105.87 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 410 LNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkgkaadipdsslwe 489
Cdd:PTZ00205 126 LEATRRLGTYIHLDMDMFYAAVEIKKHPEYAAIPLAI------------------------------------------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 490 npdsaqanGIDSVLSRAeiascSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSC 569
Cdd:PTZ00205 163 --------GTMTMLQTA-----NYVARGRGIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 570 DEALVDITEILA--ETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLK---PEEVDDFIRGQ 644
Cdd:PTZ00205 230 DELTLEVSAYIErfEGTKTAEDVASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 645 LVTNLPGVGHSMESKLASLGIKTCGD-------LQYMTMAKLQK-EFGPKTGQMLY-RFCRGLDDRPVR--TEKERKSVS 713
Cdd:PTZ00205 310 GLRSVPGVGKVTEALLKGLGITTLSDiynrrveLCYILHNNLFRfLLGASIGIMQWpDAATAANTENCEgaTGGQRKAIS 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 7706681 714 AEINYGIrFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 757
Cdd:PTZ00205 390 SERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKSELMCRQISLTI 432
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
709-828 |
1.97e-20 |
|
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
Pssm-ID: 463354 [Multi-domain] Cd Length: 104 Bit Score: 87.61 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 709 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMvrkpgapveTAKFgghgicDNIARTVTLDQ 788
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 7706681 789 ATDNAKIIGKAMLNMFHTMKLNIsDMRGVGIHVNQLVPTN 828
Cdd:pfam11799 66 PTDDTDEIYRAALRLLRRLYRGR-PVRLLGVSLSNLVPEG 104
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1167-1248 |
5.27e-17 |
|
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein REV1. It interacts with REV7, POLN, POLK and POLI.
Pssm-ID: 465248 Cd Length: 91 Bit Score: 77.27 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 1167 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1237
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 7706681 1238 VVLQQTYGSTL 1248
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1005-1040 |
5.53e-16 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 72.64 E-value: 5.53e-16
10 20 30
....*....|....*....|....*....|....*.
gi 7706681 1005 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1040
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
929-962 |
1.72e-12 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 62.63 E-value: 1.72e-12
10 20 30
....*....|....*....|....*....|....
gi 7706681 929 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 962
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
45-129 |
5.05e-12 |
|
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.
Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 62.77 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 7706681 125 SYIPY 129
Cdd:pfam16589 80 PLENY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
46-118 |
7.57e-11 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 59.31 E-value: 7.57e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706681 46 STIFSGVAIYVNGYTD-PSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 1 PKLFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
46-118 |
8.54e-11 |
|
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: 58.84 E-value: 8.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7706681 46 STIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKELK-GEKVIRPEWIVESI 118
Cdd:pfam00533 3 EKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSK-KTTHVIVEARTKKYLKAKElGIPIVTEEWLLDCI 75
|
|
| BRCT_DNA_ligase_III |
cd18431 |
BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ... |
48-124 |
1.33e-10 |
|
BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ligase III, or polydeoxyribonucleotide synthase [ATP] 3, functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.
Pssm-ID: 349384 [Multi-domain] Cd Length: 78 Bit Score: 58.48 E-value: 1.33e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706681 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATnlpNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:cd18431 4 IFTGVKVYLPGSVEDDYKKLKRYFIAYDGDVVEEYDEEDATHVVVD---RDDKLGNPSAKVVSPEWLWDCIKKQKLV 77
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
421-723 |
4.19e-09 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 60.16 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 421 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRgtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqaNGId 500
Cdd:PRK03609 4 LCDVNSFYASCETVFRPDLRGKPVVVLSNN----------------------------------------------DGC- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 501 svlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPY--DFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 578
Cdd:PRK03609 37 -------VIARSAEAKALGIKMGDPWFKQKDLFRRCGVVCFssNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 579 IlaETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKP-DGQYH-----LKPEEVDDFIRGQLVTNLPGV 652
Cdd:PRK03609 110 V--RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAKKwQRQTGgvvdlSNLERQRKLLSLQPVEEVWGV 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7706681 653 GHSMESKLASLGIKTCGDLQYMTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 723
Cdd:PRK03609 188 GRRISKKLNAMGIKTALDLADTNIRFIRKHF----NVVLERTVRELRGEPCLSLEEFAPTKQEIvcsrSFGERIT 258
|
|
| BRCT_DNA_ligase_IV_rpt1 |
cd17722 |
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ... |
48-132 |
8.42e-09 |
|
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the first one.
Pssm-ID: 349354 [Multi-domain] Cd Length: 90 Bit Score: 53.84 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 48 IFSGVAIYV-NGYTDP-SAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 7706681 123 LLSYIPYQLY 132
Cdd:cd17722 80 LLPLEPKYMI 89
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
54-117 |
8.93e-08 |
|
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: 50.05 E-value: 8.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706681 54 IYVNGYTDPSAEELRKLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVES 117
Cdd:cd00027 3 ICFSGLDDEEREELKKLIEALGGKVSESLSS-KVTHLIAKSPSGEKYYLAalaWGIPIVSPEWLLDC 68
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
48-121 |
3.32e-07 |
|
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.
Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 49.08 E-value: 3.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706681 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17731 2 PFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKN-CTHLIAGSPSGQKYEfarKWNSIHIVTPEWLYDSIEAG 77
|
|
| BRCT_PAXIP1_rpt2 |
cd17710 |
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
48-125 |
8.77e-07 |
|
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.
Pssm-ID: 349342 [Multi-domain] Cd Length: 81 Bit Score: 48.00 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 48 IFSGVAIYVNGYtdpSAEELRKL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 7706681 122 RLLS 125
Cdd:cd17710 77 TLLD 80
|
|
| BRCT_XRCC1_rpt1 |
cd17725 |
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ... |
51-129 |
2.36e-06 |
|
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one.
Pssm-ID: 349357 [Multi-domain] Cd Length: 80 Bit Score: 46.50 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 51 GVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSYIP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 7706681 129 Y 129
Cdd:cd17725 80 Y 80
|
|
| BRCT_TopBP1_rpt3 |
cd17718 |
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
44-122 |
1.37e-05 |
|
third 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 third BRCT domain.
Pssm-ID: 349350 Cd Length: 83 Bit Score: 44.51 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 44 TSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 7706681 120 AGR 122
Cdd:cd17718 81 QGK 83
|
|
| BRCT_PAXIP1_rpt1 |
cd17714 |
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; ... |
49-125 |
3.17e-05 |
|
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the first BRCT domain.
Pssm-ID: 349346 Cd Length: 76 Bit Score: 43.46 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 49 FSGVAIYVNGYTDPSAEELRKlmmlHGGQYHVYYSRSKTTHIIATNLPNAKIKELK--GEK-VIRPEWIVESIKAGRLLS 125
Cdd:cd17714 1 FKDVKYFVVGNLDEKVEQLLK----NGGAKEVSYLSDMATHVIVDDNDNPEVGEARdlFELpVVTSSWVILSIKAGKLLP 76
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
54-113 |
9.21e-04 |
|
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.
Pssm-ID: 463687 [Multi-domain] Cd Length: 63 Bit Score: 38.72 E-value: 9.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706681 54 IYVNGYTDPSAEELRKLMMLHGGQYHVYYSRsKTTHIIAtnlpnakiKELKGEK----------VIRPEW 113
Cdd:pfam12738 3 ICVTGFDGDDREGLQKLIEAMGAEYTKDLTK-SVTHLIC--------KSGEGEKyekakewgipVVSPLW 63
|
|
| BRCT_Rad4_rpt2 |
cd17746 |
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ... |
62-131 |
2.51e-03 |
|
second 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 second one.
Pssm-ID: 349377 [Multi-domain] Cd Length: 91 Bit Score: 38.37 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7706681 62 PSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIK-ELK-GEKVIRPEWIVESIKAGRLLSYIPYQL 131
Cdd:cd17746 20 PERSRIENYVLKHGGTFCPDLTRD-VTHLIAGTSSGRKYEyALKwKINVVCVEWLWQSIQRNAVLEPQYFQL 90
|
|
| IMS_HHH |
pfam11798 |
IMS family HHH motif; These proteins are involved in UV protection, eg. |
634-665 |
2.70e-03 |
|
IMS family HHH motif; These proteins are involved in UV protection, eg.
Pssm-ID: 432081 [Multi-domain] Cd Length: 32 Bit Score: 36.61 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|..
gi 7706681 634 PEEVDDFIRGQLVTNLPGVGHSMESKLASLGI 665
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
1011-1042 |
3.21e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 36.33 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|..
gi 7706681 1011 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1042
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
933-954 |
7.79e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 35.17 E-value: 7.79e-03
|
| |
