|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-823 |
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: 640.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsvlsRAEI 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP---------------------------------------------------NSEI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 508 ASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPD 587
Cdd:cd01701 87 ASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 588 EFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTC 667
Cdd:cd01701 167 ELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 668 GD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAT 745
Cdd:cd01701 247 GGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEES 326
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84043967 746 GMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 823
Cdd:cd01701 327 NVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-820 |
1.55e-90 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 295.51 E-value: 1.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangi 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 578
Cdd:COG0389 39 --------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 658
Cdd:COG0389 111 ARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 659 LASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 738
Cdd:COG0389 190 LARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 739 QRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGI 818
Cdd:COG0389 269 AERLRRQGLGARTVTVKL---------RTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGV 333
|
..
gi 84043967 819 HV 820
Cdd:COG0389 334 RL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-756 |
1.82e-72 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 245.41 E-value: 1.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpGanpqlewqyyqnkilkGKADipdsslwenpdsaqangidsvlS 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV-------------G----------------GSPG----------------------R 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 504 RAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE----IL 579
Cdd:PRK02406 30 RGVISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 580 AETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKL 659
Cdd:PRK02406 110 SATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 660 ASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQ 739
Cdd:PRK02406 185 HALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLE 263
|
330
....*....|....*....
gi 84043967 740 RRLEATGM--KGKRLTLKI 756
Cdd:PRK02406 264 RRLERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
4.95e-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: 4.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 84043967 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-621 |
4.81e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 159.28 E-value: 4.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsv 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 502 lsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASY-THNIEAVSCDEALVDITEiLA 580
Cdd:pfam00817 31 --RGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 84043967 581 ETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 621
Cdd:pfam00817 108 KLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1156-1249 |
4.75e-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: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 1156 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1235
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 84043967 1236 QVVLQQTYGSTLKV 1249
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 ... |
1166-1247 |
5.26e-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: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 1166 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1236
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 84043967 1237 VVLQQTYGSTL 1247
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1004-1039 |
5.47e-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: 5.47e-16
10 20 30
....*....|....*....|....*....|....*.
gi 84043967 1004 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1039
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
928-961 |
1.71e-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: 1.71e-12
10 20 30
....*....|....*....|....*....|....
gi 84043967 928 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 961
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 84043967 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 84043967 125 SYIPY 129
Cdd:pfam16589 80 PLENY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
46-118 |
7.56e-11 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 59.31 E-value: 7.56e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84043967 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 ... |
1010-1041 |
3.18e-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: 3.18e-03
10 20 30
....*....|....*....|....*....|..
gi 84043967 1010 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1041
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
932-953 |
7.70e-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: 7.70e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-823 |
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: 640.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsvlsRAEI 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP---------------------------------------------------NSEI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 508 ASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPD 587
Cdd:cd01701 87 ASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 588 EFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTC 667
Cdd:cd01701 167 ELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 668 GD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAT 745
Cdd:cd01701 247 GGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEES 326
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84043967 746 GMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 823
Cdd:cd01701 327 NVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
420-823 |
4.45e-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: 299.82 E-value: 4.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtGRAPLRpganpqlewqyyqnkilkgkadipdsslwenpdsaqanGId 499
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAV------GGSSDR--------------------------------------GV- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 500 svlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIL 579
Cdd:cd03586 36 -------VSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPRFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 580 AETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKL 659
Cdd:cd03586 109 RLFG-SATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 660 ASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQ 739
Cdd:cd03586 188 KELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEELA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 740 RRLEATGMKGKRLTLKImvrkpgapvetaKFGGHgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISdMRGVGIH 819
Cdd:cd03586 267 ERLRKRGLKGRTVTVKL------------KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVR 330
|
....
gi 84043967 820 VNQL 823
Cdd:cd03586 331 LSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-820 |
1.55e-90 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 295.51 E-value: 1.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangi 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 578
Cdd:COG0389 39 --------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 658
Cdd:COG0389 111 ARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 659 LASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 738
Cdd:COG0389 190 LARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 739 QRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGI 818
Cdd:COG0389 269 AERLRRQGLGARTVTVKL---------RTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGV 333
|
..
gi 84043967 819 HV 820
Cdd:COG0389 334 RL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-756 |
1.82e-72 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 245.41 E-value: 1.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpGanpqlewqyyqnkilkGKADipdsslwenpdsaqangidsvlS 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV-------------G----------------GSPG----------------------R 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 504 RAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE----IL 579
Cdd:PRK02406 30 RGVISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 580 AETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKL 659
Cdd:PRK02406 110 SATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 660 ASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQ 739
Cdd:PRK02406 185 HALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLE 263
|
330
....*....|....*....
gi 84043967 740 RRLEATGM--KGKRLTLKI 756
Cdd:PRK02406 264 RRLERAKPdkRIKTVGVKL 282
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
419-795 |
6.02e-55 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 198.62 E-value: 6.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqan 496
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 497 gidsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAV-PYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDI 575
Cdd:PRK03348 43 ----------VAGASYEARVFGARSAMPMHQARRLVGNGAVVlPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 576 TEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSM 655
Cdd:PRK03348 113 AELAGASAEEVEAFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 656 ESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLS 735
Cdd:PRK03348 193 EEKLHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIA 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 736 EEIQRRLEATGMKGKRLTLKimVRKPGAPVETakfgghgicdniaRTVTLDQATDNAKII 795
Cdd:PRK03348 273 EHAHRRLLKDGRGARTVTVK--LRKSDFSTLT-------------RSATLPYATDDAAVL 317
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
421-754 |
3.01e-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: 193.35 E-value: 3.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 421 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangids 500
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNS------------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 501 vlSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlA 580
Cdd:cd00424 33 --DSTCVIACSYEARKYGVKRGMPVREARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS-A 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 581 ETKLTPDEFANAVRMEIKDQTK-CAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKL 659
Cdd:cd00424 110 RLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 660 ASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQ 739
Cdd:cd00424 190 EAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLA 269
|
330
....*....|....*
gi 84043967 740 RRLEATGMKGKRLTL 754
Cdd:cd00424 270 RRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
419-773 |
3.06e-50 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 181.84 E-value: 3.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqan 496
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGV-------------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 497 gidsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDIT 576
Cdd:PRK14133 41 ----------VSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDIT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 577 EIlaetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSME 656
Cdd:PRK14133 111 NI----KEEPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 657 SKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSE 736
Cdd:PRK14133 187 EKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSN 265
|
330 340 350
....*....|....*....|....*....|....*..
gi 84043967 737 EIQRRLEATGMKGKRLTLKImvrkpgapvETAKFGGH 773
Cdd:PRK14133 266 IISEELKKRNLYGKTVTVKI---------KTSDFQTH 293
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
4.95e-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: 4.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 84043967 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
419-803 |
4.75e-48 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 177.14 E-value: 4.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqanGI 498
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVAGNEKERK------------------------------------------GI 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 578
Cdd:PRK01810 45 --------IVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDC 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LAetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 658
Cdd:PRK01810 117 YA--LGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 659 LASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSE 736
Cdd:PRK01810 195 LKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSK 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84043967 737 EIQRRLEATGMKGKrlTLKIMVRkpgapveTAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMF 803
Cdd:PRK01810 274 SVSKRLQKKTVVSY--NVQIMIR-------YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
419-825 |
3.20e-45 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 169.03 E-value: 3.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSnrgtgraplrpganpqlewqyyqnkilkgkadipdsslwenpDSAQANGI 498
Cdd:PRK03103 5 ILLVDMQSFYASVEKAANPELKGRPVIVSG------------------------------------------DPERRSGV 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dsVLsraeiASCsYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 578
Cdd:PRK03103 43 --VL-----AAC-PLAKAYGVKTAERLWEAQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LaetKL--TPDEFANAVRMEIKDQTKCAASVGIGSNILLARMAT---RKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGH 653
Cdd:PRK03103 115 Q---KLfgSPLEIAQKIQQRIMRETGVYARVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 654 SMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFL 731
Cdd:PRK03103 192 RMEKHLRRMGIRTIGQLANTPLERLKKRWG-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 732 LSLSEEIQRRLEATGMKGKrlTLKIMVRkpGAPVETAKfgghgicdNIARTVTLDQATDNAKIIGKAMLNMFHTMkLNIS 811
Cdd:PRK03103 271 LELCEEVCRRARAKGYMGR--TVSVSLR--GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGK 337
|
410
....*....|....
gi 84043967 812 DMRGVGIHVNQLVP 825
Cdd:PRK03103 338 PVRRVGVTLSNLVS 351
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-621 |
4.81e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 159.28 E-value: 4.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsv 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 502 lsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASY-THNIEAVSCDEALVDITEiLA 580
Cdd:pfam00817 31 --RGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 84043967 581 ETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 621
Cdd:pfam00817 108 KLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
412-800 |
6.42e-43 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 162.41 E-value: 6.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 412 SPR-------HQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGRaplrpganpqlewqyyqnkilkgkadipds 484
Cdd:PRK02794 24 SPRlvrhpelYTLSIAHIDCDAFYASVEKRDNPELRDKPVII----GGGK------------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 485 slwenpdsaqangidsvlsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIE 564
Cdd:PRK02794 70 -------------------RGVVSTACYIARIHGVRSAMPMFKALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLVE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 565 AVSCDEALVDI--TEIL--AETKLTPDEFANAVRMEIKdqtkCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFI 640
Cdd:PRK02794 131 PLSIDEAFLDLsgTERLhgAPPAVVLARFARRVEREIG----ITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 641 RGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIR 720
Cdd:PRK02794 207 APKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 721 FTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFGGHgicdniARTVTLDQATDNAKII---GK 797
Cdd:PRK02794 286 LSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKL---------KTADFRLR------TRRRTLEDPTQLADRIfrtAR 350
|
...
gi 84043967 798 AML 800
Cdd:PRK02794 351 ELL 353
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1156-1249 |
4.75e-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: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 1156 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1235
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 84043967 1236 QVVLQQTYGSTLKV 1249
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
419-756 |
4.46e-41 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 155.18 E-value: 4.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrGTGraplrpganpqlewqyyqnkilkgkadipdsslwenpDSAQAngi 498
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIVG---GNG-------------------------------------DPTEP--- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dsvlsRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVditei 578
Cdd:PRK03352 44 -----RKVVTCASYEARAFGVRAGMPLRTAARRCPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFL----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 658
Cdd:PRK03352 114 GVDTD-DPEALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 659 LASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSEE 737
Cdd:PRK03352 193 LAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELARR 272
|
330
....*....|....*....
gi 84043967 738 IQRRLEATGMKGKRLTLKI 756
Cdd:PRK03352 273 VLDEVVAEGRPVTRVAVKV 291
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
419-790 |
1.52e-40 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 155.14 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangi 498
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIV----GGG--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dSVLSraeiasCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEi 578
Cdd:PRK03858 37 -VVLA------ASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 658
Cdd:PRK03858 109 LRRISGTPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 659 LASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 738
Cdd:PRK03858 189 LRAHGITTVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRV 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 84043967 739 QRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHGicdNIARTVTLDQATD 790
Cdd:PRK03858 269 ARRMRAAGRTGRTVVLRL------------RFDDFT---RATRSHTLPRPTA 305
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
419-710 |
2.17e-34 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 135.69 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwENPDSAQangi 498
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSG------------------------------------RFEDSGA---- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 499 dsvlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 578
Cdd:PRK01216 43 --------VATANYEARKLGIKAGMPIVEAKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 LAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESK 658
Cdd:PRK01216 115 VKNYQ-DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEK 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 84043967 659 LASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTeKERKS 710
Cdd:PRK01216 194 LKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRA-RVRKS 244
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
420-756 |
1.69e-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: 129.98 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgraplrpganpqlewqyyqnkilkgkADIpdsslwenpdsaqangid 499
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSN-----------------------------NDG------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 500 SVLSRaeiascSYEARQLGIKNGMFFGHAKQLCP--NLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE 577
Cdd:cd01700 34 CVIAR------SPEAKALGIKMGSPYFKVPDLLErhGVAVFSSNYALYGDMSRRIMSILERFSPDVEVYSIDESFLDLTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 578 ILaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAK----PDGQYHLKPEEVDDFIRGQL-VTNLPGVG 652
Cdd:cd01700 108 SL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLANDLAKkknpYGGVVDLTDEEVRDKLLKILpVGDVWGIG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 653 HSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEAFL 731
Cdd:cd01700 186 RRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELNGIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQAL 264
|
330 340
....*....|....*....|....*
gi 84043967 732 LSLSEEIQRRLEATGMKGKRLTLKI 756
Cdd:cd01700 265 AEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
421-805 |
2.46e-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: 127.04 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsAQANGIDS 500
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAV----------------------------------------------VQWNSIIA 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 501 VlsraeiascSYEARQLGIKNGMFFGHAKQLCPNLQ----------AVPYDFHA-------------YKEVAQTLYETLA 557
Cdd:cd01702 36 V---------SYAARAFGVTRFMTIDEAKKKCPDLIlahvatykkgEDEADYHEnpsparhkvsldpYRRASRKILNILK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 558 SYTHNIEAVSCDEALVDITEILAETkltpdefanaVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVD 637
Cdd:cd01702 107 RFGDVVEKASIDEAYLDLGSRIVEE----------IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 638 DFIRGQLVTNLPGVGHSM-ESKLASLGIKTCGDLQYM--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAE 714
Cdd:cd01702 177 SFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSS 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 715 INY-GIRFTQPKEAEAFLLSLSEEIQRRLE----ATGMKGKRLTLKIMVRKPGAPVEtakfgghgICDNIARTVTLDQAT 789
Cdd:cd01702 257 KNFpGKTALSTEDVQHWLLVLASELNSRLEddryENNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYDAQKIVK 328
|
410
....*....|....*.
gi 84043967 790 DNAKIIGKAMLNMFHT 805
Cdd:cd01702 329 DAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
421-761 |
4.42e-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: 117.96 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyQNKILkgkadipdsslwenpdsaqangids 500
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGI------------------------QQKYI------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 501 vlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVP-YDFHAYKEVAQTLYETLASYTHN--IEAVSCDEALVDITE 577
Cdd:cd01703 33 ------VVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNgEDLTPFRDMSKKVYRLLRSYSWNdrVERLGFDENFMDVTE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 578 IlaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFI--RGQL-VTNLPGVGHS 654
Cdd:cd01703 107 M---RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPPSCADLMdfMDLHdLRKIPGIGYK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 655 MESKLASLGIKTCGDLQ---------------YMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINYG 718
Cdd:cd01703 184 TAAKLEAHGISSVRDLQefsnrnrqtvgaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSYK 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 84043967 719 -IRFTQPKEAEAFLLSLSEEIQRRL------EATGMKGKRLTLKIMVRKP 761
Cdd:cd01703 264 kCSLEEIREARNKIEELLASLLERMkqdlqeVKAGDGRRPHTLRLTLRRY 313
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
507-755 |
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 84043967 507 IASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYD----FHAYKEVAQTLYEtlasYTHNIEAVSCDEALVDITeilAET 582
Cdd:cd03468 36 ILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDpeadARALQELALWLLR----FTPLVALDGPDGLLLDVT---GCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 583 KLTPDEFANAVRMEIKDQTKC-AASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLAS 661
Cdd:cd03468 109 HLFGGEDALAASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 662 LGIKTCGDLQYMTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQ 739
Cdd:cd03468 189 LGLRTLGDLAALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLC 265
|
250
....*....|....*.
gi 84043967 740 RRLEATGMKGKRLTLK 755
Cdd:cd03468 266 AFLALRGLGARRLSLT 281
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
410-756 |
2.01e-23 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 106.26 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 410 LNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkgkadipdsslwen 489
Cdd:PTZ00205 126 LEATRRLGTYIHLDMDMFYAAVEIKKHPEYAAIPLAI------------------------------------------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 490 pdsaqanGIDSVLSRAeiascSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCD 569
Cdd:PTZ00205 163 -------GTMTMLQTA-----NYVARGRGIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 570 EALVDITEILA--ETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLK---PEEVDDFIRGQL 644
Cdd:PTZ00205 231 ELTLEVSAYIErfEGTKTAEDVASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 645 VTNLPGVGHSMESKLASLGIKTCGD-------LQYMTMAKLQK-EFGPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSA 713
Cdd:PTZ00205 311 LRSVPGVGKVTEALLKGLGITTLSDiynrrveLCYILHNNLFRfLLGASIGIMQWpDAATAANTENCEgaTGGQRKAISS 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 84043967 714 EINYGIrFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 756
Cdd:PTZ00205 391 ERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKSELMCRQISLTI 432
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
708-827 |
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 84043967 708 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMvrkpgapveTAKFgghgicDNIARTVTLDQ 787
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 84043967 788 ATDNAKIIGKAMLNMFHTMKLNIsDMRGVGIHVNQLVPTN 827
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 ... |
1166-1247 |
5.26e-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: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 1166 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1236
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 84043967 1237 VVLQQTYGSTL 1247
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1004-1039 |
5.47e-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: 5.47e-16
10 20 30
....*....|....*....|....*....|....*.
gi 84043967 1004 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1039
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
928-961 |
1.71e-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: 1.71e-12
10 20 30
....*....|....*....|....*....|....
gi 84043967 928 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 961
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 84043967 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 84043967 125 SYIPY 129
Cdd:pfam16589 80 PLENY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
46-118 |
7.56e-11 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 59.31 E-value: 7.56e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84043967 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 84043967 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 |
1.32e-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: 1.32e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84043967 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATnlpNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:cd18431 4 IFTGVKVYLPGSVEDDYKKLKRYFIAYDGDVVEEYDEEDATHVVVD---RDDKLGNPSAKVVSPEWLWDCIKKQKLV 77
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
421-722 |
3.17e-09 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 60.55 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 421 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRgtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqaNGIds 500
Cdd:PRK03609 4 LCDVNSFYASCETVFRPDLRGKPVVVLSNN---------------------------------------------DGC-- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 501 vlsraeIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPY--DFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEI 578
Cdd:PRK03609 37 ------VIARSAEAKALGIKMGDPWFKQKDLFRRCGVVCFssNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 579 laETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKP-DGQYH-----LKPEEVDDFIRGQLVTNLPGVG 652
Cdd:PRK03609 111 --RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAKKwQRQTGgvvdlSNLERQRKLLSLQPVEEVWGVG 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84043967 653 HSMESKLASLGIKTCGDLQYMTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 722
Cdd:PRK03609 189 RRISKKLNAMGIKTALDLADTNIRFIRKHF----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 |
8.58e-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: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 48 IFSGVAIYV-NGYTDP-SAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 84043967 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 |
8.92e-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: 8.92e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84043967 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 84043967 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 |
8.76e-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: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84043967 48 IFSGVAIYVNGYtdpSAEELRKL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 84043967 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 84043967 51 GVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSYIP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 84043967 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 84043967 44 TSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 84043967 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 84043967 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 84043967 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 84043967 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. |
633-664 |
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 84043967 633 PEEVDDFIRGQLVTNLPGVGHSMESKLASLGI 664
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
1010-1041 |
3.18e-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: 3.18e-03
10 20 30
....*....|....*....|....*....|..
gi 84043967 1010 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1041
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
932-953 |
7.70e-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: 7.70e-03
|
| |
