|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
346-779 |
3.20e-173 |
|
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: 516.87 E-value: 3.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 346 FISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPgreklkkvktgrsslvvtdtgtmSVLSSPRHQSCVMHVDMDCF 425
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 426 FVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngidsvlsKAE 505
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP----------------------------------------------------NSE 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 506 IASCSYEA-------------------------------------------SYTHSIEAVSCDEALIDVTDILAETKLSP 542
Cdd:cd01701 86 IASCNYEArsygikngmwvgqakklcpqlvtlpydfeayeevsltfyeilaSYTDNIEAVSCDEALIDITSLLEETYELP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 543 EEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKT 622
Cdd:cd01701 166 EELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 623 CGD--LQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEA 700
Cdd:cd01701 246 CGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEE 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069831 701 AGMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 779
Cdd:cd01701 326 SNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
417-776 |
3.05e-68 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 233.11 E-value: 3.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTG---TA-------------PLR------PGA-----NPQLEWQYYq 469
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGvvaAAsyearafgvrsgmPLFqarrlcPDLvvlppDFELYRDVS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 470 nRALRgkaadipdssvwenqdstqtngidsvlskaEIAscsyeASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAAL 549
Cdd:COG0389 82 -RRVM------------------------------AIL-----ERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 550 RIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCL 629
Cdd:COG0389 125 RRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 630 TMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLT 709
Cdd:COG0389 205 PRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVT 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069831 710 LKimvrkpgapIETAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQV 776
Cdd:COG0389 284 VK---------LRTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
422-712 |
1.27e-53 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 191.10 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 422 MDCFFVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralRGkaadipdssvwenqdstqtngidsVl 501
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAVGGSPGR-----------------------RG------------------------V- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 502 skaeIASCSYEA-------------------------------------------SYTHSIEAVSCDEALIDVTDILAEt 538
Cdd:PRK02406 33 ----ISTCNYEArkfgvrsamptaqalklcpdlifvpgrfdvykevsrqireifrRYTDLIEPLSLDEAYLDVTDNKLC- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 539 KLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASL 618
Cdd:PRK02406 108 IGSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 619 GIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRL 698
Cdd:PRK02406 188 GIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRL 266
|
330
....*....|....*.
gi 1907069831 699 EAAGM--KGKRLTLKI 712
Cdd:PRK02406 267 ERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
3.77e-48 |
|
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: 165.82 E-value: 3.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1907069831 125 SSAPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1112-1205 |
2.02e-41 |
|
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: 147.03 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 1112 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1191
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069831 1192 QVVLQQTYGSTLKV 1205
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
420-577 |
9.06e-24 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 98.42 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 420 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTG---TAPlrpganpqlewqyYQNRAL-------RGKAADI-PDssvwen 488
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGivaAAS-------------YEARKYgvrsgmpVFEAKKLcPN------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 489 qdsTQTNGID-----SVLSK-AEIASCSYeasyTHSIEAVSCDEALIDVTDiLAETKLSPEEFAAALRIEIKDKTKCAAS 562
Cdd:pfam00817 62 ---LIVVPPDlelyrRASRKiFEILRRFS----TPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLTCS 133
|
170
....*....|....*
gi 1907069831 563 VGIGSNILLARMATK 577
Cdd:pfam00817 134 IGIAPNKLLAKLASD 148
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1122-1203 |
1.30e-16 |
|
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: 76.12 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 1122 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1192
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069831 1193 VVLQQTYGSTL 1203
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
962-997 |
8.86e-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: 71.87 E-value: 8.86e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1907069831 962 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 997
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
886-919 |
1.40e-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: 63.01 E-value: 1.40e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069831 886 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 919
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 ... |
48-129 |
7.19e-11 |
|
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: 59.69 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSA 127
Cdd:pfam16589 4 LFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLE 82
|
..
gi 1907069831 128 PY 129
Cdd:pfam16589 83 NY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
48-118 |
1.88e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 58.16 E-value: 1.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069831 48 IFSGVAIYVNGYTD-PSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 3 LFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
346-779 |
3.20e-173 |
|
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: 516.87 E-value: 3.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 346 FISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPgreklkkvktgrsslvvtdtgtmSVLSSPRHQSCVMHVDMDCF 425
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 426 FVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngidsvlsKAE 505
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP----------------------------------------------------NSE 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 506 IASCSYEA-------------------------------------------SYTHSIEAVSCDEALIDVTDILAETKLSP 542
Cdd:cd01701 86 IASCNYEArsygikngmwvgqakklcpqlvtlpydfeayeevsltfyeilaSYTDNIEAVSCDEALIDITSLLEETYELP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 543 EEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKT 622
Cdd:cd01701 166 EELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 623 CGD--LQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEA 700
Cdd:cd01701 246 CGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEE 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069831 701 AGMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 779
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 ... |
418-779 |
1.40e-73 |
|
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: 247.82 E-value: 1.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 418 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTG---TAplrpganpqlewqYYQNRALRGKAAD--------IPdssvw 486
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVGGSSDRGvvsTA-------------SYEARKFGVRSAMpifqakklCP----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 487 enqdstqtNGIDSVLSKAEIASCSYE-----ASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAALRIEIKDKTKCAA 561
Cdd:cd03586 63 --------NLIFVPPRFDKYREVSRQimeilREYTPLVEPLSIDEAYLDVTDYVRLFG-SATEIAKEIRARIREETGLTA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 562 SVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpK 641
Cdd:cd03586 134 SAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKELGIKTIGDLAKLDVELLKKLFG-K 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 642 TGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKImvrkpgapi 721
Cdd:cd03586 213 SGRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVKL--------- 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069831 722 etaKFGGHgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISdMRGVGIQVNQL 779
Cdd:cd03586 284 ---KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVRLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
417-776 |
3.05e-68 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 233.11 E-value: 3.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTG---TA-------------PLR------PGA-----NPQLEWQYYq 469
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGvvaAAsyearafgvrsgmPLFqarrlcPDLvvlppDFELYRDVS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 470 nRALRgkaadipdssvwenqdstqtngidsvlskaEIAscsyeASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAAL 549
Cdd:COG0389 82 -RRVM------------------------------AIL-----ERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 550 RIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCL 629
Cdd:COG0389 125 RRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 630 TMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLT 709
Cdd:COG0389 205 PRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVT 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069831 710 LKimvrkpgapIETAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQV 776
Cdd:COG0389 284 VK---------LRTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
422-712 |
1.27e-53 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 191.10 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 422 MDCFFVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralRGkaadipdssvwenqdstqtngidsVl 501
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAVGGSPGR-----------------------RG------------------------V- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 502 skaeIASCSYEA-------------------------------------------SYTHSIEAVSCDEALIDVTDILAEt 538
Cdd:PRK02406 33 ----ISTCNYEArkfgvrsamptaqalklcpdlifvpgrfdvykevsrqireifrRYTDLIEPLSLDEAYLDVTDNKLC- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 539 KLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASL 618
Cdd:PRK02406 108 IGSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 619 GIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRL 698
Cdd:PRK02406 188 GIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRL 266
|
330
....*....|....*.
gi 1907069831 699 EAAGM--KGKRLTLKI 712
Cdd:PRK02406 267 ERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
3.77e-48 |
|
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: 165.82 E-value: 3.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1907069831 125 SSAPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
417-751 |
1.82e-44 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 167.80 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGT-GTAPL---RPGAN---PQlewqyYQNRALRGKAADI--PDSSV 485
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGVvAGASYearVFGARsamPM-----HQARRLVGNGAVVlpPRFVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 486 WenqdstqtngidSVLSKAeiascSYEASYTHS--IEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAASV 563
Cdd:PRK03348 82 Y------------RAASRR-----VFDTLRELSpvVEQLSFDEAFVEPAELAGASAEEVEAFAERLRARVREETGLPASV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 564 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTG 643
Cdd:PRK03348 145 GAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRLGIETIGDLAALSEAEVANLLGATVG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 644 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimVRKPGAPIET 723
Cdd:PRK03348 225 PALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRGARTVTVK--LRKSDFSTLT 302
|
330 340
....*....|....*....|....*...
gi 1907069831 724 akfgghgicdniaRTVTLDQATDSAKII 751
Cdd:PRK03348 303 -------------RSATLPYATDDAAVL 317
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1112-1205 |
2.02e-41 |
|
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: 147.03 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 1112 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1191
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069831 1192 QVVLQQTYGSTLKV 1205
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
417-783 |
1.97e-37 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 145.92 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrgtGTAPLRPG----ANPQLEWQYYQN-RALRGKAADIPDSSVWENQDS 491
Cdd:PRK03103 5 ILLVDMQSFYASVEKAANPELKGRPVIVS-----GDPERRSGvvlaACPLAKAYGVKTaERLWEAQQKCPDLVVVKPRMQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 492 TQtngIDSVLSKAEIAScsyeaSYTHSIEAVSCDEALIDVTDILaetKL--SPEEFAAALRIEIKDKTKCAASVGIGSNI 569
Cdd:PRK03103 80 RY---IDVSLQITRILE-----DFTDLVEPFSIDEQFLDVTGSQ---KLfgSPLEIAQKIQQRIMRETGVYARVGIGPNK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 570 LLARMAT---KKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQML 646
Cdd:PRK03103 149 LLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIGQLANTPLERLKKRWG-INGEVL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 647 YRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKrlTLKIMVRkpGAPIETA 724
Cdd:PRK03103 228 WRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVLLELCEEVCRRARAKGYMGR--TVSVSLR--GADFDWP 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069831 725 KfgghgicdNIARTVTLDQATDSAKIIGKATLNMFHTMkLNISDMRGVGIQVNQLVPAN 783
Cdd:PRK03103 304 T--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGKPVRRVGVTLSNLVSDD 353
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
419-710 |
6.12e-36 |
|
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: 139.80 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 419 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTAPL------RPGANPQLEWQYYQNRALRGKAADIPDSSVWENQDST 492
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNSDSTCVIacsyeaRKYGVKRGMPVREARKMCPNLILVPARLDLYRRLSER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 493 QTNGIDSVLSKAEIASCsyeasythsieavscDEALIDVTDIlAETKLSPEEFAAALRIEIKDKTK-CAASVGIGSNILL 571
Cdd:cd00424 82 LLSELEEVAPLVEVASI---------------DELFLDLTGS-ARLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 572 ARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCR 651
Cdd:cd00424 146 AKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWYALR 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069831 652 GLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTL 710
Cdd:cd00424 226 GIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
417-788 |
8.13e-36 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 139.85 E-value: 8.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRG-TGTAPlrpganpqlewqyYQNRALRGKAAdIPdssVWENQDSTq 493
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGvVSTCS-------------YEARKYGVHSA-MP---VFMAKKRC- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 494 TNGID-SVLSK--AEIASCSYEASY--THSIEAVSCDEALIDVTDIlaetKLSPEEFAAALRIEIKDKTKCAASVGIGSN 568
Cdd:PRK14133 67 PHGIFlPVRHEryKEVSKNIFKILYevTPIVEPVSIDEAYLDITNI----KEEPIKIAKYIKKKVKKETGLTLSVGISYN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 569 ILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYR 648
Cdd:PRK14133 143 KFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 649 FCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpgapIETAKFGG 728
Cdd:PRK14133 222 RIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKTVTVK---------IKTSDFQT 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 729 HgicdniARTVTLDQATDSAKIIGKATLNMFHTMKLNiSDMRGVGIQVnqlvpanSNLST 788
Cdd:PRK14133 293 H------TKSKTLNDYIRDKEEIYNVACEILEHINIK-EPIRLIGLSV-------SNLSE 338
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
410-782 |
9.60e-34 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 135.44 E-value: 9.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 410 SPR-------HQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVT-SNRGTGTAP--------LRpGANPQlewqyYQNRAL 473
Cdd:PRK02794 24 SPRlvrhpelYTLSIAHIDCDAFYASVEKRDNPELRDKPVIIGgGKRGVVSTAcyiarihgVR-SAMPM-----FKALKL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 474 RGKAADI-PDSSVWenqdstqtngidsVLSKAEIASCSYEAsyTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIE 552
Cdd:PRK02794 98 CPDAVVIkPDMEKY-------------VRVGREVRAMMQAL--TPLVEPLSIDEAFLDLSGTERLHGAPPAVVLARFARR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 553 IKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMA 632
Cdd:PRK02794 163 VEREIGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 633 KLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKi 712
Cdd:PRK02794 243 DLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLK- 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 713 mvrkpgapIETAKFGGHgicdniARTVTLDQATDSAKIIGKATLNMFHTMkLNISDMRGVGIQVNQLVPA 782
Cdd:PRK02794 321 --------LKTADFRLR------TRRRTLEDPTQLADRIFRTARELLEKE-TDGTAFRLIGIGVSDLSPA 375
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
417-712 |
5.80e-32 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 128.22 E-value: 5.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVtSNRGTGTAPLRPGANPQLEWQYYQNRA---LRGKAADIPDSsvwenqdstq 493
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIV-GGNGDPTEPRKVVTCASYEARAFGVRAgmpLRTAARRCPDA---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 494 tngidsVLSKAEIAScsYEA----------SYTHSIEAVSCDEALI--DVTDilaetklsPEEFAAALRIEIKDKTKCAA 561
Cdd:PRK03352 76 ------VFLPSDPAA--YDAaseevmatlrDLGVPVEVWGWDEAFLgvDTDD--------PEALAEEIRAAVLERTGLSC 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 562 SVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPK 641
Cdd:PRK03352 140 SVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAALGITTVADLAAADPAELAATFGPT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069831 642 TGQMLYRFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKI 712
Cdd:PRK03352 220 TGPWLLLLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELARRVLDEVVAEGRPVTRVAVKV 291
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
417-747 |
3.81e-31 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 127.02 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSN-----------RGTGTAplRPGAnpqlewqyyQNRALrgkaadIPDSSV 485
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIVGGGvvlaasyeakaYGVRTA--MGGR---------QARRL------CPQAVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 486 WENQDSTQTNGIDSVLskaEIAScsyeaSYTHSIEAVSCDEALIDVTDIlaeTKLS--PEEFAAALRIEIKDKTKCAASV 563
Cdd:PRK03858 69 VPPRMSAYSRASKAVF---EVFR-----DTTPLVEGLSIDEAFLDVGGL---RRISgtPVQIAARLRRRVREEVGLPITV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 564 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTG 643
Cdd:PRK03858 138 GVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAHGITTVGDVAELPESALVSLLGPAAG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 644 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKImvrkpgapiet 723
Cdd:PRK03858 218 RHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGRTVVLRL----------- 286
|
330 340
....*....|....*....|....
gi 1907069831 724 aKFGGHGicdNIARTVTLDQATDS 747
Cdd:PRK03858 287 -RFDDFT---RATRSHTLPRPTAS 306
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
417-759 |
1.80e-30 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 125.53 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrgtGTAPLRPG----ANpqlewqyYQNRAlRGKAADIPdssVWEnqdsT 492
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVA-----GNEKERKGiivtCS-------YEARA-YGIRTTMP---LWE----A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 493 QTNGIDSVLSKAEIA---SCSYE-----ASYTHSIEAVSCDEALIDVTDILAetKLSPEEFAAALRIEIKDKTKCAASVG 564
Cdd:PRK01810 67 KRLCPQLIVRRPNFDryrEASRQmfqilSEFTPLVQPVSIDEGYLDITDCYA--LGSPLEIAKMIQQRLLTELQLPCSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 565 IGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQ 644
Cdd:PRK01810 145 IAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIGIQTIGDLAKADEHILRAKLG-INGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 645 MLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKrlTLKIMVRkpgapie 722
Cdd:PRK01810 224 RLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRLQKKTVVSY--NVQIMIR------- 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907069831 723 TAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMF 759
Cdd:PRK01810 295 YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
418-712 |
2.28e-29 |
|
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: 120.73 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 418 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSN-RGTGTAplrpgANPQLewqyyqnralrgKAADIPDSS-VWENQDSTQTN 495
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSNnDGCVIA-----RSPEA------------KALGIKMGSpYFKVPDLLERH 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 496 GIdsvlskaEIASCSYE-------------ASYTHSIEAVSCDEALIDVTDILaeTKLSPEEFAAALRIEIKDKTKCAAS 562
Cdd:cd01700 64 GV-------AVFSSNYAlygdmsrrimsilERFSPDVEVYSIDESFLDLTGSL--RFGDLEELARKIRRRILQETGIPVT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 563 VGIGSNILLARMAT----KKAKPDGQYHLQPDEVDDFIRGQL-VTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKE 637
Cdd:cd01700 135 VGIGPTKTLAKLANdlakKKNPYGGVVDLTDEEVRDKLLKILpVGDVWGIGRRTAKKLNAMGIHTAGDLAQADPDLLRKK 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069831 638 FGpKTGQMLYRFCRGLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKI 712
Cdd:cd01700 215 FG-VVGERLVRELNGIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
417-666 |
5.75e-25 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 107.95 E-value: 5.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRG-TGTAPLRPGANpqlewqyYQNRALrGKAADIPDSSVWE-------- 487
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSGrFEDSGAVATAN-------YEARKL-GIKAGMPIVEAKKilpnavyl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 488 --NQDSTQ--TNGIDSVLSKaeiascsyeasYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAALRIEIKDKTKCAASV 563
Cdd:PRK01216 75 pmRKEVYQqvSNRIMKLLRE-----------YSEKIEIASIDEAYLDISDKVKNYQ-DAYNLGLEIKNKILEKEKITVTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 564 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTG 643
Cdd:PRK01216 143 GISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKLGVNKLVDTLRIEFDELKGIIGEAKA 222
|
250 260
....*....|....*....|...
gi 1907069831 644 QMLYRFCRGLDDRPVRTeKERKS 666
Cdd:PRK01216 223 KYLFSLARNEYNEPVRA-RVRKS 244
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
420-577 |
9.06e-24 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 98.42 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 420 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTG---TAPlrpganpqlewqyYQNRAL-------RGKAADI-PDssvwen 488
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGivaAAS-------------YEARKYgvrsgmpVFEAKKLcPN------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 489 qdsTQTNGID-----SVLSK-AEIASCSYeasyTHSIEAVSCDEALIDVTDiLAETKLSPEEFAAALRIEIKDKTKCAAS 562
Cdd:pfam00817 62 ---LIVVPPDlelyrRASRKiFEILRRFS----TPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLTCS 133
|
170
....*....|....*
gi 1907069831 563 VGIGSNILLARMATK 577
Cdd:pfam00817 134 IGIAPNKLLAKLASD 148
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
419-761 |
5.24e-22 |
|
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: 99.31 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 419 HVDMDCFFVSVGIRNRPDLKGKPVAVT----------SNRGTG---------------------TAPLRPGANpqlEWQY 467
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAVVqwnsiiavsyAARAFGvtrfmtideakkkcpdlilahVATYKKGED---EADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 468 YQNRAL-RGKAADIPdssvwENQDSTQtngIDSVLSKaeiascsyeasYTHSIEAVSCDEALIDVTDILAETklspeefa 546
Cdd:cd01702 79 HENPSPaRHKVSLDP-----YRRASRK---ILNILKR-----------FGDVVEKASIDEAYLDLGSRIVEE-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 547 aaLRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSM-ESKLASLGIKTCGD 625
Cdd:cd01702 132 --IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 626 LQCL--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINY-GIRFTQPKEAEAFLLSLSEEIQRRLEAA- 701
Cdd:cd01702 210 VAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpGKTALSTEDVQHWLLVLASELNSRLEDDr 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069831 702 ---GMKGKRLTLKIMVRKPGAPIEtakfgghgICDNIARTVTLDQATDSAKIIGKATLNMFHT 761
Cdd:cd01702 290 yenNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYDAQKIVKDAFKLIKAINEEGLGL 344
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
664-783 |
8.13e-21 |
|
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: 88.39 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 664 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMvrkpgapieTAKFgghgicDNIARTVTLDQ 743
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907069831 744 ATDSAKIIGKATLNMFHTMKLNIsDMRGVGIQVNQLVPAN 783
Cdd:pfam11799 66 PTDDTDEIYRAALRLLRRLYRGR-PVRLLGVSLSNLVPEG 104
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
419-717 |
2.24e-17 |
|
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: 85.60 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 419 HVDMDCFFVSVGIRNRPDLKGKPVA-------VTSNrgtgtaplrpganpqlewqyYQNRALRGKAADipdsSVWENQDS 491
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGiqqkyivVTCN--------------------YEARRLGVKKLM----SIKDAKEI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 492 TQtngiDSVLSKAEIASCSYEASY-----------THSIEAVSCDEALIDVTDIlaeTKLSPEEFAAALRIEIKDKTKCA 560
Cdd:cd01703 58 CP----DLVLVNGEDLTPFRDMSKkvyrllrsyswNDRVERLGFDENFMDVTEM---RLLVASHIAYEMRERIENELGLT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 561 ASVGIGSNILLARMATKKAKPDGQYHLQP---DEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQ---------- 627
Cdd:cd01703 131 CCAGIASNKLLAKLVGSVNKPNQQTTLLPpscADLMDFMDLHDLRKIPGIGYKTAAKLEAHGISSVRDLQefsnrnrqtv 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 628 -----CLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINYG-IRFTQPKEAEAFLLSLSEEIQRRL-- 698
Cdd:cd01703 211 gaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSYKkCSLEEIREARNKIEELLASLLERMkq 290
|
330 340
....*....|....*....|...
gi 1907069831 699 ----EAAGMKGKRLTLKIMVRKP 717
Cdd:cd01703 291 dlqeVKAGDGRRPHTLRLTLRRY 313
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1122-1203 |
1.30e-16 |
|
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: 76.12 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 1122 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1192
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069831 1193 VVLQQTYGSTL 1203
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
408-712 |
3.27e-16 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 83.53 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 408 LSSPRHQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAV-------TSN---RGTGtapLRPGANPQLEWQYYQNRALRGka 477
Cdd:PTZ00205 126 LEATRRLGTYIHLDMDMFYAAVEIKKHPEYAAIPLAIgtmtmlqTANyvaRGRG---IRQGMPGFLALKICPNLLILP-- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 478 adiPDSSVWeNQDStqtNGIDSVLSKaeiascsYEASYThsieAVSCDEALIDVTDILA--ETKLSPEEFAAALRIEIKD 555
Cdd:PTZ00205 201 ---PDFDAY-NEES---NTVRRIVAE-------YDPNYI----SFGLDELTLEVSAYIErfEGTKTAEDVASELRVRVFG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 556 KTKCAASVGIGSNILLARMATKKAKPDGQYHLQ---PDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQ----- 627
Cdd:PTZ00205 263 ETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDIYnrrve 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 628 -CLTMAKLQKEF--GPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSAEINYGIrFTQPKEAEAFLLSLSEEIQRRLEAA 701
Cdd:PTZ00205 343 lCYILHNNLFRFllGASIGIMQWpDAATAANTENCEgaTGGQRKAISSERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKS 421
|
330
....*....|.
gi 1907069831 702 GMKGKRLTLKI 712
Cdd:PTZ00205 422 ELMCRQISLTI 432
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
962-997 |
8.86e-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: 71.87 E-value: 8.86e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1907069831 962 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 997
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
515-711 |
3.01e-13 |
|
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: 72.41 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 515 YTHSIEAVSCDEALIDVTdilAETKLSPEEFAAALRIEIKDKTKC-AASVGIGSNILLARMATKKAKPDGQYHLQPDEVD 593
Cdd:cd03468 88 FTPLVALDGPDGLLLDVT---GCLHLFGGEDALAASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 594 DFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEI 671
Cdd:cd03468 165 LVLLAPLPVAALRLPPETVELLARLGLRTLGDLAALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLEL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907069831 672 NYGIRFTQPKEAEafLLSLSEEIQRRLEAAGMKGKRLTLK 711
Cdd:cd03468 244 QLEEPIARGLLFP--LRRLLEQLCAFLALRGLGARRLSLT 281
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
886-919 |
1.40e-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: 63.01 E-value: 1.40e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069831 886 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 919
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 ... |
48-129 |
7.19e-11 |
|
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: 59.69 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSA 127
Cdd:pfam16589 4 LFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLE 82
|
..
gi 1907069831 128 PY 129
Cdd:pfam16589 83 NY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
48-118 |
1.88e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 58.16 E-value: 1.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069831 48 IFSGVAIYVNGYTD-PSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 3 LFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
419-678 |
2.49e-10 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 64.02 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 419 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNrGTGTAPLRPGANPQLEWQ----YYQNRALRGKAADIPDSSVWENQDStQT 494
Cdd:PRK03609 4 LCDVNSFYASCETVFRPDLRGKPVVVLSN-NDGCVIARSAEAKALGIKmgdpWFKQKDLFRRCGVVCFSSNYELYAD-MS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 495 NGIDSVLSkaEIAScsyeasythSIEAVSCDEALIDVTDIlaETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARM 574
Cdd:PRK03609 82 NRVMSTLE--ELSP---------RVEIYSIDEAFCDLTGV--RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 575 ATKKAKpdgQYHLQPDEVDDFIRGQ----LVTNLP-----GVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFgpktGQM 645
Cdd:PRK03609 149 ANHAAK---KWQRQTGGVVDLSNLErqrkLLSLQPveevwGVGRRISKKLNAMGIKTALDLADTNIRFIRKHF----NVV 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907069831 646 LYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 678
Cdd:PRK03609 222 LERTVRELRGEPCLSLEEFAPTKQEIvcsrSFGERIT 258
|
|
| 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 |
3.04e-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: 57.32 E-value: 3.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATnlpNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:cd18431 4 IFTGVKVYLPGSVEDDYKKLKRYFIAYDGDVVEEYDEEDATHVVVD---RDDKLGNPSAKVVSPEWLWDCIKKQKLV 77
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
48-118 |
6.79e-10 |
|
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: 56.53 E-value: 6.79e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKELK-GEKVIRPEWIVESI 118
Cdd:pfam00533 5 LFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSK-KTTHVIVEARTKKYLKAKElGIPIVTEEWLLDCI 75
|
|
| 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 |
3.57e-08 |
|
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: 51.92 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 48 IFSGVAIYV-NGYTDP-SAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 1907069831 123 LLSSAPYQLY 132
Cdd:cd17722 80 LLPLEPKYMI 89
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
54-117 |
1.67e-07 |
|
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.
Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 49.28 E-value: 1.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069831 54 IYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKEL---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 |
9.38e-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: 47.53 E-value: 9.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069831 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17731 2 PFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKN-CTHLIAGSPSGQKYEfarKWNSIHIVTPEWLYDSIEAG 77
|
|
| BRCT_XRCC1_rpt1 |
cd17725 |
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ... |
51-129 |
1.73e-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: 46.89 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 51 GVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSSAP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 1907069831 129 Y 129
Cdd:cd17725 80 Y 80
|
|
| BRCT_PAXIP1_rpt2 |
cd17710 |
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
48-125 |
1.76e-06 |
|
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: 46.84 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 48 IFSGVAIYVNGYtdpSAEELRNL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 1907069831 122 RLLS 125
Cdd:cd17710 77 TLLD 80
|
|
| BRCT_PAXIP1_rpt1 |
cd17714 |
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; ... |
49-125 |
4.66e-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: 42.69 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 49 FSGVAIYVNGYTDPSAEELrnlmmLH-GGQYHVYYSRSKTTHIIATNLPNAKIKELK--GEK-VIRPEWIVESIKAGRLL 124
Cdd:cd17714 1 FKDVKYFVVGNLDEKVEQL-----LKnGGAKEVSYLSDMATHVIVDDNDNPEVGEARdlFELpVVTSSWVILSIKAGKLL 75
|
.
gi 1907069831 125 S 125
Cdd:cd17714 76 P 76
|
|
| BRCT_TopBP1_rpt3 |
cd17718 |
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
44-122 |
1.09e-04 |
|
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: 41.81 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 44 TASAIFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 1907069831 120 AGR 122
Cdd:cd17718 81 QGK 83
|
|
| BRCT_Rad4_rpt2 |
cd17746 |
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ... |
62-131 |
1.45e-04 |
|
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: 41.84 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069831 62 PSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIK-ELK-GEKVIRPEWIVESIKAGRLLSSAPYQL 131
Cdd:cd17746 20 PERSRIENYVLKHGGTFCPDLTRD-VTHLIAGTSSGRKYEyALKwKINVVCVEWLWQSIQRNAVLEPQYFQL 90
|
|
| IMS_HHH |
pfam11798 |
IMS family HHH motif; These proteins are involved in UV protection, eg. |
589-620 |
5.34e-04 |
|
IMS family HHH motif; These proteins are involved in UV protection, eg.
Pssm-ID: 432081 [Multi-domain] Cd Length: 32 Bit Score: 38.53 E-value: 5.34e-04
10 20 30
....*....|....*....|....*....|..
gi 1907069831 589 PDEVDDFIRGQLVTNLPGVGRSMESKLASLGI 620
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
54-113 |
7.08e-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: 39.11 E-value: 7.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069831 54 IYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIAtnlpnakiKELKGEK----------VIRPEW 113
Cdd:pfam12738 3 ICVTGFDGDDREGLQKLIEAMGAEYTKDLTK-SVTHLIC--------KSGEGEKyekakewgipVVSPLW 63
|
|
| |
