|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
346-812 |
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: 619.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 346 FISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPgreklkkvktgtmSVLSSPRHQSCVMHVDMDCFFVSVGIRNRP 425
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-------------SNSIHPDLQRIIMHVDFDCFFVSVSIRNRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 426 DLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngidsvlsKAEIASCSYEARQ 505
Cdd:cd01701 68 DLKGKPVAVCHGKGP----------------------------------------------------NSEIASCNYEARS 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 506 VGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIE 585
Cdd:cd01701 96 YGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 586 IKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGD--LQCLT 663
Cdd:cd01701 176 IRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 664 MAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTL 743
Cdd:cd01701 256 KEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITL 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069828 744 KIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 812
Cdd:cd01701 336 KLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
407-809 |
4.01e-88 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 288.97 E-value: 4.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtng 486
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 idsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTD 566
Cdd:COG0389 39 ---------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 567 ILAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMES 646
Cdd:COG0389 110 SARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 647 KLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEE 726
Cdd:COG0389 189 KLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAER 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 727 IQRRLEAAGMKGKRLTLKimvrkpgapIETAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVG 806
Cdd:COG0389 268 LAERLRRQGLGARTVTVK---------LRTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLG 332
|
...
gi 1907069828 807 IQV 809
Cdd:COG0389 333 VRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
412-745 |
2.38e-70 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 239.25 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 412 MDCFFVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralRGkaadipdssvwenqdstqtngidsVl 491
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAVGGSPGR-----------------------RG------------------------V- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 492 skaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAEt 571
Cdd:PRK02406 33 ----ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLC- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 572 KLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASL 651
Cdd:PRK02406 108 IGSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 652 GIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRL 731
Cdd:PRK02406 188 GIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRL 266
|
330
....*....|....*.
gi 1907069828 732 EAAGM--KGKRLTLKI 745
Cdd:PRK02406 267 ERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
3.88e-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: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1907069828 125 SSAPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
410-610 |
9.58e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 158.51 E-value: 9.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 410 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngids 489
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGI----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 490 vlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASY-THSIEAVSCDEALIDVTDiL 568
Cdd:pfam00817 34 ------VAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-L 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907069828 569 AETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATK 610
Cdd:pfam00817 107 EKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1145-1238 |
2.08e-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: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 1145 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1224
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069828 1225 QVVLQQTYGSTLKV 1238
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 ... |
1155-1236 |
1.34e-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: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 1155 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1225
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069828 1226 VVLQQTYGSTL 1236
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
995-1030 |
9.10e-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: 9.10e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1907069828 995 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 1030
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
919-952 |
1.45e-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: 1.45e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069828 919 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 952
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 |
7.39e-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: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSA 127
Cdd:pfam16589 4 LFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLE 82
|
..
gi 1907069828 128 PY 129
Cdd:pfam16589 83 NY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
48-118 |
1.93e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 58.16 E-value: 1.93e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069828 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. ... |
346-812 |
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: 619.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 346 FISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPgreklkkvktgtmSVLSSPRHQSCVMHVDMDCFFVSVGIRNRP 425
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-------------SNSIHPDLQRIIMHVDFDCFFVSVSIRNRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 426 DLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngidsvlsKAEIASCSYEARQ 505
Cdd:cd01701 68 DLKGKPVAVCHGKGP----------------------------------------------------NSEIASCNYEARS 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 506 VGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIE 585
Cdd:cd01701 96 YGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 586 IKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGD--LQCLT 663
Cdd:cd01701 176 IRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 664 MAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTL 743
Cdd:cd01701 256 KEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITL 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069828 744 KIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 812
Cdd:cd01701 336 KLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
408-812 |
2.48e-93 |
|
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: 303.29 E-value: 2.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 408 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgtaplrpganpqlewqyyqnralrgkaadiPDSSVwenqdstqtngi 487
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVGGS---------------------------------SDRGV------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 488 dsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 567
Cdd:cd03586 36 --------VSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPRFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDY 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 568 LAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESK 647
Cdd:cd03586 108 VRLFG-SATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 648 LASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 727
Cdd:cd03586 187 LKELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 728 QRRLEAAGMKGKRLTLKImvrkpgapietaKFGGHgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISdMRGVGI 807
Cdd:cd03586 266 AERLRKRGLKGRTVTVKL------------KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGV 329
|
....*
gi 1907069828 808 QVNQL 812
Cdd:cd03586 330 RLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
407-809 |
4.01e-88 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 288.97 E-value: 4.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtng 486
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 idsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTD 566
Cdd:COG0389 39 ---------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 567 ILAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMES 646
Cdd:COG0389 110 SARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 647 KLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEE 726
Cdd:COG0389 189 KLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAER 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 727 IQRRLEAAGMKGKRLTLKimvrkpgapIETAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVG 806
Cdd:COG0389 268 LAERLRRQGLGARTVTVK---------LRTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLG 332
|
...
gi 1907069828 807 IQV 809
Cdd:COG0389 333 VRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
412-745 |
2.38e-70 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 239.25 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 412 MDCFFVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralRGkaadipdssvwenqdstqtngidsVl 491
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAVGGSPGR-----------------------RG------------------------V- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 492 skaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAEt 571
Cdd:PRK02406 33 ----ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLC- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 572 KLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASL 651
Cdd:PRK02406 108 IGSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 652 GIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRL 731
Cdd:PRK02406 188 GIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRL 266
|
330
....*....|....*.
gi 1907069828 732 EAAGM--KGKRLTLKI 745
Cdd:PRK02406 267 ERAKPdkRIKTVGVKL 282
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
407-784 |
2.61e-54 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 197.08 E-value: 2.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqt 484
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 485 ngidsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAV-PYDFHACREVAQAMYETLASYTHSIEAVSCDEALID 563
Cdd:PRK03348 43 -----------VAGASYEARVFGARSAMPMHQARRLVGNGAVVlPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 564 VTDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRS 643
Cdd:PRK03348 112 PAELAGASAEEVEAFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 644 MESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSL 723
Cdd:PRK03348 192 TEEKLHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERI 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069828 724 SEEIQRRLEAAGMKGKRLTLKimVRKPGAPIETakfgghgicdniaRTVTLDQATDSAKII 784
Cdd:PRK03348 272 AEHAHRRLLKDGRGARTVTVK--LRKSDFSTLT-------------RSATLPYATDDAAVL 317
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
409-743 |
3.14e-53 |
|
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: 190.26 E-value: 3.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 409 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTAplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngid 488
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNSDSTC--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 489 svlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDIl 568
Cdd:cd00424 37 -------VIACSYEARKYGVKRGMPVREARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 569 AETKLSPEEFAAALRIEIKDKTK-CAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESK 647
Cdd:cd00424 109 ARLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 648 LASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 727
Cdd:cd00424 189 LEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKL 268
|
330
....*....|....*.
gi 1907069828 728 QRRLEAAGMKGKRLTL 743
Cdd:cd00424 269 ARRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
407-821 |
2.86e-50 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 181.84 E-value: 2.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqt 484
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGV-------------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 485 ngidsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDV 564
Cdd:PRK14133 41 -----------VSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDI 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 565 TDIlaetKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSM 644
Cdd:PRK14133 110 TNI----KEEPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 645 ESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLS 724
Cdd:PRK14133 186 VEKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 725 EEIQRRLEAAGMKGKRLTLKimvrkpgapIETAKFGGHgicdniARTVTLDQATDSAKIIGKATLNMFHTMKLNiSDMRG 804
Cdd:PRK14133 265 NIISEELKKRNLYGKTVTVK---------IKTSDFQTH------TKSKTLNDYIRDKEEIYNVACEILEHINIK-EPIRL 328
|
410
....*....|....*..
gi 1907069828 805 VGIQVnqlvpanSNLST 821
Cdd:PRK14133 329 IGLSV-------SNLSE 338
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
3.88e-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: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1907069828 125 SSAPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
407-792 |
2.08e-47 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 175.22 E-value: 2.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdSTQTNG 486
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVAGN-------------------------------------------EKERKG 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 IdsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTD 566
Cdd:PRK01810 44 I--------IVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 567 ILAetKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMES 646
Cdd:PRK01810 116 CYA--LGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 647 KLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLS 724
Cdd:PRK01810 194 KLKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLS 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069828 725 EEIQRRLEAAGMKGKrlTLKIMVRkpgapieTAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMF 792
Cdd:PRK01810 273 KSVSKRLQKKTVVSY--NVQIMIR-------YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
407-816 |
2.23e-45 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 169.41 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSnrgtgtaplrpganpqlewqyyqnralrgkaadipdssvwenqDSTQTNG 486
Cdd:PRK03103 5 ILLVDMQSFYASVEKAANPELKGRPVIVSG-------------------------------------------DPERRSG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 IdsVLskaeiASCsYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTD 566
Cdd:PRK03103 42 V--VL-----AAC-PLAKAYGVKTAERLWEAQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 567 ILaetKL--SPEEFAAALRIEIKDKTKCAASVGIGSNILLARMAT---KKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVG 641
Cdd:PRK03103 114 SQ---KLfgSPLEIAQKIQQRIMRETGVYARVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 642 RSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAF 719
Cdd:PRK03103 191 SRMEKHLRRMGIRTIGQLANTPLERLKKRWG-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 720 LLSLSEEIQRRLEAAGMKGKrlTLKIMVRkpGAPIETAKfgghgicdNIARTVTLDQATDSAKIIGKATLNMFHTMkLNI 799
Cdd:PRK03103 270 LLELCEEVCRRARAKGYMGR--TVSVSLR--GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDG 336
|
410
....*....|....*..
gi 1907069828 800 SDMRGVGIQVNQLVPAN 816
Cdd:PRK03103 337 KPVRRVGVTLSNLVSDD 353
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
410-610 |
9.58e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 158.51 E-value: 9.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 410 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtngids 489
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGI----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 490 vlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASY-THSIEAVSCDEALIDVTDiL 568
Cdd:pfam00817 34 ------VAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-L 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907069828 569 AETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATK 610
Cdd:pfam00817 107 EKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
407-780 |
1.83e-42 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 160.54 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGTaplrpganpqlewqyyqnralrgkaadipdssvwenqdstqtng 486
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIV----GGGV-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 idsVLSkaeiasCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTD 566
Cdd:PRK03858 38 ---VLA------ASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 567 IlaeTKLS--PEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSM 644
Cdd:PRK03858 109 L---RRISgtPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVT 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 645 ESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLS 724
Cdd:PRK03858 186 AAKLRAHGITTVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALV 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069828 725 EEIQRRLEAAGMKGKRLTLKImvrkpgapietaKFGGHGicdNIARTVTLDQATDS 780
Cdd:PRK03858 266 DRVARRMRAAGRTGRTVVLRL------------RFDDFT---RATRSHTLPRPTAS 306
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
400-815 |
1.26e-41 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 158.56 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 400 SPR-------HQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGTaplrpganpqlewqyyqnralRGkaadipd 472
Cdd:PRK02794 24 SPRlvrhpelYTLSIAHIDCDAFYASVEKRDNPELRDKPVII----GGGK---------------------RG------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 473 ssvwenqdstqtngidsVLSkaeiaSCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDF----HACREVAQAMyETLasy 548
Cdd:PRK02794 72 -----------------VVS-----TACYIARIHGVRSAMPMFKALKLCPDAVVIKPDMekyvRVGREVRAMM-QAL--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 549 THSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDF 628
Cdd:PRK02794 126 TPLVEPLSIDEAFLDLSGTERLHGAPPAVVLARFARRVEREIGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 629 IRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGI 708
Cdd:PRK02794 206 LAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFET 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 709 RFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpgapIETAKFGGHgicdniARTVTLDQATDSAKIIGKAT 788
Cdd:PRK02794 285 DLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLK---------LKTADFRLR------TRRRTLEDPTQLADRIFRTA 349
|
410 420
....*....|....*....|....*..
gi 1907069828 789 LNMFHTMkLNISDMRGVGIQVNQLVPA 815
Cdd:PRK02794 350 RELLEKE-TDGTAFRLIGIGVSDLSPA 375
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1145-1238 |
2.08e-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: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 1145 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1224
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069828 1225 QVVLQQTYGSTLKV 1238
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
407-745 |
4.33e-40 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 152.10 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrGTGtaplrpganpqlewqyyqnralrgkaadipdssvwenqDSTQTNG 486
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIVG---GNG--------------------------------------DPTEPRK 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 IdsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALI--DV 564
Cdd:PRK03352 46 V--------VTCASYEARAFGVRAGMPLRTAARRCPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLgvDT 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 565 TDilaetklsPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSM 644
Cdd:PRK03352 118 DD--------PEALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 645 ESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSL 723
Cdd:PRK03352 190 AKRLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVREL 269
|
330 340
....*....|....*....|..
gi 1907069828 724 SEEIQRRLEAAGMKGKRLTLKI 745
Cdd:PRK03352 270 ARRVLDEVVAEGRPVTRVAVKV 291
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
408-745 |
6.95e-33 |
|
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: 131.13 E-value: 6.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 408 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgtaplrpganpqlewqyyqnralrgkaadiPDSSVwenqdstqtngi 487
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSN---------------------------------NDGCV------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 488 dsvlskaeIAScSYEARQVGIKNGMFFGYAKQLCPNLQAV---P-YDFHAcrEVAQAMYETLASYTHSIEAVSCDEALID 563
Cdd:cd01700 36 --------IAR-SPEAKALGIKMGSPYFKVPDLLERHGVAvfsSnYALYG--DMSRRIMSILERFSPDVEVYSIDESFLD 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 564 VTDILaeTKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMAT----KKAKPDGQYHLQPDEVDDFIRGQL-VTNLP 638
Cdd:cd01700 105 LTGSL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLANdlakKKNPYGGVVDLTDEEVRDKLLKILpVGDVW 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 639 GVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAE 717
Cdd:cd01700 183 GIGRRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELNGIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELK 261
|
330 340
....*....|....*....|....*...
gi 1907069828 718 AFLLSLSEEIQRRLEAAGMKGKRLTLKI 745
Cdd:cd01700 262 QALAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
407-699 |
1.13e-32 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 130.68 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 407 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrgtgtaplrpganpqlewqYYQNRalrgkaadipdssvweNQDStqtng 486
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVC---------------------VYSGR----------------FEDS----- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 487 idsvlskAEIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTD 566
Cdd:PRK01216 41 -------GAVATANYEARKLGIKAGMPIVEAKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 567 ILAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMES 646
Cdd:PRK01216 114 KVKNYQ-DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAE 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907069828 647 KLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTeKERKS 699
Cdd:PRK01216 193 KLKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRA-RVRKS 244
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
409-794 |
5.84e-29 |
|
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: 120.11 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 409 HVDMDCFFVSVGIRNRPDLKGKPVAVTsnrgtgtaplrpganpqlewqyyqnralrgkaadipdssvwenqdstQTNGID 488
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAVV-----------------------------------------------QWNSII 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 489 SVlskaeiascSYEARQVGIKNGMFFGYAKQLCPNLQAV----------------------------PYDfHACREVAqa 540
Cdd:cd01702 35 AV---------SYAARAFGVTRFMTIDEAKKKCPDLILAhvatykkgedeadyhenpsparhkvsldPYR-RASRKIL-- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 541 myETLASYTHSIEAVSCDEALIDVTDILAETklspeefaaaLRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHL 620
Cdd:cd01702 103 --NILKRFGDVVEKASIDEAYLDLGSRIVEE----------IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTIL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 621 QPDEVDDFIRGQLVTNLPGVGRSM-ESKLASLGIKTCGDLQCL--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER 697
Cdd:cd01702 171 RNDAVASFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 698 KSVSAEINY-GIRFTQPKEAEAFLLSLSEEIQRRLEAA----GMKGKRLTLKIMVRKPGAPIEtakfgghgICDNIARTV 772
Cdd:cd01702 251 KSMGSSKNFpGKTALSTEDVQHWLLVLASELNSRLEDDryenNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYD 322
|
410 420
....*....|....*....|..
gi 1907069828 773 TLDQATDSAKIIGKATLNMFHT 794
Cdd:cd01702 323 AQKIVKDAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
409-750 |
2.57e-27 |
|
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: 115.65 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 409 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgtaplrpganpqlewqyyQNRALrgkaadipdssvwenqdstqtngid 488
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGI------------------------QQKYI------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 489 svlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAV------PYdfhacREVAQAMYETLASYT--HSIEAVSCDEA 560
Cdd:cd01703 33 -------VVTCNYEARRLGVKKLMSIKDAKEICPDLVLVngedltPF-----RDMSKKVYRLLRSYSwnDRVERLGFDEN 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 561 LIDVTDIlaeTKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQP---DEVDDFIRGQLVTNL 637
Cdd:cd01703 101 FMDVTEM---RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPpscADLMDFMDLHDLRKI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 638 PGVGRSMESKLASLGIKTCGDLQ---------------CLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVS 701
Cdd:cd01703 178 PGIGYKTAAKLEAHGISSVRDLQefsnrnrqtvgaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQIS 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069828 702 AEINYG-IRFTQPKEAEAFLLSLSEEIQRRL------EAAGMKGKRLTLKIMVRKP 750
Cdd:cd01703 258 IEDSYKkCSLEEIREARNKIEELLASLLERMkqdlqeVKAGDGRRPHTLRLTLRRY 313
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
496-744 |
6.44e-23 |
|
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: 101.69 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 496 IASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHAcrevAQAMYETLAS----YTHSIEAVSCDEALIDVTdilAET 571
Cdd:cd03468 36 ILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDPEA----DARALQELALwllrFTPLVALDGPDGLLLDVT---GCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 572 KLSPEEFAAALRIEIKDKTKC-AASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLAS 650
Cdd:cd03468 109 HLFGGEDALAASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 651 LGIKTCGDLQCLTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQ 728
Cdd:cd03468 189 LGLRTLGDLAALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLC 265
|
250
....*....|....*.
gi 1907069828 729 RRLEAAGMKGKRLTLK 744
Cdd:cd03468 266 AFLALRGLGARRLSLT 281
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
398-745 |
1.29e-21 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 100.86 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 398 LSSPRHQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgtaplrpganpqlewqyyqnralrgkaadipdssvwe 477
Cdd:PTZ00205 126 LEATRRLGTYIHLDMDMFYAAVEIKKHPEYAAIPLAI------------------------------------------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 478 nqdstqtnGIDSVLSKAeiascSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSC 557
Cdd:PTZ00205 163 --------GTMTMLQTA-----NYVARGRGIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 558 DEALIDVTDILA--ETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQ---PDEVDDFIRGQ 632
Cdd:PTZ00205 230 DELTLEVSAYIErfEGTKTAEDVASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 633 LVTNLPGVGRSMESKLASLGIKTCGDLQ------CLTMAKLQKEF--GPKTGQMLY-RFCRGLDDRPVR--TEKERKSVS 701
Cdd:PTZ00205 310 GLRSVPGVGKVTEALLKGLGITTLSDIYnrrvelCYILHNNLFRFllGASIGIMQWpDAATAANTENCEgaTGGQRKAIS 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907069828 702 AEINYGIrFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKI 745
Cdd:PTZ00205 390 SERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKSELMCRQISLTI 432
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
697-816 |
5.95e-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: 88.77 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 697 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMvrkpgapieTAKFgghgicDNIARTVTLDQ 776
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907069828 777 ATDSAKIIGKATLNMFHTMKLNIsDMRGVGIQVNQLVPAN 816
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 ... |
1155-1236 |
1.34e-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: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 1155 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1225
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069828 1226 VVLQQTYGSTL 1236
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
995-1030 |
9.10e-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: 9.10e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1907069828 995 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 1030
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
919-952 |
1.45e-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: 1.45e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069828 919 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 952
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 |
7.39e-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: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSA 127
Cdd:pfam16589 4 LFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLE 82
|
..
gi 1907069828 128 PY 129
Cdd:pfam16589 83 NY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
48-118 |
1.93e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 58.16 E-value: 1.93e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069828 48 IFSGVAIYVNGYTD-PSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 3 LFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| 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 |
3.13e-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: 3.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069828 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 |
6.98e-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: 6.98e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069828 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKELK-GEKVIRPEWIVESI 118
Cdd:pfam00533 5 LFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSK-KTTHVIVEARTKKYLKAKElGIPIVTEEWLLDCI 75
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
409-711 |
2.08e-09 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 61.32 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 409 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRgtgtaplrpganpqlewqyyqnralrgkaadipDSSVwenqdstqtngid 488
Cdd:PRK03609 4 LCDVNSFYASCETVFRPDLRGKPVVVLSNN---------------------------------DGCV------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 489 svlskaeIAsCSYEARQVGIKNGMffGYAKQLCPNLQAVPYDFHACREVAQAMYE----TLASYTHSIEAVSCDEALIDV 564
Cdd:PRK03609 38 -------IA-RSAEAKALGIKMGD--PWFKQKDLFRRCGVVCFSSNYELYADMSNrvmsTLEELSPRVEIYSIDEAFCDL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 565 TDIlaETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKpdgQYHLQPDEVDDFIRGQ----LVTNLP-- 638
Cdd:PRK03609 108 TGV--RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAK---KWQRQTGGVVDLSNLErqrkLLSLQPve 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 639 ---GVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 711
Cdd:PRK03609 183 evwGVGRRISKKLNAMGIKTALDLADTNIRFIRKHF----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 |
3.68e-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: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 48 IFSGVAIYV-NGYTDP-SAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 1907069828 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 |
1.72e-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: 1.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069828 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 |
8.83e-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: 8.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069828 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 |
1.78e-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: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 51 GVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSSAP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 1907069828 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 |
1.81e-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: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 48 IFSGVAIYVNGYtdpSAEELRNL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 1907069828 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 |
4.79e-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: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 49 FSGVAIYVNGYTDPSAEELrnlmmLH-GGQYHVYYSRSKTTHIIATNLPNAKIKELK--GEK-VIRPEWIVESIKAGRLL 124
Cdd:cd17714 1 FKDVKYFVVGNLDEKVEQL-----LKnGGAKEVSYLSDMATHVIVDDNDNPEVGEARdlFELpVVTSSWVILSIKAGKLL 75
|
.
gi 1907069828 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 |
1.12e-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: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 44 TASAIFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 1907069828 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 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069828 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. |
622-653 |
5.49e-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: 5.49e-04
10 20 30
....*....|....*....|....*....|..
gi 1907069828 622 PDEVDDFIRGQLVTNLPGVGRSMESKLASLGI 653
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 |
7.28e-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: 7.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069828 54 IYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIAtnlpnakiKELKGEK----------VIRPEW 113
Cdd:pfam12738 3 ICVTGFDGDDREGLQKLIEAMGAEYTKDLTK-SVTHLIC--------KSGEGEKyekakewgipVVSPLW 63
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