|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
346-821 |
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: 615.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 346 FISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPgreklkkvktgrsslvvtdtgtmSVLSSPRHQSCVMHVDMDCF 425
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 426 FVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngidsvlsKAEI 505
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP---------------------------------------------------NSEI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 506 ASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPE 585
Cdd:cd01701 87 ASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 586 EFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTC 665
Cdd:cd01701 167 ELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 666 GD--LQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAA 743
Cdd:cd01701 247 GGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEES 326
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069840 744 GMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 821
Cdd:cd01701 327 NVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
417-818 |
3.12e-88 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 289.35 E-value: 3.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngi 496
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 576
Cdd:COG0389 39 --------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 577 LAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESK 656
Cdd:COG0389 111 ARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 657 LASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 736
Cdd:COG0389 190 LARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 737 QRRLEAAGMKGKRLTLKimvrkpgapIETAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGI 816
Cdd:COG0389 269 AERLRRQGLGARTVTVK---------LRTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGV 333
|
..
gi 1907069840 817 QV 818
Cdd:COG0389 334 RL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
422-754 |
1.79e-70 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 239.64 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 422 MDCFFVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralRGkadipdssvwenqdstqtngidsVls 501
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAVGGSPGR-----------------------RG-----------------------V-- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 502 kaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAEtK 581
Cdd:PRK02406 33 ---ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLC-I 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 582 LSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLG 661
Cdd:PRK02406 109 GSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 662 IKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLE 741
Cdd:PRK02406 189 IYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLE 267
|
330
....*....|....*
gi 1907069840 742 AAGM--KGKRLTLKI 754
Cdd:PRK02406 268 RAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
3.90e-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: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1907069840 125 SSAPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
420-619 |
7.08e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 158.89 E-value: 7.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 420 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngidsv 499
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGI----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 500 lskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASY-THSIEAVSCDEALIDVTDiLA 578
Cdd:pfam00817 34 -----VAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907069840 579 ETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATK 619
Cdd:pfam00817 108 KLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1154-1247 |
2.09e-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: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 1154 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1233
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069840 1234 QVVLQQTYGSTLKV 1247
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 ... |
1164-1245 |
1.35e-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: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 1164 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1234
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069840 1235 VVLQQTYGSTL 1245
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1004-1039 |
8.72e-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: 8.72e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1907069840 1004 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 1039
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
928-961 |
1.35e-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: 1.35e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069840 928 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 961
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
48-129 |
7.45e-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: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSA 127
Cdd:pfam16589 4 LFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLE 82
|
..
gi 1907069840 128 PY 129
Cdd:pfam16589 83 NY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
48-118 |
1.95e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 58.16 E-value: 1.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069840 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. ... |
346-821 |
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: 615.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 346 FISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPgreklkkvktgrsslvvtdtgtmSVLSSPRHQSCVMHVDMDCF 425
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 426 FVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngidsvlsKAEI 505
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP---------------------------------------------------NSEI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 506 ASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPE 585
Cdd:cd01701 87 ASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 586 EFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTC 665
Cdd:cd01701 167 ELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 666 GD--LQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAA 743
Cdd:cd01701 247 GGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEES 326
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069840 744 GMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 821
Cdd:cd01701 327 NVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
418-821 |
1.95e-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: 303.67 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 418 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgtaplrpganpqlewqyyqnralrgkadiPDSSVwenqdstqtngid 497
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVGGS--------------------------------SDRGV------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 498 svlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDIL 577
Cdd:cd03586 36 -------VSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPRFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 578 AETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKL 657
Cdd:cd03586 109 RLFG-SATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 658 ASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQ 737
Cdd:cd03586 188 KELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEELA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 738 RRLEAAGMKGKRLTLKImvrkpgapietaKFGGHgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISdMRGVGIQ 817
Cdd:cd03586 267 ERLRKRGLKGRTVTVKL------------KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVR 330
|
....
gi 1907069840 818 VNQL 821
Cdd:cd03586 331 LSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
417-818 |
3.12e-88 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 289.35 E-value: 3.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngi 496
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 576
Cdd:COG0389 39 --------VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 577 LAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESK 656
Cdd:COG0389 111 ARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 657 LASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEI 736
Cdd:COG0389 190 LARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 737 QRRLEAAGMKGKRLTLKimvrkpgapIETAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGI 816
Cdd:COG0389 269 AERLRRQGLGARTVTVK---------LRTSDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGV 333
|
..
gi 1907069840 817 QV 818
Cdd:COG0389 334 RL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
422-754 |
1.79e-70 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 239.64 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 422 MDCFFVSVGIRNRPDLKGKPVAVTSNRGTgtaplrpganpqlewqyyqnralRGkadipdssvwenqdstqtngidsVls 501
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAVGGSPGR-----------------------RG-----------------------V-- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 502 kaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAEtK 581
Cdd:PRK02406 33 ---ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLC-I 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 582 LSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLG 661
Cdd:PRK02406 109 GSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 662 IKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLE 741
Cdd:PRK02406 189 IYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLE 267
|
330
....*....|....*
gi 1907069840 742 AAGM--KGKRLTLKI 754
Cdd:PRK02406 268 RAKPdkRIKTVGVKL 282
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
417-793 |
2.54e-54 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 197.08 E-value: 2.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgtaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtn 494
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 495 gidsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAV-PYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDV 573
Cdd:PRK03348 43 ----------VAGASYEARVFGARSAMPMHQARRLVGNGAVVlPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 574 TDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSM 653
Cdd:PRK03348 113 AELAGASAEEVEAFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 654 ESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLS 733
Cdd:PRK03348 193 EEKLHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIA 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 734 EEIQRRLEAAGMKGKRLTLKimVRKPGAPIETakfgghgicdniaRTVTLDQATDSAKII 793
Cdd:PRK03348 273 EHAHRRLLKDGRGARTVTVK--LRKSDFSTLT-------------RSATLPYATDDAAVL 317
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
419-752 |
2.34e-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: 190.65 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 419 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTAplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngids 498
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNSDSTC--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 499 vlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDIlA 578
Cdd:cd00424 37 ------VIACSYEARKYGVKRGMPVREARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS-A 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 579 ETKLSPEEFAAALRIEIKDKTK-CAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKL 657
Cdd:cd00424 110 RLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 658 ASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQ 737
Cdd:cd00424 190 EAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLA 269
|
330
....*....|....*
gi 1907069840 738 RRLEAAGMKGKRLTL 752
Cdd:cd00424 270 RRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
417-830 |
2.12e-50 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 182.22 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgtaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtn 494
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGV-------------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 495 gidsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVT 574
Cdd:PRK14133 41 ----------VSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDIT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 575 DIlaetKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSME 654
Cdd:PRK14133 111 NI----KEEPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 655 SKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSE 734
Cdd:PRK14133 187 EKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 735 EIQRRLEAAGMKGKRLTLKimvrkpgapIETAKFGGHgicdniARTVTLDQATDSAKIIGKATLNMFHTMKLNiSDMRGV 814
Cdd:PRK14133 266 IISEELKKRNLYGKTVTVK---------IKTSDFQTH------TKSKTLNDYIRDKEEIYNVACEILEHINIK-EPIRLI 329
|
410
....*....|....*.
gi 1907069840 815 GIQVnqlvpanSNLST 830
Cdd:PRK14133 330 GLSV-------SNLSE 338
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
3.90e-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: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1907069840 125 SSAPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
417-801 |
1.55e-47 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 175.60 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgtaplrpganpqlewqyyqnralrgkadipdssvwenqdSTQTNGI 496
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVAGN------------------------------------------EKERKGI 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 576
Cdd:PRK01810 45 --------IVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDC 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 577 LAetKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESK 656
Cdd:PRK01810 117 YA--LGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 657 LASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSE 734
Cdd:PRK01810 195 LKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSK 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069840 735 EIQRRLEAAGMKGKrlTLKIMVRkpgapieTAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMF 801
Cdd:PRK01810 274 SVSKRLQKKTVVSY--NVQIMIR-------YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
417-825 |
1.66e-45 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 169.80 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTSnrgtgtaplrpganpqlewqyyqnralrgkadipdssvwenqDSTQTNGI 496
Cdd:PRK03103 5 ILLVDMQSFYASVEKAANPELKGRPVIVSG------------------------------------------DPERRSGV 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsVLskaeiASCsYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 576
Cdd:PRK03103 43 --VL-----AAC-PLAKAYGVKTAERLWEAQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 577 LaetKL--SPEEFAAALRIEIKDKTKCAASVGIGSNILLARMAT---KKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGR 651
Cdd:PRK03103 115 Q---KLfgSPLEIAQKIQQRIMRETGVYARVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 652 SMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFL 729
Cdd:PRK03103 192 RMEKHLRRMGIRTIGQLANTPLERLKKRWG-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 730 LSLSEEIQRRLEAAGMKGKrlTLKIMVRkpGAPIETAKfgghgicdNIARTVTLDQATDSAKIIGKATLNMFHTMkLNIS 809
Cdd:PRK03103 271 LELCEEVCRRARAKGYMGR--TVSVSLR--GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGK 337
|
410
....*....|....*.
gi 1907069840 810 DMRGVGIQVNQLVPAN 825
Cdd:PRK03103 338 PVRRVGVTLSNLVSDD 353
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
420-619 |
7.08e-45 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 158.89 E-value: 7.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 420 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngidsv 499
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGI----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 500 lskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASY-THSIEAVSCDEALIDVTDiLA 578
Cdd:pfam00817 34 -----VAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907069840 579 ETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATK 619
Cdd:pfam00817 108 KLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
417-789 |
1.36e-42 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 160.92 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGTaplrpganpqlewqyyqnralrgkadipdssvwenqdstqtngi 496
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIV----GGGV-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsVLSkaeiasCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 576
Cdd:PRK03858 38 --VLA------ASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGGL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 577 laeTKLS--PEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSME 654
Cdd:PRK03858 110 ---RRISgtPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 655 SKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSE 734
Cdd:PRK03858 187 AKLRAHGITTVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069840 735 EIQRRLEAAGMKGKRLTLKImvrkpgapietaKFGGHGicdNIARTVTLDQATDS 789
Cdd:PRK03858 267 RVARRMRAAGRTGRTVVLRL------------RFDDFT---RATRSHTLPRPTAS 306
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
410-824 |
9.44e-42 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 158.94 E-value: 9.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 410 SPR-------HQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGTaplrpganpqlewqyyqnralRGkadipds 482
Cdd:PRK02794 24 SPRlvrhpelYTLSIAHIDCDAFYASVEKRDNPELRDKPVII----GGGK---------------------RG------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 483 svwenqdstqtngidsVLSkaeiaSCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDF----HACREVAQAMyETLasyT 558
Cdd:PRK02794 72 ----------------VVS-----TACYIARIHGVRSAMPMFKALKLCPDAVVIKPDMekyvRVGREVRAMM-QAL---T 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 559 HSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFI 638
Cdd:PRK02794 127 PLVEPLSIDEAFLDLSGTERLHGAPPAVVLARFARRVEREIGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 639 RGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIR 718
Cdd:PRK02794 207 APKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 719 FTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpgapIETAKFGGHgicdniARTVTLDQATDSAKIIGKATL 798
Cdd:PRK02794 286 LSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLK---------LKTADFRLR------TRRRTLEDPTQLADRIFRTAR 350
|
410 420
....*....|....*....|....*.
gi 1907069840 799 NMFHTMkLNISDMRGVGIQVNQLVPA 824
Cdd:PRK02794 351 ELLEKE-TDGTAFRLIGIGVSDLSPA 375
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1154-1247 |
2.09e-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: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 1154 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1233
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069840 1234 QVVLQQTYGSTLKV 1247
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
417-754 |
3.23e-40 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 152.48 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrGTGtaplrpganpqlewqyyqnralrgkadipdssvwenqDSTQTNGI 496
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIVG---GNG-------------------------------------DPTEPRKV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsvlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALI--DVT 574
Cdd:PRK03352 47 --------VTCASYEARAFGVRAGMPLRTAARRCPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLgvDTD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 575 DilaetklsPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSME 654
Cdd:PRK03352 119 D--------PEALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 655 SKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLS 733
Cdd:PRK03352 191 KRLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELA 270
|
330 340
....*....|....*....|.
gi 1907069840 734 EEIQRRLEAAGMKGKRLTLKI 754
Cdd:PRK03352 271 RRVLDEVVAEGRPVTRVAVKV 291
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
418-754 |
5.18e-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: 131.52 E-value: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 418 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgtaplrpganpqlewqyyqnralrgkadiPDSSVwenqdstqtngid 497
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSN--------------------------------NDGCV------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 498 svlskaeIAScSYEARQVGIKNGMFFGYAKQLCPNLQAV---P-YDFHAcrEVAQAMYETLASYTHSIEAVSCDEALIDV 573
Cdd:cd01700 36 -------IAR-SPEAKALGIKMGSPYFKVPDLLERHGVAvfsSnYALYG--DMSRRIMSILERFSPDVEVYSIDESFLDL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 574 TDILaeTKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMAT----KKAKPDGQYHLQPDEVDDFIRGQL-VTNLPG 648
Cdd:cd01700 106 TGSL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLANdlakKKNPYGGVVDLTDEEVRDKLLKILpVGDVWG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 649 VGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEA 727
Cdd:cd01700 184 IGRRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELNGIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQ 262
|
330 340
....*....|....*....|....*..
gi 1907069840 728 FLLSLSEEIQRRLEAAGMKGKRLTLKI 754
Cdd:cd01700 263 ALAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
417-708 |
8.40e-33 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 131.07 E-value: 8.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 417 VMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrgtgtaplrpganpqlewqYYQNRalrgkadipdssvweNQDStqtngi 496
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVC---------------------VYSGR---------------FEDS------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 497 dsvlskAEIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDI 576
Cdd:PRK01216 41 ------GAVATANYEARKLGIKAGMPIVEAKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 577 LAETKlSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESK 656
Cdd:PRK01216 115 VKNYQ-DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEK 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907069840 657 LASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTeKERKS 708
Cdd:PRK01216 194 LKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRA-RVRKS 244
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
419-803 |
4.29e-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: 120.50 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 419 HVDMDCFFVSVGIRNRPDLKGKPVAVTsnrgtgtaplrpganpqlewqyyqnralrgkadipdssvwenqdstQTNGIDS 498
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAVV----------------------------------------------QWNSIIA 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 499 VlskaeiascSYEARQVGIKNGMFFGYAKQLCPNLQAV----------------------------PYDfHACREVAqam 550
Cdd:cd01702 36 V---------SYAARAFGVTRFMTIDEAKKKCPDLILAhvatykkgedeadyhenpsparhkvsldPYR-RASRKIL--- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 551 yETLASYTHSIEAVSCDEALIDVTDILAETklspeefaaaLRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQ 630
Cdd:cd01702 103 -NILKRFGDVVEKASIDEAYLDLGSRIVEE----------IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 631 PDEVDDFIRGQLVTNLPGVGRSM-ESKLASLGIKTCGDLQCL--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERK 707
Cdd:cd01702 172 NDAVASFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 708 SVSAEINY-GIRFTQPKEAEAFLLSLSEEIQRRLEAA----GMKGKRLTLKIMVRKPGAPIEtakfgghgICDNIARTVT 782
Cdd:cd01702 252 SMGSSKNFpGKTALSTEDVQHWLLVLASELNSRLEDDryenNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYDA 323
|
410 420
....*....|....*....|.
gi 1907069840 783 LDQATDSAKIIGKATLNMFHT 803
Cdd:cd01702 324 QKIVKDAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
419-759 |
2.13e-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: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 419 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgtaplrpganpqlewqyyQNRALrgkadipdssvwenqdstqtngids 498
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGI------------------------QQKYI------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 499 vlskaeIASCSYEARQVGIKNGMFFGYAKQLCPNLQAV------PYdfhacREVAQAMYETLASYT--HSIEAVSCDEAL 570
Cdd:cd01703 33 ------VVTCNYEARRLGVKKLMSIKDAKEICPDLVLVngedltPF-----RDMSKKVYRLLRSYSwnDRVERLGFDENF 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 571 IDVTDIlaeTKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQP---DEVDDFIRGQLVTNLP 647
Cdd:cd01703 102 MDVTEM---RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPpscADLMDFMDLHDLRKIP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 648 GVGRSMESKLASLGIKTCGDLQ---------------CLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVSA 711
Cdd:cd01703 179 GIGYKTAAKLEAHGISSVRDLQefsnrnrqtvgaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQISI 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069840 712 EINYG-IRFTQPKEAEAFLLSLSEEIQRRL------EAAGMKGKRLTLKIMVRKP 759
Cdd:cd01703 259 EDSYKkCSLEEIREARNKIEELLASLLERMkqdlqeVKAGDGRRPHTLRLTLRRY 313
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
505-753 |
6.49e-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: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 505 IASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHAcrevAQAMYETLAS----YTHSIEAVSCDEALIDVTdilAET 580
Cdd:cd03468 36 ILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDPEA----DARALQELALwllrFTPLVALDGPDGLLLDVT---GCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 581 KLSPEEFAAALRIEIKDKTKC-AASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLAS 659
Cdd:cd03468 109 HLFGGEDALAASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 660 LGIKTCGDLQCLTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQ 737
Cdd:cd03468 189 LGLRTLGDLAALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLC 265
|
250
....*....|....*.
gi 1907069840 738 RRLEAAGMKGKRLTLK 753
Cdd:cd03468 266 AFLALRGLGARRLSLT 281
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
408-754 |
9.83e-22 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 101.25 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 408 LSSPRHQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgtaplrpganpqlewqyyqnralrgkadipdssvwen 487
Cdd:PTZ00205 126 LEATRRLGTYIHLDMDMFYAAVEIKKHPEYAAIPLAI------------------------------------------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 488 qdstqtnGIDSVLSKAeiascSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCD 567
Cdd:PTZ00205 163 -------GTMTMLQTA-----NYVARGRGIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 568 EALIDVTDILA--ETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQ---PDEVDDFIRGQL 642
Cdd:PTZ00205 231 ELTLEVSAYIErfEGTKTAEDVASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 643 VTNLPGVGRSMESKLASLGIKTCGDLQ------CLTMAKLQKEF--GPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSA 711
Cdd:PTZ00205 311 LRSVPGVGKVTEALLKGLGITTLSDIYnrrvelCYILHNNLFRFllGASIGIMQWpDAATAANTENCEgaTGGQRKAISS 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907069840 712 EINYGIrFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKI 754
Cdd:PTZ00205 391 ERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKSELMCRQISLTI 432
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
706-825 |
6.87e-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: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 706 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMvrkpgapieTAKFgghgicDNIARTVTLDQ 785
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907069840 786 ATDSAKIIGKATLNMFHTMKLNIsDMRGVGIQVNQLVPAN 825
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 ... |
1164-1245 |
1.35e-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: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 1164 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1234
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069840 1235 VVLQQTYGSTL 1245
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1004-1039 |
8.72e-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: 8.72e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1907069840 1004 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 1039
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
928-961 |
1.35e-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: 1.35e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069840 928 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 961
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
48-129 |
7.45e-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: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSA 127
Cdd:pfam16589 4 LFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLE 82
|
..
gi 1907069840 128 PY 129
Cdd:pfam16589 83 NY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
48-118 |
1.95e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 58.16 E-value: 1.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069840 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 |
3.15e-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: 3.15e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069840 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 |
7.03e-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: 7.03e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069840 48 IFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKELK-GEKVIRPEWIVESI 118
Cdd:pfam00533 5 LFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSK-KTTHVIVEARTKKYLKAKElGIPIVTEEWLLDCI 75
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
419-720 |
1.60e-09 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 61.70 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 419 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRgtgtaplrpganpqlewqyyqnralrgkadipDSSVwenqdstqtngids 498
Cdd:PRK03609 4 LCDVNSFYASCETVFRPDLRGKPVVVLSNN--------------------------------DGCV-------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 499 vlskaeIAsCSYEARQVGIKNGMffGYAKQLCPNLQAVPYDFHACREVAQAMYE----TLASYTHSIEAVSCDEALIDVT 574
Cdd:PRK03609 38 ------IA-RSAEAKALGIKMGD--PWFKQKDLFRRCGVVCFSSNYELYADMSNrvmsTLEELSPRVEIYSIDEAFCDLT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 575 DIlaETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKpdgQYHLQPDEVDDFIRGQ----LVTNLP--- 647
Cdd:PRK03609 109 GV--RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAK---KWQRQTGGVVDLSNLErqrkLLSLQPvee 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069840 648 --GVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 720
Cdd:PRK03609 184 vwGVGRRISKKLNAMGIKTALDLADTNIRFIRKHF----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 |
3.67e-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: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 48 IFSGVAIYV-NGYTDP-SAEELRNLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 1907069840 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 |
1.73e-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: 1.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069840 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 |
9.07e-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: 9.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069840 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 |
1.79e-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: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 51 GVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSSAP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 1907069840 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 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 48 IFSGVAIYVNGYtdpSAEELRNL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 1907069840 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 |
4.83e-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: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 49 FSGVAIYVNGYTDPSAEELrnlmmLH-GGQYHVYYSRSKTTHIIATNLPNAKIKELK--GEK-VIRPEWIVESIKAGRLL 124
Cdd:cd17714 1 FKDVKYFVVGNLDEKVEQL-----LKnGGAKEVSYLSDMATHVIVDDNDNPEVGEARdlFELpVVTSSWVILSIKAGKLL 75
|
.
gi 1907069840 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 |
1.13e-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: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 44 TASAIFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 1907069840 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 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069840 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. |
631-662 |
5.53e-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: 5.53e-04
10 20 30
....*....|....*....|....*....|..
gi 1907069840 631 PDEVDDFIRGQLVTNLPGVGRSMESKLASLGI 662
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 |
7.33e-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: 7.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069840 54 IYVNGYTDPSAEELRNLMMLHGGQYHVYYSRsKTTHIIAtnlpnakiKELKGEK----------VIRPEW 113
Cdd:pfam12738 3 ICVTGFDGDDREGLQKLIEAMGAEYTKDLTK-SVTHLIC--------KSGEGEKyekakewgipVVSPLW 63
|
|
| |
