|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-860 |
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: 622.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangidsvlsRAE 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP----------------------------------------------------NSE 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 508 IASCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQ 587
Cdd:cd01701 86 IASCNYEARSY------------------------------------GIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSL 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 588 TLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYH 667
Cdd:cd01701 130 TFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYH 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 668 LKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER 745
Cdd:cd01701 210 LSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKER 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 746 KSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQA 825
Cdd:cd01701 290 KSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVA 369
|
490 500 510
....*....|....*....|....*....|....*
gi 1034614580 826 TDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 860
Cdd:cd01701 370 TDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-857 |
9.27e-84 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 277.03 E-value: 9.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqang 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 499 idsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYD 578
Cdd:COG0389 39 ---------VAAASYEAR------------------------------------AFGVRSGMPLFQARRLCPDLVVLPPD 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 579 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:COG0389 74 FELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASD 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 659 KAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRP 738
Cdd:COG0389 153 LAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 739 VRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIAR 818
Cdd:COG0389 232 VEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVKL---------RTSDF------RTTTR 296
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034614580 819 TVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHV 857
Cdd:COG0389 297 SRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-793 |
5.13e-66 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 227.31 E-value: 5.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkGKAADipdsslwenpdsaqangidsvl 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV------------------------------GGSPG---------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 504 SRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYK 583
Cdd:PRK02406 29 RRGVISTCNYEAR------------------------------------KFGVRSAMPTAQALKLCPDLIFVPGRFDVYK 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 584 EVAQTLYETLASYTHNIEAVSCDEALVDITE----ILAETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRK 659
Cdd:PRK02406 73 EVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIGSATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDW 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 660 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV 739
Cdd:PRK02406 148 NKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPV 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034614580 740 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGM--KGKRLTLKI 793
Cdd:PRK02406 227 KPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
5.10e-49 |
|
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.
Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 168.52 E-value: 5.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1034614580 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1193-1286 |
4.90e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 213388 Cd Length: 94 Bit Score: 148.96 E-value: 4.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 1193 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1272
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1034614580 1273 QVVLQQTYGSTLKV 1286
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-658 |
1.44e-38 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 140.79 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangids 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 502 vlsRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHA 581
Cdd:pfam00817 31 ---RGIVAAASYEAR------------------------------------KYGVRSGMPVFEAKKLCPNLIVVPPDLEL 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034614580 582 YKEVAQTLYETLASY-THNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:pfam00817 72 YRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1203-1284 |
5.42e-17 |
|
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein REV1. It interacts with REV7, POLN, POLK and POLI.
Pssm-ID: 465248 Cd Length: 91 Bit Score: 77.27 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 1203 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1273
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1034614580 1274 VVLQQTYGSTL 1284
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1041-1076 |
4.00e-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: 73.03 E-value: 4.00e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1034614580 1041 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1076
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
965-998 |
1.37e-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: 1.37e-12
10 20 30
....*....|....*....|....*....|....
gi 1034614580 965 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 998
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
45-129 |
5.20e-12 |
|
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.
Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 62.77 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 1034614580 125 SYIPY 129
Cdd:pfam16589 80 PLENY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
46-118 |
7.79e-11 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 59.31 E-value: 7.79e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034614580 46 STIFSGVAIYVNGYTD-PSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 1 PKLFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
1047-1078 |
2.69e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 36.71 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|..
gi 1034614580 1047 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1078
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
969-990 |
6.51e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 35.56 E-value: 6.51e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-860 |
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: 622.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangidsvlsRAE 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP----------------------------------------------------NSE 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 508 IASCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQ 587
Cdd:cd01701 86 IASCNYEARSY------------------------------------GIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSL 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 588 TLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYH 667
Cdd:cd01701 130 TFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYH 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 668 LKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER 745
Cdd:cd01701 210 LSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKER 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 746 KSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQA 825
Cdd:cd01701 290 KSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVA 369
|
490 500 510
....*....|....*....|....*....|....*
gi 1034614580 826 TDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 860
Cdd:cd01701 370 TDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
420-860 |
2.80e-85 |
|
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: 281.33 E-value: 2.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtGRAPLRpganpqlewqyyqnkilkgkaadipdsslwenpdsaqanGI 499
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAV------GGSSDR---------------------------------------GV 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 500 dsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDF 579
Cdd:cd03586 36 --------VSTASYEAR------------------------------------KFGVRSAMPIFQAKKLCPNLIFVPPRF 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 580 HAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 659
Cdd:cd03586 72 DKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYVRLFG-SATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 660 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV 739
Cdd:cd03586 151 NKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPV 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 740 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHgicDNIART 819
Cdd:cd03586 230 EPDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVKL------------KYADF---STRTRS 294
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1034614580 820 VTLDQATDNAKIIGKAMLNMFHTMKLNISdMRGVGIHVNQL 860
Cdd:cd03586 295 RTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVRLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-857 |
9.27e-84 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 277.03 E-value: 9.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqang 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 499 idsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYD 578
Cdd:COG0389 39 ---------VAAASYEAR------------------------------------AFGVRSGMPLFQARRLCPDLVVLPPD 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 579 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:COG0389 74 FELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASD 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 659 KAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRP 738
Cdd:COG0389 153 LAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 739 VRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIAR 818
Cdd:COG0389 232 VEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVKL---------RTSDF------RTTTR 296
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034614580 819 TVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHV 857
Cdd:COG0389 297 SRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-793 |
5.13e-66 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 227.31 E-value: 5.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkGKAADipdsslwenpdsaqangidsvl 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV------------------------------GGSPG---------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 504 SRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYK 583
Cdd:PRK02406 29 RRGVISTCNYEAR------------------------------------KFGVRSAMPTAQALKLCPDLIFVPGRFDVYK 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 584 EVAQTLYETLASYTHNIEAVSCDEALVDITE----ILAETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRK 659
Cdd:PRK02406 73 EVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIGSATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDW 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 660 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV 739
Cdd:PRK02406 148 NKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPV 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034614580 740 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGM--KGKRLTLKI 793
Cdd:PRK02406 227 KPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 282
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
48-131 |
5.10e-49 |
|
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.
Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 168.52 E-value: 5.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1034614580 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
419-832 |
8.70e-49 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 180.90 E-value: 8.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqa 496
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 497 ngidsvlsraeIASCSYEARSLkvlepwllprvmsyhvqccwhlnhcGATSGawnwqlgikngMFFGHAKQLCPNLQAV- 575
Cdd:PRK03348 43 -----------VAGASYEARVF-------------------------GARSA-----------MPMHQARRLVGNGAVVl 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 576 PYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARM 655
Cdd:PRK03348 76 PPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEPAELAGASAEEVEAFAERLRARVREETGLPASVGAGSGKQIAKI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 656 ATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLD 735
Cdd:PRK03348 156 ASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGID 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 736 DRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKimVRKPGAPVETakfgghgicdn 815
Cdd:PRK03348 236 DRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRGARTVTVK--LRKSDFSTLT----------- 302
|
410
....*....|....*..
gi 1034614580 816 iaRTVTLDQATDNAKII 832
Cdd:PRK03348 303 --RSATLPYATDDAAVL 317
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
421-791 |
2.55e-48 |
|
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: 176.01 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 421 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangid 500
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNS------------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 501 svlSRAEIASCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDFH 580
Cdd:cd00424 33 ---DSTCVIACSYEARKY------------------------------------GVKRGMPVREARKMCPNLILVPARLD 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 581 AYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlAETKLTPDEFANAVRMEIKDQTK-CAASVGIGSNILLARMATRK 659
Cdd:cd00424 74 LYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS-ARLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKY 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 660 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPV 739
Cdd:cd00424 153 AKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPL 232
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034614580 740 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTL 791
Cdd:cd00424 233 SPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
419-810 |
7.17e-44 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 163.35 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqa 496
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGV-------------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 497 ngidsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVP 576
Cdd:PRK14133 41 -----------VSTCSYEAR------------------------------------KYGVHSAMPVFMAKKRCPHGIFLP 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 577 YDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlaetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMA 656
Cdd:PRK14133 74 VRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDITNI----KEEPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLA 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 657 TRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDD 736
Cdd:PRK14133 150 SDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGIDY 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034614580 737 RPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFGGH 810
Cdd:PRK14133 229 REVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKTVTVKI---------KTSDFQTH 293
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1193-1286 |
4.90e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 213388 Cd Length: 94 Bit Score: 148.96 E-value: 4.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 1193 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1272
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1034614580 1273 QVVLQQTYGSTLKV 1286
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
419-840 |
1.03e-41 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 158.65 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqanG 498
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVAGNEKERK-------------------------------------------G 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 499 IdsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYD 578
Cdd:PRK01810 44 I--------IVTCSYEAR------------------------------------AYGIRTTMPLWEAKRLCPQLIVRRPN 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 579 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:PRK01810 80 FDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDCYA--LGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 659 KAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRP 738
Cdd:PRK01810 158 MKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGIDDRP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 739 VRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKrlTLKIMVRkpgapveTAKFgghgicDNI 816
Cdd:PRK01810 237 VDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRLQKKTVVSY--NVQIMIR-------YHDR------RTI 301
|
410 420
....*....|....*....|....
gi 1034614580 817 ARTVTLDQATDNAKIIGKAMLNMF 840
Cdd:PRK01810 302 TRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
555-862 |
5.66e-40 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 153.62 E-value: 5.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 555 GIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILaetKL--TPDEFANAVRM 632
Cdd:PRK03103 54 GVKTAERLWEAQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGSQ---KLfgSPLEIAQKIQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 633 EIKDQTKCAASVGIGSNILLARMAT---RKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQY 709
Cdd:PRK03103 131 RIMRETGVYARVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIGQLAN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 710 MTMAKLQKEFGpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGK 787
Cdd:PRK03103 211 TPLERLKKRWG-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVLLELCEEVCRRARAKGYMGR 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034614580 788 rlTLKIMVRkpGAPVETAKfgghgicdNIARTVTLDQATDNAKIIGKAMLNMFHTMkLNISDMRGVGIHVNQLVP 862
Cdd:PRK03103 290 --TVSVSLR--GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGKPVRRVGVTLSNLVS 351
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-658 |
1.44e-38 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 140.79 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqangids 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 502 vlsRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHA 581
Cdd:pfam00817 31 ---RGIVAAASYEAR------------------------------------KYGVRSGMPVFEAKKLCPNLIVVPPDLEL 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034614580 582 YKEVAQTLYETLASY-THNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:pfam00817 72 YRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
560-837 |
4.80e-37 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 145.46 E-value: 4.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 560 MFfgHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDI--TEIL--AETKLTPDEFANAVRMEIK 635
Cdd:PRK02794 91 MF--KALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLVEPLSIDEAFLDLsgTERLhgAPPAVVLARFARRVEREIG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 636 dqtkCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKL 715
Cdd:PRK02794 169 ----ITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 716 QKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImv 795
Cdd:PRK02794 245 MRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKL-- 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034614580 796 rkpgapvETAKFGGHgicdniARTVTLDQATDNAKII---GKAML 837
Cdd:PRK02794 322 -------KTADFRLR------TRRRTLEDPTQLADRIfrtARELL 353
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
419-793 |
1.00e-34 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 136.69 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrGTGraplrpganpqlewqyyqnkilkgkaadipdsslwenpDSAQAng 498
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIVG---GNG--------------------------------------DPTEP-- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 499 idsvlsRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYD 578
Cdd:PRK03352 44 ------RKVVTCASYEAR------------------------------------AFGVRAGMPLRTAARRCPDAVFLPSD 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 579 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVditeiLAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:PRK03352 82 PAAYDAASEEVMATLRDLGVPVEVWGWDEAFL-----GVDTD-DPEALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 659 KAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRP 738
Cdd:PRK03352 156 FAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTE 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034614580 739 VRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 793
Cdd:PRK03352 236 VSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELARRVLDEVVAEGRPVTRVAVKV 291
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
419-827 |
1.98e-34 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 137.04 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsaqang 498
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIV----GGG--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 499 idSVLSraeiasCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYD 578
Cdd:PRK03858 37 --VVLA------ASYEAKAY------------------------------------GVRTAMGGRQARRLCPQAVVVPPR 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 579 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:PRK03858 73 MSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG-LRRISGTPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 659 KAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRP 738
Cdd:PRK03858 152 VAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAHGITTVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 739 VRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHGicdNIAR 818
Cdd:PRK03858 232 VETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGRTVVLRL------------RFDDFT---RATR 296
|
....*....
gi 1034614580 819 TVTLDQATD 827
Cdd:PRK03858 297 SHTLPRPTA 305
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
419-747 |
4.39e-28 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 117.20 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkaadipdsslwENPDSAQang 498
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSG-------------------------------------RFEDSGA--- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 499 idsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYD 578
Cdd:PRK01216 43 ---------VATANYEAR------------------------------------KLGIKAGMPIVEAKKILPNAVYLPMR 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 579 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 658
Cdd:PRK01216 78 KEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKNYQ-DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAAD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 659 KAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRP 738
Cdd:PRK01216 157 MAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEP 236
|
....*....
gi 1034614580 739 VRTeKERKS 747
Cdd:PRK01216 237 VRA-RVRKS 244
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
420-793 |
3.38e-26 |
|
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: 111.49 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgraplrpganpqlewqyyqnkilkgkaADIpdsslwenpdsaqangi 499
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSN------------------------------NDG----------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 500 dSVLSRaeiascSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCP--NLQAVPY 577
Cdd:cd01700 34 -CVIAR------SPEAK------------------------------------ALGIKMGSPYFKVPDLLErhGVAVFSS 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 578 DFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMAT 657
Cdd:cd01700 71 NYALYGDMSRRIMSILERFSPDVEVYSIDESFLDLTGSL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLAN 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 658 RKAK----PDGQYHLKPEEVDDFIRGQL-VTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCR 732
Cdd:cd01700 149 DLAKkknpYGGVVDLTDEEVRDKLLKILpVGDVWGIGRRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELN 227
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034614580 733 GLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 793
Cdd:cd01700 228 GIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
421-842 |
4.42e-25 |
|
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: 108.55 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkgkaadipdsslwenpdsAQANGID 500
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAV-----------------------------------------------VQWNSII 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 501 SVlsraeiascSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQ------- 573
Cdd:cd01702 35 AV---------SYAARAF------------------------------------GVTRFMTIDEAKKKCPDLIlahvaty 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 574 ---AVPYDFHA-------------YKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETkltpdefanaVRMEIKDQ 637
Cdd:cd01702 70 kkgEDEADYHEnpsparhkvsldpYRRASRKILNILKRFGDVVEKASIDEAYLDLGSRIVEE----------IRQQVYDE 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 638 TKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSM-ESKLASLGIKTCGDLQYM--TMAK 714
Cdd:cd01702 140 LGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGDVAGFrsSESD 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 715 LQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINY-GIRFTQPKEAEAFLLSLSEEIQRRLE----ATGMKGKRL 789
Cdd:cd01702 220 LQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpGKTALSTEDVQHWLLVLASELNSRLEddryENNRRPKTL 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034614580 790 TLKIMVRKPGAPVEtakfgghgICDNIARTVTLDQATDNAKIIGKAMLNMFHT 842
Cdd:cd01702 300 VLSLRQRGDGVRRS--------RSCALPRYDAQKIVKDAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
421-798 |
5.65e-22 |
|
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: 99.47 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyQNKILkgkaadipdsslwenpdsaqangid 500
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGI------------------------QQKYI------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 501 svlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVP-YDF 579
Cdd:cd01703 33 -------VVTCNYEAR------------------------------------RLGVKKLMSIKDAKEICPDLVLVNgEDL 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 580 HAYKEVAQTLYETLASYTHN--IEAVSCDEALVDITEIlaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMAT 657
Cdd:cd01703 70 TPFRDMSKKVYRLLRSYSWNdrVERLGFDENFMDVTEM---RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVG 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 658 RKAKPDGQYHLKPEEVDDFI--RGQL-VTNLPGVGHSMESKLASLGIKTCGDLQ---------------YMTMAKLQKEF 719
Cdd:cd01703 147 SVNKPNQQTTLLPPSCADLMdfMDLHdLRKIPGIGYKTAAKLEAHGISSVRDLQefsnrnrqtvgaapsLLELLLMVKEF 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 720 GPKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINYG-IRFTQPKEAEAFLLSLSEEIQRRL------EATGMKGKRLTL 791
Cdd:cd01703 227 GEGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSYKkCSLEEIREARNKIEELLASLLERMkqdlqeVKAGDGRRPHTL 306
|
....*..
gi 1034614580 792 KIMVRKP 798
Cdd:cd01703 307 RLTLRRY 313
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
553-792 |
6.75e-21 |
|
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: 95.53 E-value: 6.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 553 QLGIKNGMFFGHAKQLCPNLQAVPYD----FHAYKEVAQTLYEtlasYTHNIEAVSCDEALVDITeilAETKLTPDEFAN 628
Cdd:cd03468 45 AAGVRPGMPLAEALALCPNLQVVEYDpeadARALQELALWLLR----FTPLVALDGPDGLLLDVT---GCLHLFGGEDAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 629 AVRMEIKDQTKC-AASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDL 707
Cdd:cd03468 118 AASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLARLGLRTLGDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 708 QYMTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQRRLEATGMK 785
Cdd:cd03468 198 AALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLCAFLALRGLG 274
|
....*..
gi 1034614580 786 GKRLTLK 792
Cdd:cd03468 275 ARRLSLT 281
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
745-864 |
2.03e-20 |
|
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
Pssm-ID: 463354 [Multi-domain] Cd Length: 104 Bit Score: 87.61 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 745 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMvrkpgapveTAKFgghgicDNIARTVTLDQ 824
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034614580 825 ATDNAKIIGKAMLNMFHTMKLNIsDMRGVGIHVNQLVPTN 864
Cdd:pfam11799 66 PTDDTDEIYRAALRLLRRLYRGR-PVRLLGVSLSNLVPEG 104
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
555-793 |
5.50e-20 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 95.47 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 555 GIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILA--ETKLTPDEFANAVRM 632
Cdd:PTZ00205 179 GIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLDELTLEVSAYIErfEGTKTAEDVASELRV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 633 EIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLK---PEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--- 706
Cdd:PTZ00205 259 RVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDiyn 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 707 ----LQYMTMAKLQK-EFGPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSAEINYGIrFTQPKEAEAFLLSLSEEIQRR 778
Cdd:PTZ00205 339 rrveLCYILHNNLFRfLLGASIGIMQWpDAATAANTENCEgaTGGQRKAISSERSFTT-PRTKEGLQEMVDTVFNGAYEE 417
|
250
....*....|....*
gi 1034614580 779 LEATGMKGKRLTLKI 793
Cdd:PTZ00205 418 MRKSELMCRQISLTI 432
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1203-1284 |
5.42e-17 |
|
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein REV1. It interacts with REV7, POLN, POLK and POLI.
Pssm-ID: 465248 Cd Length: 91 Bit Score: 77.27 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 1203 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1273
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1034614580 1274 VVLQQTYGSTL 1284
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1041-1076 |
4.00e-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: 73.03 E-value: 4.00e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1034614580 1041 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1076
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
965-998 |
1.37e-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: 1.37e-12
10 20 30
....*....|....*....|....*....|....
gi 1034614580 965 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 998
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
45-129 |
5.20e-12 |
|
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.
Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 62.77 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 1034614580 125 SYIPY 129
Cdd:pfam16589 80 PLENY 84
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
46-118 |
7.79e-11 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 59.31 E-value: 7.79e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034614580 46 STIFSGVAIYVNGYTD-PSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK----GEKVIRPEWIVESI 118
Cdd:smart00292 1 PKLFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKaialGIPIVKEEWLLDCL 78
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
46-118 |
8.80e-11 |
|
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.
Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 58.84 E-value: 8.80e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034614580 46 STIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKELK-GEKVIRPEWIVESI 118
Cdd:pfam00533 3 EKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSK-KTTHVIVEARTKKYLKAKElGIPIVTEEWLLDCI 75
|
|
| BRCT_DNA_ligase_III |
cd18431 |
BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ... |
48-124 |
1.36e-10 |
|
BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ligase III, or polydeoxyribonucleotide synthase [ATP] 3, functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.
Pssm-ID: 349384 [Multi-domain] Cd Length: 78 Bit Score: 58.48 E-value: 1.36e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614580 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATnlpNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:cd18431 4 IFTGVKVYLPGSVEDDYKKLKRYFIAYDGDVVEEYDEEDATHVVVD---RDDKLGNPSAKVVSPEWLWDCIKKQKLV 77
|
|
| BRCT_DNA_ligase_IV_rpt1 |
cd17722 |
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ... |
48-132 |
8.76e-09 |
|
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the first one.
Pssm-ID: 349354 [Multi-domain] Cd Length: 90 Bit Score: 53.84 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 48 IFSGVAIYV-NGYTDP-SAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 1034614580 123 LLSYIPYQLY 132
Cdd:cd17722 80 LLPLEPKYMI 89
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
54-117 |
9.19e-08 |
|
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.
Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 50.05 E-value: 9.19e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614580 54 IYVNGYTDPSAEELRKLMMLHGGQYHVYYSRsKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVES 117
Cdd:cd00027 3 ICFSGLDDEEREELKKLIEALGGKVSESLSS-KVTHLIAKSPSGEKYYLAalaWGIPIVSPEWLLDC 68
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
48-121 |
3.80e-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: 48.69 E-value: 3.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614580 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17731 2 PFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKN-CTHLIAGSPSGQKYEfarKWNSIHIVTPEWLYDSIEAG 77
|
|
| BRCT_PAXIP1_rpt2 |
cd17710 |
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
48-125 |
9.03e-07 |
|
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.
Pssm-ID: 349342 [Multi-domain] Cd Length: 81 Bit Score: 48.00 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 48 IFSGVAIYVNGYtdpSAEELRKL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 1034614580 122 RLLS 125
Cdd:cd17710 77 TLLD 80
|
|
| BRCT_XRCC1_rpt1 |
cd17725 |
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ... |
51-129 |
2.43e-06 |
|
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one.
Pssm-ID: 349357 [Multi-domain] Cd Length: 80 Bit Score: 46.50 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 51 GVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSYIP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 1034614580 129 Y 129
Cdd:cd17725 80 Y 80
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
553-759 |
1.10e-05 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 49.38 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 553 QLGIKNGMFFGHAKQLCPNLQAVPY--DFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlaETKLTPDEFANAV 630
Cdd:PRK03609 46 ALGIKMGDPWFKQKDLFRRCGVVCFssNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGV--RNCRDLTDFGREI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 631 RMEIKDQTKCAASVGIGSNILLARMATRKAKP-DGQYH-----LKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTC 704
Cdd:PRK03609 124 RATVLQRTHLTVGVGIAQTKTLAKLANHAAKKwQRQTGgvvdlSNLERQRKLLSLQPVEEVWGVGRRISKKLNAMGIKTA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034614580 705 GDLQYMTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 759
Cdd:PRK03609 204 LDLADTNIRFIRKHF----NVVLERTVRELRGEPCLSLEEFAPTKQEIvcsrSFGERIT 258
|
|
| BRCT_TopBP1_rpt3 |
cd17718 |
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
44-122 |
1.41e-05 |
|
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain.
Pssm-ID: 349350 Cd Length: 83 Bit Score: 44.51 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 44 TSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 1034614580 120 AGR 122
Cdd:cd17718 81 QGK 83
|
|
| BRCT_PAXIP1_rpt1 |
cd17714 |
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; ... |
49-125 |
3.27e-05 |
|
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the first BRCT domain.
Pssm-ID: 349346 Cd Length: 76 Bit Score: 43.46 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 49 FSGVAIYVNGYTDPSAEELRKlmmlHGGQYHVYYSRSKTTHIIATNLPNAKIKELK--GEK-VIRPEWIVESIKAGRLLS 125
Cdd:cd17714 1 FKDVKYFVVGNLDEKVEQLLK----NGGAKEVSYLSDMATHVIVDDNDNPEVGEARdlFELpVVTSSWVILSIKAGKLLP 76
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
54-113 |
9.48e-04 |
|
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.
Pssm-ID: 463687 [Multi-domain] Cd Length: 63 Bit Score: 38.72 E-value: 9.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614580 54 IYVNGYTDPSAEELRKLMMLHGGQYHVYYSRsKTTHIIAtnlpnakiKELKGEK----------VIRPEW 113
Cdd:pfam12738 3 ICVTGFDGDDREGLQKLIEAMGAEYTKDLTK-SVTHLIC--------KSGEGEKyekakewgipVVSPLW 63
|
|
| BRCT_Rad4_rpt2 |
cd17746 |
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ... |
62-131 |
2.58e-03 |
|
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one.
Pssm-ID: 349377 [Multi-domain] Cd Length: 91 Bit Score: 38.37 E-value: 2.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034614580 62 PSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIK-ELK-GEKVIRPEWIVESIKAGRLLSYIPYQL 131
Cdd:cd17746 20 PERSRIENYVLKHGGTFCPDLTRD-VTHLIAGTSSGRKYEyALKwKINVVCVEWLWQSIQRNAVLEPQYFQL 90
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
1047-1078 |
2.69e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 36.71 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|..
gi 1034614580 1047 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1078
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| IMS_HHH |
pfam11798 |
IMS family HHH motif; These proteins are involved in UV protection, eg. |
670-701 |
2.78e-03 |
|
IMS family HHH motif; These proteins are involved in UV protection, eg.
Pssm-ID: 432081 [Multi-domain] Cd Length: 32 Bit Score: 36.61 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|..
gi 1034614580 670 PEEVDDFIRGQLVTNLPGVGHSMESKLASLGI 701
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
969-990 |
6.51e-03 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 35.56 E-value: 6.51e-03
|
| |
