|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
348-859 |
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: 622.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsvlsRAEI 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP---------------------------------------------------NSEI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 508 ASCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQT 587
Cdd:cd01701 87 ASCNYEARSY------------------------------------GIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLT 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 588 LYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHL 667
Cdd:cd01701 131 FYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 668 KPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERK 745
Cdd:cd01701 211 SAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 746 SVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQAT 825
Cdd:cd01701 291 SVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVAT 370
|
490 500 510
....*....|....*....|....*....|....
gi 1034614582 826 DNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 859
Cdd:cd01701 371 DDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-856 |
6.71e-84 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 277.41 E-value: 6.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangi 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 499 dsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDF 578
Cdd:COG0389 39 --------VAAASYEAR------------------------------------AFGVRSGMPLFQARRLCPDLVVLPPDF 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 579 HAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 658
Cdd:COG0389 75 ELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 659 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV 738
Cdd:COG0389 154 AKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 739 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIART 818
Cdd:COG0389 233 EPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVKL---------RTSDF------RTTTRS 297
|
410 420 430
....*....|....*....|....*....|....*...
gi 1034614582 819 VTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHV 856
Cdd:COG0389 298 RTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-792 |
4.43e-66 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 227.31 E-value: 4.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpGanpqlewqyyqnkilkGKADipdsslwenpdsaqangidsvlS 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV-------------G----------------GSPG----------------------R 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 504 RAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKE 583
Cdd:PRK02406 30 RGVISTCNYEAR------------------------------------KFGVRSAMPTAQALKLCPDLIFVPGRFDVYKE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 584 VAQTLYETLASYTHNIEAVSCDEALVDITE----ILAETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRKA 659
Cdd:PRK02406 74 VSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIGSATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDWN 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 660 KPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVR 739
Cdd:PRK02406 149 KPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVK 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034614582 740 TEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGM--KGKRLTLKI 792
Cdd:PRK02406 228 PDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 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 1034614582 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1034614582 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 ... |
1192-1285 |
4.89e-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: 4.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 1192 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1271
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1034614582 1272 QVVLQQTYGSTLKV 1285
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-657 |
1.05e-38 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 141.17 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsv 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 502 lsRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHAY 581
Cdd:pfam00817 31 --RGIVAAASYEAR------------------------------------KYGVRSGMPVFEAKKLCPNLIVVPPDLELY 72
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614582 582 KEVAQTLYETLASY-THNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 657
Cdd:pfam00817 73 RRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
1202-1283 |
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 1034614582 1202 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1272
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1034614582 1273 VVLQQTYGSTL 1283
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1040-1075 |
3.96e-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: 3.96e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1034614582 1040 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1075
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
964-997 |
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 1034614582 964 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 997
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 1034614582 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 1034614582 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 1034614582 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 ... |
1046-1077 |
2.68e-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: 2.68e-03
10 20 30
....*....|....*....|....*....|..
gi 1034614582 1046 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1077
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
968-989 |
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. ... |
348-859 |
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: 622.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 348 FISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPgreklkkmktgrsalvvtdtgdmSVLNSPRHQSCIMHVDMDCF 427
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------------------SNSIHPDLQRIIMHVDFDCF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 428 FVSVGIRNRPDLKGKPVAVTSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsvlsRAEI 507
Cdd:cd01701 58 FVSVSIRNRPDLKGKPVAVCHGKGP---------------------------------------------------NSEI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 508 ASCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQT 587
Cdd:cd01701 87 ASCNYEARSY------------------------------------GIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLT 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 588 LYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHL 667
Cdd:cd01701 131 FYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 668 KPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERK 745
Cdd:cd01701 211 SAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 746 SVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQAT 825
Cdd:cd01701 291 SVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVAT 370
|
490 500 510
....*....|....*....|....*....|....
gi 1034614582 826 DNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 859
Cdd:cd01701 371 DDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
420-859 |
2.03e-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: 281.72 E-value: 2.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtGRAPLRpganpqlewqyyqnkilkgkadipdsslwenpdsaqanGId 499
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAV------GGSSDR--------------------------------------GV- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 500 svlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFH 579
Cdd:cd03586 36 -------VSTASYEAR------------------------------------KFGVRSAMPIFQAKKLCPNLIFVPPRFD 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 580 AYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKA 659
Cdd:cd03586 73 KYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYVRLFG-SATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLN 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 660 KPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVR 739
Cdd:cd03586 152 KPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 740 TEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHgicDNIARTV 819
Cdd:cd03586 231 PDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVKL------------KYADF---STRTRSR 295
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1034614582 820 TLDQATDNAKIIGKAMLNMFHTMKLNISdMRGVGIHVNQL 859
Cdd:cd03586 296 TLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVRLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
419-856 |
6.71e-84 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 277.41 E-value: 6.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangi 498
Cdd:COG0389 3 ILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 499 dsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDF 578
Cdd:COG0389 39 --------VAAASYEAR------------------------------------AFGVRSGMPLFQARRLCPDLVVLPPDF 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 579 HAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 658
Cdd:COG0389 75 ELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 659 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV 738
Cdd:COG0389 154 AKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 739 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFgghgicDNIART 818
Cdd:COG0389 233 EPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVKL---------RTSDF------RTTTRS 297
|
410 420 430
....*....|....*....|....*....|....*...
gi 1034614582 819 VTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHV 856
Cdd:COG0389 298 RTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
424-792 |
4.43e-66 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 227.31 E-value: 4.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 424 MDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpGanpqlewqyyqnkilkGKADipdsslwenpdsaqangidsvlS 503
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVAV-------------G----------------GSPG----------------------R 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 504 RAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKE 583
Cdd:PRK02406 30 RGVISTCNYEAR------------------------------------KFGVRSAMPTAQALKLCPDLIFVPGRFDVYKE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 584 VAQTLYETLASYTHNIEAVSCDEALVDITE----ILAETKLtpdefANAVRMEIKDQTKCAASVGIGSNILLARMATRKA 659
Cdd:PRK02406 74 VSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIGSATLI-----AQEIRQDIFEELGLTASAGVAPNKFLAKIASDWN 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 660 KPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPVR 739
Cdd:PRK02406 149 KPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVK 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034614582 740 TEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGM--KGKRLTLKI 792
Cdd:PRK02406 228 PDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 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 1034614582 48 IFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELK---GEKVIRPEWIVESIKAGRLL 124
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKkarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 1034614582 125 SYIPYQL 131
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
419-831 |
6.42e-49 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 181.29 E-value: 6.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqan 496
Cdd:PRK03348 7 VLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 497 gidsvlsraeIASCSYEARSLkvlepwllprvmsyhvqccwhlnhcGATSGawnwqlgikngMFFGHAKQLCPNLQAV-P 575
Cdd:PRK03348 43 ----------VAGASYEARVF-------------------------GARSA-----------MPMHQARRLVGNGAVVlP 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 576 YDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMA 655
Cdd:PRK03348 77 PRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEPAELAGASAEEVEAFAERLRARVREETGLPASVGAGSGKQIAKIA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 656 TRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDD 735
Cdd:PRK03348 157 SGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDD 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 736 RPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKimVRKPGAPVETakfgghgicdni 815
Cdd:PRK03348 237 RPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRGARTVTVK--LRKSDFSTLT------------ 302
|
410
....*....|....*.
gi 1034614582 816 aRTVTLDQATDNAKII 831
Cdd:PRK03348 303 -RSATLPYATDDAAVL 317
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
421-790 |
1.87e-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: 176.40 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 421 HVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangids 500
Cdd:cd00424 2 HIDFDNFFASVEQLARPELKGRPVVVVPFNS------------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 501 vlSRAEIASCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDFHA 580
Cdd:cd00424 33 --DSTCVIACSYEARKY------------------------------------GVKRGMPVREARKMCPNLILVPARLDL 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 581 YKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlAETKLTPDEFANAVRMEIKDQTK-CAASVGIGSNILLARMATRKA 659
Cdd:cd00424 75 YRRLSERLLSELEEVAPLVEVASIDELFLDLTGS-ARLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKYA 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 660 KPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVR 739
Cdd:cd00424 154 KPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLS 233
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034614582 740 TEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTL 790
Cdd:cd00424 234 PPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRLRRDGRGATRLRL 284
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
419-809 |
5.28e-44 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 163.73 E-value: 5.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAV--TSNRGTgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqan 496
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIVggISERGV-------------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 497 gidsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPY 576
Cdd:PRK14133 41 ----------VSTCSYEAR------------------------------------KYGVHSAMPVFMAKKRCPHGIFLPV 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 577 DFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlaetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMAT 656
Cdd:PRK14133 75 RHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDITNI----KEEPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLAS 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 657 RKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDR 736
Cdd:PRK14133 151 DWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNIGIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGIDYR 229
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034614582 737 PVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvETAKFGGH 809
Cdd:PRK14133 230 EVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKTVTVKI---------KTSDFQTH 293
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
1192-1285 |
4.89e-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: 4.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 1192 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 1271
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1034614582 1272 QVVLQQTYGSTLKV 1285
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
419-839 |
7.60e-42 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 159.04 E-value: 7.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRaplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqanGI 498
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVAGNEKERK------------------------------------------GI 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 499 dsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDF 578
Cdd:PRK01810 45 --------IVTCSYEAR------------------------------------AYGIRTTMPLWEAKRLCPQLIVRRPNF 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 579 HAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAetKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 658
Cdd:PRK01810 81 DRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDCYA--LGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDM 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 659 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRGLDDRPV 738
Cdd:PRK01810 159 KKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGIDDRPV 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 739 RTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKrlTLKIMVRkpgapveTAKFgghgicDNIA 816
Cdd:PRK01810 238 DPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRLQKKTVVSY--NVQIMIR-------YHDR------RTIT 302
|
410 420
....*....|....*....|...
gi 1034614582 817 RTVTLDQATDNAKIIGKAMLNMF 839
Cdd:PRK01810 303 RSKTLKNPIWEKRDIFQAASRLF 325
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
554-861 |
5.65e-40 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 153.62 E-value: 5.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 554 GIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILaetKL--TPDEFANAVRM 631
Cdd:PRK03103 54 GVKTAERLWEAQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGSQ---KLfgSPLEIAQKIQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 632 EIKDQTKCAASVGIGSNILLARMAT---RKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQY 708
Cdd:PRK03103 131 RIMRETGVYARVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIGQLAN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 709 MTMAKLQKEFGpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGK 786
Cdd:PRK03103 211 TPLERLKKRWG-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVLLELCEEVCRRARAKGYMGR 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034614582 787 rlTLKIMVRkpGAPVETAKfgghgicdNIARTVTLDQATDNAKIIGKAMLNMFHTMkLNISDMRGVGIHVNQLVP 861
Cdd:PRK03103 290 --TVSVSLR--GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGKPVRRVGVTLSNLVS 351
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
422-657 |
1.05e-38 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 141.17 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 422 VDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangidsv 501
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNG-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 502 lsRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDFHAY 581
Cdd:pfam00817 31 --RGIVAAASYEAR------------------------------------KYGVRSGMPVFEAKKLCPNLIVVPPDLELY 72
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614582 582 KEVAQTLYETLASY-THNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 657
Cdd:pfam00817 73 RRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
559-836 |
4.79e-37 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 145.46 E-value: 4.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 559 MFfgHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDI--TEIL--AETKLTPDEFANAVRMEIK 634
Cdd:PRK02794 91 MF--KALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLVEPLSIDEAFLDLsgTERLhgAPPAVVLARFARRVEREIG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 635 dqtkCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKL 714
Cdd:PRK02794 169 ----ITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 715 QKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImv 794
Cdd:PRK02794 245 MRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKL-- 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034614582 795 rkpgapvETAKFGGHgicdniARTVTLDQATDNAKII---GKAML 836
Cdd:PRK02794 322 -------KTADFRLR------TRRRTLEDPTQLADRIfrtARELL 353
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
419-792 |
7.40e-35 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 137.08 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTsnrGTGraplrpganpqlewqyyqnkilkgkadipdsslwenpDSAQAngi 498
Cdd:PRK03352 7 VLHVDLDQFIAAVELLRRPELAGLPVIVG---GNG-------------------------------------DPTEP--- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 499 dsvlsRAEIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDF 578
Cdd:PRK03352 44 -----RKVVTCASYEAR------------------------------------AFGVRAGMPLRTAARRCPDAVFLPSDP 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 579 HAYKEVAQTLYETLASYTHNIEAVSCDEALVditeiLAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 658
Cdd:PRK03352 83 AAYDAASEEVMATLRDLGVPVEVWGWDEAFL-----GVDTD-DPEALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATGF 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 659 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPV 738
Cdd:PRK03352 157 AKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEV 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034614582 739 RTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 792
Cdd:PRK03352 237 SAEPwVPRSRSREVTFPQDLTDRAEVESAVRELARRVLDEVVAEGRPVTRVAVKV 291
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
419-826 |
1.47e-34 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 137.43 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVtsnrGTGraplrpganpqlewqyyqnkilkgkadipdsslwenpdsaqangi 498
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIV----GGG--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 499 dSVLSraeiasCSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQAVPYDF 578
Cdd:PRK03858 37 -VVLA------ASYEAKAY------------------------------------GVRTAMGGRQARRLCPQAVVVPPRM 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 579 HAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 658
Cdd:PRK03858 74 SAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG-LRRISGTPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 659 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPV 738
Cdd:PRK03858 153 AKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAHGITTVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRRV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 739 RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvetaKFGGHGicdNIART 818
Cdd:PRK03858 233 ETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGRTVVLRL------------RFDDFT---RATRS 297
|
....*...
gi 1034614582 819 VTLDQATD 826
Cdd:PRK03858 298 HTLPRPTA 305
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
419-746 |
3.25e-28 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 117.58 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 419 IMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGtgraplrpganpqlewqyyqnkilkgkadipdsslwENPDSAQangi 498
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSG------------------------------------RFEDSGA---- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 499 dsvlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVPYDF 578
Cdd:PRK01216 43 --------VATANYEAR------------------------------------KLGIKAGMPIVEAKKILPNAVYLPMRK 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 579 HAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRK 658
Cdd:PRK01216 79 EVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKNYQ-DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADM 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 659 AKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPV 738
Cdd:PRK01216 158 AKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPV 237
|
....*...
gi 1034614582 739 RTeKERKS 746
Cdd:PRK01216 238 RA-RVRKS 244
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
420-792 |
2.50e-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: 111.87 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 420 MHVDMDCFFVSVGIRNRPDLKGKPVAVTSNrgtgraplrpganpqlewqyyqnkilkgkADIpdsslwenpdsaqangid 499
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSN-----------------------------NDG------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 500 SVLSRaeiascSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCP--NLQAVPYD 577
Cdd:cd01700 34 CVIAR------SPEAK------------------------------------ALGIKMGSPYFKVPDLLErhGVAVFSSN 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 578 FHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 657
Cdd:cd01700 72 YALYGDMSRRIMSILERFSPDVEVYSIDESFLDLTGSL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLAND 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 658 KAK----PDGQYHLKPEEVDDFIRGQL-VTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTGQMLYRFCRG 732
Cdd:cd01700 150 LAKkknpYGGVVDLTDEEVRDKLLKILpVGDVWGIGRRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELNG 228
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034614582 733 LDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 792
Cdd:cd01700 229 IDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
421-841 |
3.28e-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: 108.94 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyqnkilkgkadipdsslwenpdsAQANGIDS 500
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAV----------------------------------------------VQWNSIIA 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 501 VlsraeiascSYEARSLkvlepwllprvmsyhvqccwhlnhcgatsgawnwqlGIKNGMFFGHAKQLCPNLQ-------- 572
Cdd:cd01702 36 V---------SYAARAF------------------------------------GVTRFMTIDEAKKKCPDLIlahvatyk 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 573 --AVPYDFHA-------------YKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETkltpdefanaVRMEIKDQT 637
Cdd:cd01702 71 kgEDEADYHEnpsparhkvsldpYRRASRKILNILKRFGDVVEKASIDEAYLDLGSRIVEE----------IRQQVYDEL 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 638 KCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSM-ESKLASLGIKTCGDLQYM--TMAKL 714
Cdd:cd01702 141 GYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLgEEIIDLLGLPTEGDVAGFrsSESDL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 715 QKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINY-GIRFTQPKEAEAFLLSLSEEIQRRLE----ATGMKGKRLT 789
Cdd:cd01702 221 QEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpGKTALSTEDVQHWLLVLASELNSRLEddryENNRRPKTLV 300
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034614582 790 LKIMVRKPGAPVEtakfgghgICDNIARTVTLDQATDNAKIIGKAMLNMFHT 841
Cdd:cd01702 301 LSLRQRGDGVRRS--------RSCALPRYDAQKIVKDAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
421-797 |
4.20e-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: 99.85 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 421 HVDMDCFFVSVGIRNRPDLKGKPVAVtsnrgtgraplrpganpqlewqyyQNKILkgkadipdsslwenpdsaqangids 500
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGI------------------------QQKYI------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 501 vlsraeIASCSYEARslkvlepwllprvmsyhvqccwhlnhcgatsgawnwQLGIKNGMFFGHAKQLCPNLQAVP-YDFH 579
Cdd:cd01703 33 ------VVTCNYEAR------------------------------------RLGVKKLMSIKDAKEICPDLVLVNgEDLT 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 580 AYKEVAQTLYETLASYTHN--IEAVSCDEALVDITEIlaeTKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATR 657
Cdd:cd01703 71 PFRDMSKKVYRLLRSYSWNdrVERLGFDENFMDVTEM---RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGS 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 658 KAKPDGQYHLKPEEVDDFI--RGQL-VTNLPGVGHSMESKLASLGIKTCGDLQ---------------YMTMAKLQKEFG 719
Cdd:cd01703 148 VNKPNQQTTLLPPSCADLMdfMDLHdLRKIPGIGYKTAAKLEAHGISSVRDLQefsnrnrqtvgaapsLLELLLMVKEFG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 720 PKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINYG-IRFTQPKEAEAFLLSLSEEIQRRL------EATGMKGKRLTLK 791
Cdd:cd01703 228 EGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSYKkCSLEEIREARNKIEELLASLLERMkqdlqeVKAGDGRRPHTLR 307
|
....*.
gi 1034614582 792 IMVRKP 797
Cdd:cd01703 308 LTLRRY 313
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
552-791 |
6.74e-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: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 552 QLGIKNGMFFGHAKQLCPNLQAVPYD----FHAYKEVAQTLYEtlasYTHNIEAVSCDEALVDITeilAETKLTPDEFAN 627
Cdd:cd03468 45 AAGVRPGMPLAEALALCPNLQVVEYDpeadARALQELALWLLR----FTPLVALDGPDGLLLDVT---GCLHLFGGEDAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 628 AVRMEIKDQTKC-AASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDL 706
Cdd:cd03468 118 AASLRAALATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLARLGLRTLGDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 707 QYMTMAKLQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQRRLEATGMK 784
Cdd:cd03468 198 AALPRAELARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLCAFLALRGLG 274
|
....*..
gi 1034614582 785 GKRLTLK 791
Cdd:cd03468 275 ARRLSLT 281
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
744-863 |
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 1034614582 744 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMvrkpgapveTAKFgghgicDNIARTVTLDQ 823
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034614582 824 ATDNAKIIGKAMLNMFHTMKLNIsDMRGVGIHVNQLVPTN 863
Cdd:pfam11799 66 PTDDTDEIYRAALRLLRRLYRGR-PVRLLGVSLSNLVPEG 104
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
554-792 |
5.49e-20 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 95.47 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 554 GIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILA--ETKLTPDEFANAVRM 631
Cdd:PTZ00205 179 GIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLDELTLEVSAYIErfEGTKTAEDVASELRV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 632 EIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLK---PEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--- 705
Cdd:PTZ00205 259 RVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDiyn 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 706 ----LQYMTMAKLQK-EFGPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSAEINYGIrFTQPKEAEAFLLSLSEEIQRR 777
Cdd:PTZ00205 339 rrveLCYILHNNLFRfLLGASIGIMQWpDAATAANTENCEgaTGGQRKAISSERSFTT-PRTKEGLQEMVDTVFNGAYEE 417
|
250
....*....|....*
gi 1034614582 778 LEATGMKGKRLTLKI 792
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 ... |
1202-1283 |
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 1034614582 1202 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 1272
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1034614582 1273 VVLQQTYGSTL 1283
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
1040-1075 |
3.96e-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: 3.96e-16
10 20 30
....*....|....*....|....*....|....*.
gi 1034614582 1040 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 1075
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
964-997 |
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 1034614582 964 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 997
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 1034614582 45 SSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLL 124
Cdd:pfam16589 1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWIFDCVKKGKLL 79
|
....*
gi 1034614582 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 1034614582 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 |
8.79e-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: 8.79e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034614582 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 1034614582 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 |
8.84e-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: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 48 IFSGVAIYV-NGYTDP-SAEELRKLMMLHGGQYhVYYSRSKTTHIIATNLPNAKIKEL---KGEKVIRPEWIVESIKAGR 122
Cdd:cd17722 1 IFEGVEFCVmSDMSSPkSKAELEKLIKENGGKV-VQNPGAPDTICVIAGREVVKVKNLiksGGHDVVKPSWLLDCIARKE 79
|
90
....*....|
gi 1034614582 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 |
9.18e-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: 9.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614582 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 |
3.91e-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: 3.91e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034614582 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 |
9.02e-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: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 48 IFSGVAIYVNGYtdpSAEELRKL--MM-LHGGQYHVYYSrSKTTHIIATNLPNAKIK---ELKGEKVIRPEWIVESIKAG 121
Cdd:cd17710 1 LFSGVVVCPSQI---SAEDRLKLwaMVtFHGGKCQLNLD-KKCTHLVTGKASGAKYEcalKHEGIKIVTPDWVTDCIKAK 76
|
....
gi 1034614582 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 1034614582 51 GVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK--VIRPEWIVESIKAGRLLSYIP 128
Cdd:cd17725 1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTAD-CTHLICAFANTPKYKQVKGAGgiIVSKEWILDCYKKKKRLPWKR 79
|
.
gi 1034614582 129 Y 129
Cdd:cd17725 80 Y 80
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
552-758 |
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 1034614582 552 QLGIKNGMFFGHAKQLCPNLQAVPY--DFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlaETKLTPDEFANAV 629
Cdd:PRK03609 46 ALGIKMGDPWFKQKDLFRRCGVVCFssNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGV--RNCRDLTDFGREI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 630 RMEIKDQTKCAASVGIGSNILLARMATRKAKP-DGQYH-----LKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTC 703
Cdd:PRK03609 124 RATVLQRTHLTVGVGIAQTKTLAKLANHAAKKwQRQTGgvvdlSNLERQRKLLSLQPVEEVWGVGRRISKKLNAMGIKTA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034614582 704 GDLQYMTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTEKERKSVSAEI----NYGIRFT 758
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 1034614582 44 TSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSkTTHIIATNLPNAKIKELKGEK----VIRPEWIVESIK 119
Cdd:cd17718 2 KAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNES-VTHVVVGESSEELLKELAKLAgrphVVTPSWLLECFK 80
|
...
gi 1034614582 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 |
3.26e-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: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614582 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 1034614582 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 1034614582 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 ... |
1046-1077 |
2.68e-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: 2.68e-03
10 20 30
....*....|....*....|....*....|..
gi 1034614582 1046 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 1077
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| IMS_HHH |
pfam11798 |
IMS family HHH motif; These proteins are involved in UV protection, eg. |
669-700 |
2.77e-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: 2.77e-03
10 20 30
....*....|....*....|....*....|..
gi 1034614582 669 PEEVDDFIRGQLVTNLPGVGHSMESKLASLGI 700
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
968-989 |
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
|
| |
