|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
1-366 |
2.61e-140 |
|
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: 413.25 E-value: 2.61e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 1 MWADDAKKLCPDLLLAQVR----------------ESRGKANLTKYREASVEVMEIMSRF-AVIERASIDEAYVDLtsav 63
Cdd:cd01702 49 MTIDEAKKKCPDLILAHVAtykkgedeadyhenpsPARHKVSLDPYRRASRKILNILKRFgDVVEKASIDEAYLDL---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 64 qerlqklqgqpisadllpstyieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvGAVIVEEMRAAIE 143
Cdd:cd01702 125 -------------------------------------------------------------------GSRIVEEIRQQVY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 144 RETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQF--TE 221
Cdd:cd01702 138 DELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDLLGLPTEGDVAGFrsSE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 222 SQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATrEQVQWWLLQLAQELEERLTKDRNDNDRVA 301
Cdd:cd01702 218 SDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFPGKTALST-EDVQHWLLVLASELNSRLEDDRYENNRRP 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382162 302 TQLVVSIRVQGDKrlSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCATK 366
Cdd:cd01702 297 KTLVLSLRQRGDG--VRRSRSCALPRYDAQKIVKDAFKLIKAINEEGLGLAWNYPLTLLSLSFTK 359
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
5-309 |
1.14e-51 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 181.50 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 5 DAKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA-VIERASIDEAYVDLTSAvqerlQKLQGQPisadllpst 83
Cdd:COG0389 59 QARRLCPDLVVL-------PPDFELYRDVSRRVMAILERYTpLVEPLSIDEAFLDVTGS-----ARLFGSA--------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 84 yieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvgAVIVEEMRAAIERETGFQCSAGISHNKVLAKL 163
Cdd:COG0389 118 ------------------------------------------------EAIARRIRRRIRRETGLTVSVGIAPNKFLAKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 164 ACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLgASVIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGI 243
Cdd:COG0389 150 ASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKT-AEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382162 244 EHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKDRndndRVATQLVVSIR 309
Cdd:COG0389 228 DPRPVEPRRPRKSIGVERTFG--EDLTDLEELEAALRRLAERLAERLRRQG----LGARTVTVKLR 287
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
6-309 |
4.73e-41 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 152.58 E-value: 4.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAQVResrgkanLTKYREASVEVMEIMSRF-AVIERASIDEAYVDLTSAVQerlqklqgqpisadllpsty 84
Cdd:PRK02406 54 ALKLCPDLIFVPGR-------FDVYKEVSRQIREIFRRYtDLIEPLSLDEAYLDVTDNKL-------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglPQGPTTAeetvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK02406 107 ----CIGSATL--------------------------------------IAQEIRQDIFEELGLTASAGVAPNKFLAKIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRslG-GKLGASVIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGI 243
Cdd:PRK02406 145 SDWNKPNGLFVITPEEVDAFLATLPVEKIP--GvGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGI 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382162 244 EHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTkdRNDNDRVATQLVVSIR 309
Cdd:PRK02406 222 DERPVKPDRERKSVGVERTFA--EDLYDLEACLAELPRLAEKLERRLE--RAKPDKRIKTVGVKLK 283
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
1-165 |
7.93e-20 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 86.47 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 1 MWADDAKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA--VIERASIDEAYVDLTSavqerLQKLQGQPISad 78
Cdd:pfam00817 50 MPVFEAKKLCPNLIVV-------PPDLELYRRASRKIFEILRRFStpKVEQASIDEAFLDLTG-----LEKLFGAEEA-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 79 llpstyieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNK 158
Cdd:pfam00817 116 -------------------------------------------------------LAKRLRREIAEETGLTCSIGIAPNK 140
|
....*..
gi 530382162 159 VLAKLAC 165
Cdd:pfam00817 141 LLAKLAS 147
|
|
| zf_UBZ |
pfam18439 |
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA ... |
569-599 |
1.56e-11 |
|
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA polymerase eta (EC:2.7.7.7). It is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. The UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a beta-beta-alpha fold.
Pssm-ID: 465769 Cd Length: 32 Bit Score: 59.06 E-value: 1.56e-11
10 20 30
....*....|....*....|....*....|.
gi 530382162 569 DQVPCEKCGSLVPVWDMPEHMDYHFALELQK 599
Cdd:pfam18439 1 DTYVCPRCGKEIPESELPEHEDWHFAKDLQR 31
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
1-366 |
2.61e-140 |
|
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: 413.25 E-value: 2.61e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 1 MWADDAKKLCPDLLLAQVR----------------ESRGKANLTKYREASVEVMEIMSRF-AVIERASIDEAYVDLtsav 63
Cdd:cd01702 49 MTIDEAKKKCPDLILAHVAtykkgedeadyhenpsPARHKVSLDPYRRASRKILNILKRFgDVVEKASIDEAYLDL---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 64 qerlqklqgqpisadllpstyieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvGAVIVEEMRAAIE 143
Cdd:cd01702 125 -------------------------------------------------------------------GSRIVEEIRQQVY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 144 RETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQF--TE 221
Cdd:cd01702 138 DELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDLLGLPTEGDVAGFrsSE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 222 SQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATrEQVQWWLLQLAQELEERLTKDRNDNDRVA 301
Cdd:cd01702 218 SDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFPGKTALST-EDVQHWLLVLASELNSRLEDDRYENNRRP 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382162 302 TQLVVSIRVQGDKrlSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCATK 366
Cdd:cd01702 297 KTLVLSLRQRGDG--VRRSRSCALPRYDAQKIVKDAFKLIKAINEEGLGLAWNYPLTLLSLSFTK 359
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
5-309 |
1.14e-51 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 181.50 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 5 DAKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA-VIERASIDEAYVDLTSAvqerlQKLQGQPisadllpst 83
Cdd:COG0389 59 QARRLCPDLVVL-------PPDFELYRDVSRRVMAILERYTpLVEPLSIDEAFLDVTGS-----ARLFGSA--------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 84 yieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvgAVIVEEMRAAIERETGFQCSAGISHNKVLAKL 163
Cdd:COG0389 118 ------------------------------------------------EAIARRIRRRIRRETGLTVSVGIAPNKFLAKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 164 ACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLgASVIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGI 243
Cdd:COG0389 150 ASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKT-AEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382162 244 EHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKDRndndRVATQLVVSIR 309
Cdd:COG0389 228 DPRPVEPRRPRKSIGVERTFG--EDLTDLEELEAALRRLAERLAERLRRQG----LGARTVTVKLR 287
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
6-309 |
1.45e-49 |
|
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: 175.79 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA-VIERASIDEAYVDLTsavqerlqklqgqpisadllpsty 84
Cdd:cd03586 57 AKKLCPNLIFV-------PPRFDKYREVSRQIMEILREYTpLVEPLSIDEAYLDVT------------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieGLPQGPTTAEEtvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:cd03586 106 --DYVRLFGSATE------------------------------------IAKEIRARIREETGLTASAGIAPNKFLAKIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEiLGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGIE 244
Cdd:cd03586 148 SDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKE-LGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGID 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382162 245 HDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKDrndnDRVATQLVVSIR 309
Cdd:cd03586 226 NRPVEPDRERKSIGVERTFS--EDLTDPEELLEELLELAEELAERLRKR----GLKGRTVTVKLK 284
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
6-309 |
4.73e-41 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 152.58 E-value: 4.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAQVResrgkanLTKYREASVEVMEIMSRF-AVIERASIDEAYVDLTSAVQerlqklqgqpisadllpsty 84
Cdd:PRK02406 54 ALKLCPDLIFVPGR-------FDVYKEVSRQIREIFRRYtDLIEPLSLDEAYLDVTDNKL-------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglPQGPTTAeetvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK02406 107 ----CIGSATL--------------------------------------IAQEIRQDIFEELGLTASAGVAPNKFLAKIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRslG-GKLGASVIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGI 243
Cdd:PRK02406 145 SDWNKPNGLFVITPEEVDAFLATLPVEKIP--GvGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGI 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530382162 244 EHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTkdRNDNDRVATQLVVSIR 309
Cdd:PRK02406 222 DERPVKPDRERKSVGVERTFA--EDLYDLEACLAELPRLAEKLERRLE--RAKPDKRIKTVGVKLK 283
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
1-342 |
8.82e-32 |
|
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: 126.32 E-value: 8.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 1 MWADDAKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA-VIERASIDEAYVDLTSAVQerlqklqgqpisadl 79
Cdd:cd00424 53 MPVREARKMCPNLILV-------PARLDLYRRLSERLLSELEEVApLVEVASIDELFLDLTGSAR--------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 80 lpstyieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlQLTVGAVIVEEMRAAI-ERETGFQCSAGISHNK 158
Cdd:cd00424 111 -----------------------------------------------LLGLGSEVALRIKRHIaEQLGGITASIGIASNK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 159 VLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLgASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYA 238
Cdd:cd00424 144 LLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVT-AKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 239 MCRGIEHDPVKPRQLPKTIGCSKNFPGKtaLATREQVQWWLLQLAQELEERLTKDrndnDRVATQLVVSIR-VQGDKRLS 317
Cdd:cd00424 223 ALRGIDDEPLSPPRPRKSFSHERVLPRD--SRNAEDARPLLRLLLEKLARRLRRD----GRGATRLRLWLRtVDGRWSGH 296
|
330 340
....*....|....*....|....*
gi 530382162 318 SLRRCCALTRYdAHKMSHDAFTVIK 342
Cdd:cd00424 297 ADIPSRSAPRP-ISTEDGELLHALD 320
|
|
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
1-310 |
2.39e-27 |
|
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: 114.72 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 1 MWADDAKKLCPDLLLAQVresrgkaNLTKYREASVEVMEI-MSRFAVIERASIDEAYVDLTSAVQERlqklqgqpisadl 79
Cdd:cd01701 102 MWVGQAKKLCPQLVTLPY-------DFEAYEEVSLTFYEIlASYTDNIEAVSCDEALIDITSLLEET------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 80 lpstyieglpqgPTTAEEtvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKV 159
Cdd:cd01701 162 ------------YELPEE------------------------------------LAEAIRNEIRETTGCSASVGIGPNIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 160 LAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEILG-IEYMGELTQFTESQLQSHFGEKNGSWLYA 238
Cdd:cd01701 194 LARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGdTCGGLELRSKTKEKLQKVLGPKTGEKLYD 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382162 239 MCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLtkdrNDNDRVATQLVVSIRV 310
Cdd:cd01701 274 YCRGIDDRPVTGEKERKSVSAEINYG--IRFTNVDDVEQFLQRLSEELSKRL----EESNVTGRQITLKLMK 339
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
5-337 |
6.20e-24 |
|
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: 104.09 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 5 DAKKLCPDLLLAQvresrGKaNLTKYREASVEVMEIMSRFA---VIERASIDEAYVDLTsavqerlqklqgqpisadllp 81
Cdd:cd01703 53 DAKEICPDLVLVN-----GE-DLTPFRDMSKKVYRLLRSYSwndRVERLGFDENFMDVT--------------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 82 styieglpqgpttaeetvqkegmrkqglfqwldslqidnltspDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLA 161
Cdd:cd01703 106 -------------------------------------------EMRLLVASHIAYEMRERIENELGLTCCAGIASNKLLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 162 KLACGLNKPNRQT-LVSHGS--VPQLFSQMPIRKIRSLGGKLgASVIEILGIEYMGELTQFTESQLQSH----------- 227
Cdd:cd01703 143 KLVGSVNKPNQQTtLLPPSCadLMDFMDLHDLRKIPGIGYKT-AAKLEAHGISSVRDLQEFSNRNRQTVgaapsllelll 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 228 ----FGEKNGSWLYAMCRGIEHDPVKP-RQLPKTIGCSKNFPgKTALATREQVQWWLLQLAQELEERLTKDRNDNDrvat 302
Cdd:cd01703 222 mvkeFGEGIGQRIWKLLFGRDTSPVKPaSDFPQQISIEDSYK-KCSLEEIREARNKIEELLASLLERMKQDLQEVK---- 296
|
330 340 350
....*....|....*....|....*....|....*
gi 530382162 303 qlVVSIRVQGDKRLSSLRRccALTRYDAHKMSHDA 337
Cdd:cd01703 297 --AGDGRRPHTLRLTLRRY--TSTKKHYNRESKQA 327
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
6-293 |
3.56e-23 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 103.09 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPdlLLAQVRESRGKAnltkYREASVEVMEIMSRFA-VIERASIDEAYVDltsavqerlqklqgqpisadllpsty 84
Cdd:PRK03348 64 ARRLVG--NGAVVLPPRFVV----YRAASRRVFDTLRELSpVVEQLSFDEAFVE-------------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglPQG--PTTAEETVQkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAK 162
Cdd:PRK03348 112 ----PAElaGASAEEVEA---------------------------------FAERLRARVREETGLPASVGAGSGKQIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 163 LACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLG----GKLgasviEILGIEYMGELTQFTESQLQSHFGEKNGSWLYA 238
Cdd:PRK03348 155 IASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGpvteEKL-----HRLGIETIGDLAALSEAEVANLLGATVGPALHR 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 530382162 239 MCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKD 293
Cdd:PRK03348 230 LARGIDDRPVAERAEAKQISAESTFA--VDLTTRAQLREAIERIAEHAHRRLLKD 282
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
6-311 |
8.77e-22 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 98.18 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA-VIERASIDEAYVDLTsavqerlqklqgqpisadllpsty 84
Cdd:PRK01810 66 AKRLCPQLIVR-------RPNFDRYREASRQMFQILSEFTpLVQPVSIDEGYLDIT------------------------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglpqgPTTAEETVqkegmrkqglfqwldslqidnltspdlqltvgAVIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK01810 115 -------DCYALGSP--------------------------------LEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLgASVIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGIE 244
Cdd:PRK01810 156 SDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKT-AEKLKDIGIQTIGDLAKADEHILRAKLG-INGVRLQRRANGID 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 245 HDPVKPRQLP--KTIGCSKNFPGKTalaTREQVQWWLL-QLAQELEERLTKDRndndrvatqlVVSIRVQ 311
Cdd:PRK01810 234 DRPVDPEAIYqfKSVGNSTTLSHDM---DEEKELLDVLrRLSKSVSKRLQKKT----------VVSYNVQ 290
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
6-294 |
6.03e-21 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 94.78 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAQVRESRgkanltkYREASVEVMEIMSRFA-VIERASIDEAYVDLTSavqerlqklqgqpisadllpsty 84
Cdd:PRK14133 62 AKKRCPHGIFLPVRHER-------YKEVSKNIFKILYEVTpIVEPVSIDEAYLDITN----------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglpqgpttaeetVQKEGMRkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK14133 112 --------------IKEEPIK----------------------------IAKYIKKKVKKETGLTLSVGISYNKFLAKLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEIlGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGIE 244
Cdd:PRK14133 150 SDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNI-GIYTIEDLLKLSREFLIEYFG-KFGVEIYERIRGID 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530382162 245 HDPVKPRQLPKTIGCSKNFPGKTalATREQVQWWLLQLAQELEERLTKDR 294
Cdd:PRK14133 228 YREVEVSRERKSIGKETTLKKDT--KDKEELKKYLKDFSNIISEELKKRN 275
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
6-258 |
1.53e-20 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 94.30 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAQVRESRgkanltkYREASVEVMEIMSRFA-VIERASIDEAYVDLTSAvqerlQKLQGQPISadllpsty 84
Cdd:PRK03103 64 AQQKCPDLVVVKPRMQR-------YIDVSLQITRILEDFTdLVEPFSIDEQFLDVTGS-----QKLFGSPLE-------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK03103 124 -------------------------------------------------IAQKIQQRIMRETGVYARVGIGPNKLLAKMA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGL---NKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASvIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYAMCR 241
Cdd:PRK03103 155 CDNfakKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKH-LRRMGIRTIGQLANTPLERLKKRWG-INGEVLWRTAN 232
|
250
....*....|....*....
gi 530382162 242 GIEHDPVKPRQLP--KTIG 258
Cdd:PRK03103 233 GIDYSPVTPHSLDrqKAIG 251
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
1-165 |
7.93e-20 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 86.47 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 1 MWADDAKKLCPDLLLAqvresrgKANLTKYREASVEVMEIMSRFA--VIERASIDEAYVDLTSavqerLQKLQGQPISad 78
Cdd:pfam00817 50 MPVFEAKKLCPNLIVV-------PPDLELYRRASRKIFEILRRFStpKVEQASIDEAFLDLTG-----LEKLFGAEEA-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 79 llpstyieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNK 158
Cdd:pfam00817 116 -------------------------------------------------------LAKRLRREIAEETGLTCSIGIAPNK 140
|
....*..
gi 530382162 159 VLAKLAC 165
Cdd:pfam00817 141 LLAKLAS 147
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
5-309 |
9.49e-20 |
|
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: 91.07 E-value: 9.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 5 DAKKLCPDLLLAqVRESrgkaNLTKYREASVEVMEIMSRFAV-IERASIDEAYVDLTsavqerlqklqgqpisadllpst 83
Cdd:cd01700 55 KVPDLLERHGVA-VFSS----NYALYGDMSRRIMSILERFSPdVEVYSIDESFLDLT----------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 84 yieglpqgpttaeetvqkegmrkqglfqwlDSLQIDNLTSpdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKL 163
Cdd:cd01700 107 ------------------------------GSLRFGDLEE----------LARKIRRRILQETGIPVTVGIGPTKTLAKL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 164 ACGLNKPNRQT-----LVSHGSVPQLFSQMPIRKI----RSLGGKLGAsvieiLGIEYMGELTQFTESQLQSHFGeKNGS 234
Cdd:cd01700 147 ANDLAKKKNPYggvvdLTDEEVRDKLLKILPVGDVwgigRRTAKKLNA-----MGIHTAGDLAQADPDLLRKKFG-VVGE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382162 235 WLYAMCRGI---EHDPVKPRQlpKTIGCSKNFPGK-TALATREQVqwwLLQLAQELEERLtkdRNDNdRVATQLVVSIR 309
Cdd:cd01700 221 RLVRELNGIdclPLEEYPPPK--KSIGSSRSFGRDvTDLDELKQA---LAEYAERAAEKL---RRQK-SVARTISVFIG 290
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
136-309 |
2.49e-16 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 80.84 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 136 EEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEiLGIEYMGE 215
Cdd:PRK03352 125 EEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAA-LGITTVAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 216 LTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPV--KPRQlPKTIGCSKNFPgkTALATREQVQWWLLQLAQeleeRLTKD 293
Cdd:PRK03352 204 LAAADPAELAATFGPTTGPWLLLLARGGGDTEVsaEPWV-PRSRSREVTFP--QDLTDRAEVESAVRELAR----RVLDE 276
|
170
....*....|....*.
gi 530382162 294 RNDNDRVATQLVVSIR 309
Cdd:PRK03352 277 VVAEGRPVTRVAVKVR 292
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
6-257 |
4.89e-16 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 80.75 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDlllAQVResrgKANLTKYREASVEVMEIMSRFA-VIERASIDEAYVDLTSAvqERLQklqgqpisadllpsty 84
Cdd:PRK02794 94 ALKLCPD---AVVI----KPDMEKYVRVGREVRAMMQALTpLVEPLSIDEAFLDLSGT--ERLH---------------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglpqgpttaeetvqkeGMrkqglfqwldslqidnltSPdlqltvgAVIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK02794 149 ------------------GA------------------PP-------AVVLARFARRVEREIGITVSVGLSYNKFLAKIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASvIEILGIEYMGELTQFTESQLQSHFGEkNGSWLYAMCRGIE 244
Cdd:PRK02794 186 SDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAAR-LARDGIRTIGDLQRADEADLMRRFGS-MGLRLWRLARGID 263
|
250
....*....|...
gi 530382162 245 HDPVKPRQLPKTI 257
Cdd:PRK02794 264 DRKVSPDREAKSV 276
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
6-251 |
1.62e-12 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 69.43 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDLLLAQVRESrgkanltKYREASVEVMEIMSRFA-VIERASIDEAYVDLTSAVQErlqklqgqpisadllpstY 84
Cdd:PRK01216 64 AKKILPNAVYLPMRKE-------VYQQVSNRIMKLLREYSeKIEIASIDEAYLDISDKVKN------------------Y 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 IEGLPQGPTTAEETVQKEGMRkqglfqwldslqidnltspdlqLTVGaviveemraaieretgfqcsagISHNKVLAKLA 164
Cdd:PRK01216 119 QDAYNLGLEIKNKILEKEKIT----------------------VTVG----------------------ISKNKVFAKIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLgGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIE 244
Cdd:PRK01216 155 ADMAKPNGIKVIDDEEVKRFINELDIADIPGI-GDITAEKLKKLGVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEY 233
|
....*..
gi 530382162 245 HDPVKPR 251
Cdd:PRK01216 234 NEPVRAR 240
|
|
| zf_UBZ |
pfam18439 |
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA ... |
569-599 |
1.56e-11 |
|
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA polymerase eta (EC:2.7.7.7). It is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. The UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a beta-beta-alpha fold.
Pssm-ID: 465769 Cd Length: 32 Bit Score: 59.06 E-value: 1.56e-11
10 20 30
....*....|....*....|....*....|.
gi 530382162 569 DQVPCEKCGSLVPVWDMPEHMDYHFALELQK 599
Cdd:pfam18439 1 DTYVCPRCGKEIPESELPEHEDWHFAKDLQR 31
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
6-309 |
4.04e-11 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 65.39 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 6 AKKLCPDlllAQVRESRGKAnltkYREASVEVMEIMSRFA-VIERASIDEAYVDLTSavqerLQKLQGQPISadllpsty 84
Cdd:PRK03858 59 ARRLCPQ---AVVVPPRMSA----YSRASKAVFEVFRDTTpLVEGLSIDEAFLDVGG-----LRRISGTPVQ-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 85 ieglpqgpttaeetvqkegmrkqglfqwldslqidnltspdlqltvgavIVEEMRAAIERETGFQCSAGISHNKVLAKLA 164
Cdd:PRK03858 119 -------------------------------------------------IAARLRRRVREEVGLPITVGVARTKFLAKVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 165 CGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEIlGIEYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIE 244
Cdd:PRK03858 150 SQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAH-GITTVGDVAELPESALVSLLGPAAGRHLHALAHNRD 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382162 245 HDPVKPRQLPKTIGcsknfpGKTAL----ATREQVQWWLLQLAqeleERLTKDRNDNDRVATQLVVSIR 309
Cdd:PRK03858 229 PRRVETGRRRRSVG------AQRALgrgpNSPAEVDAVVVALV----DRVARRMRAAGRTGRTVVLRLR 287
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
93-333 |
4.61e-06 |
|
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: 49.30 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 93 TTAEETVQKEGMRKQGLFQWLD-SLQIDNLTSPD-LQLTVGAV---------IVEEMRAAIEReTGFQCSAGISHNKVLA 161
Cdd:cd03468 65 QVVEYDPEADARALQELALWLLrFTPLVALDGPDgLLLDVTGClhlfggedaLAASLRAALAT-LGLSARAGIADTPGAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 162 KLACGLNKP---NRQTlvSHGSVPQLFSQMPIRKIRSlgGKLGASVIEILGIEYMGELTQFTESQLQSHFGeKNGSWLYA 238
Cdd:cd03468 144 WLLARAGGGrgvLRRE--ALAAALVLLAPLPVAALRL--PPETVELLARLGLRTLGDLAALPRAELARRFG-LALLLRLD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 239 MCRGIEHDPVKPRQLPktigcsKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDNDRVATQLVVSIRvQGDKRLSS 318
Cdd:cd03468 219 QAYGRDPEPLLFSPPP------PAFDFRLELQLEEPIARGLLFPLRRLLEQLCAFLALRGLGARRLSLTLF-REDGRVTR 291
|
250
....*....|....*
gi 530382162 319 LRRCCALTRYDAHKM 333
Cdd:cd03468 292 VLVGLARPSRDDLPL 306
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
254-328 |
4.68e-06 |
|
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: 45.63 E-value: 4.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382162 254 PKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKDRndndRVATQLVVSIRvqgDKRLSSLRRCCALTRY 328
Cdd:pfam11799 1 RKSIGAERTFG--RDLTDLEELREALLELAEELAERLRRQG----LVARTVTVKIR---YSDFRTITRSVTLPSP 66
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
134-309 |
4.75e-04 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 43.08 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 134 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQ---TLVSHGSVPQLFSQMPIRKIRSLgGKLGASVIEILGI 210
Cdd:PTZ00205 252 VASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQhdlNLHTRGDVMTYVRDLGLRSVPGV-GKVTEALLKGLGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382162 211 EYMGELTQfTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLP------------KTIGCSKNFpgkTALATREQVQWW 278
Cdd:PTZ00205 331 TTLSDIYN-RRVELCYILHNNLFRFLLGASIGIMQWPDAATAANtencegatggqrKAISSERSF---TTPRTKEGLQEM 406
|
170 180 190
....*....|....*....|....*....|.
gi 530382162 279 LLQLAQELEERLTKdrndNDRVATQLVVSIR 309
Cdd:PTZ00205 407 VDTVFNGAYEEMRK----SELMCRQISLTIR 433
|
|
|