|
Name |
Accession |
Description |
Interval |
E-value |
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
31-341 |
5.23e-59 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 198.44 E-value: 5.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 31 PVAVTLANR---VIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEGVIAAVDDLVPRAELLRPGLLVLP 107
Cdd:COG0389 27 PVAVGGDNNrgvVAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 108 VRGPARFFGSEQMAAERLIDAVAAA-GAECQVGIADRLSTAVFAARAG-----RIVEPGGDARFLSLLSIRQLAtepsls 181
Cdd:COG0389 107 VTGSARLFGSAEAIARRIRRRIRREtGLTVSVGIAPNKFLAKIASDLAkpdglTVIPPGEVAAFLAPLPVEKLW------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 182 GPGRDdLTDLLWRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARGEPERAPCGREPPPDLAAELACDPPIDRVDAAAF 261
Cdd:COG0389 181 GVGPK-TAEKLARLGIRTIGDLAALPRAELRRRFGKVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 262 AGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSRVWRCAEPLTEDAT-ADRVRWQLDGWlnnrnarDRPTAAVTLLR 340
Cdd:COG0389 260 ALRRLAERLAERLRRQGLGARTVTVKLRTSDFRTTTRSRTLPEPTDDTAElLRAARELLERI-------YRPGRPVRLLG 332
|
.
gi 489997036 341 L 341
Cdd:COG0389 333 V 333
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
8-345 |
5.49e-45 |
|
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: 161.39 E-value: 5.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 8 LAIWCMDWPAVAAAAAAGLSATAPVAV---TLANRVIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEG 84
Cdd:cd03468 1 LALWFPRLPLDALLRNRPADDEAPLAVverKKAGRILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDPEADARALQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 85 VIAAVDDLVPRAELLRPGLLVLPVRGPARFFGSEQMAAERLIDAVAAAGAECQVGIADRLSTAVFAARAG--RIVEPGGD 162
Cdd:cd03468 81 LALWLLRFTPLVALDGPDGLLLDVTGCLHLFGGEDALAASLRAALATLGLSARAGIADTPGAAWLLARAGggRGVLRREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 163 ARFLSLLSIRQLATEPSLSGPGRDDLTdllwRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARG-EPERAPCG-REPP 240
Cdd:cd03468 161 LAAALVLLAPLPVAALRLPPETVELLA----RLGLRTLGDLAALPRAELARRFGLALLLRLDQAYGrDPEPLLFSpPPPA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 241 PDLAAELAcdPPIDRVDAAAFAGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSRVWRCAEPLTEDAT-ADRVRWQL 319
Cdd:cd03468 237 FDFRLELQ--LEEPIARGLLFPLRRLLEQLCAFLALRGLGARRLSLTLFREDGRVTRVLVGLARPSRDDLPlLRLLRERL 314
|
330 340
....*....|....*....|....*.
gi 489997036 320 DgwlnnRNARDRPTAAVTLLRLQAVE 345
Cdd:cd03468 315 E-----RLALPRGIAPVRLLALTAEP 335
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
31-142 |
9.38e-08 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 51.42 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 31 PVAV---TLANRVIACSATARAAGVRRGLRRREAAARCPQLFIATADAD--RDA--RLFEGVIAAVDDLVPRAELLRpgl 103
Cdd:pfam00817 22 PVAVgggNGRGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLElyRRAsrKIFEILRRFSTPKVEQASIDE--- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489997036 104 LVLPVRGPARFFGSEQMAAERLIDAVAAA-GAECQVGIAD 142
Cdd:pfam00817 99 AFLDLTGLEKLFGAEEALAKRLRREIAEEtGLTCSIGIAP 138
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
40-226 |
6.61e-07 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 51.53 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 40 VIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEGVIAAVDDLVPRAELLRPGLLVLPVRGPARFFGSEQ 119
Cdd:PRK03858 38 VLAASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGGLRRISGTPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 120 MAAERLIDAVAA-AGAECQVGIADRLSTAVFAARAGR-----IVEPGGDARFLSLLSIRQLAtepslsGPGrDDLTDLLW 193
Cdd:PRK03858 118 QIAARLRRRVREeVGLPITVGVARTKFLAKVASQVAKpdgllVVPPDRELAFLHPLPVRRLW------GVG-PVTAAKLR 190
|
170 180 190
....*....|....*....|....*....|...
gi 489997036 194 RMGIRTIGQFAALSRTDVASRFGAdAVAAHRFA 226
Cdd:PRK03858 191 AHGITTVGDVAELPESALVSLLGP-AAGRHLHA 222
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
31-341 |
5.23e-59 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 198.44 E-value: 5.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 31 PVAVTLANR---VIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEGVIAAVDDLVPRAELLRPGLLVLP 107
Cdd:COG0389 27 PVAVGGDNNrgvVAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 108 VRGPARFFGSEQMAAERLIDAVAAA-GAECQVGIADRLSTAVFAARAG-----RIVEPGGDARFLSLLSIRQLAtepsls 181
Cdd:COG0389 107 VTGSARLFGSAEAIARRIRRRIRREtGLTVSVGIAPNKFLAKIASDLAkpdglTVIPPGEVAAFLAPLPVEKLW------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 182 GPGRDdLTDLLWRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARGEPERAPCGREPPPDLAAELACDPPIDRVDAAAF 261
Cdd:COG0389 181 GVGPK-TAEKLARLGIRTIGDLAALPRAELRRRFGKVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 262 AGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSRVWRCAEPLTEDAT-ADRVRWQLDGWlnnrnarDRPTAAVTLLR 340
Cdd:COG0389 260 ALRRLAERLAERLRRQGLGARTVTVKLRTSDFRTTTRSRTLPEPTDDTAElLRAARELLERI-------YRPGRPVRLLG 332
|
.
gi 489997036 341 L 341
Cdd:COG0389 333 V 333
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
8-345 |
5.49e-45 |
|
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: 161.39 E-value: 5.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 8 LAIWCMDWPAVAAAAAAGLSATAPVAV---TLANRVIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEG 84
Cdd:cd03468 1 LALWFPRLPLDALLRNRPADDEAPLAVverKKAGRILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDPEADARALQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 85 VIAAVDDLVPRAELLRPGLLVLPVRGPARFFGSEQMAAERLIDAVAAAGAECQVGIADRLSTAVFAARAG--RIVEPGGD 162
Cdd:cd03468 81 LALWLLRFTPLVALDGPDGLLLDVTGCLHLFGGEDALAASLRAALATLGLSARAGIADTPGAAWLLARAGggRGVLRREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 163 ARFLSLLSIRQLATEPSLSGPGRDDLTdllwRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARG-EPERAPCG-REPP 240
Cdd:cd03468 161 LAAALVLLAPLPVAALRLPPETVELLA----RLGLRTLGDLAALPRAELARRFGLALLLRLDQAYGrDPEPLLFSpPPPA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 241 PDLAAELAcdPPIDRVDAAAFAGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSRVWRCAEPLTEDAT-ADRVRWQL 319
Cdd:cd03468 237 FDFRLELQ--LEEPIARGLLFPLRRLLEQLCAFLALRGLGARRLSLTLFREDGRVTRVLVGLARPSRDDLPlLRLLRERL 314
|
330 340
....*....|....*....|....*.
gi 489997036 320 DgwlnnRNARDRPTAAVTLLRLQAVE 345
Cdd:cd03468 315 E-----RLALPRGIAPVRLLALTAEP 335
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
31-298 |
1.05e-13 |
|
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: 72.39 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 31 PVAVTLAN----RVIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEGVIAAVDDLVPRAELLRPGLLVL 106
Cdd:cd00424 24 PVVVVPFNsdstCVIACSYEARKYGVKRGMPVREARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 107 PVRGPARFFGSEQMAAERLIDAVAA--AGAECQVGIADRLSTAVFAARAGR-----IVEPGGDARFLSLLSIRqlatepS 179
Cdd:cd00424 104 DLTGSARLLGLGSEVALRIKRHIAEqlGGITASIGIASNKLLAKLAAKYAKpdgltILDPEDLPGFLSKLPLT------D 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 180 LSGPGRdDLTDLLWRMGIRTIGQFAALSRTD-VASRFGADAVAAHRFARGEPERAPCGREPPPDLAAELACDPPIDRVDA 258
Cdd:cd00424 178 LPGIGA-VTAKRLEAVGINPIGDLLAASPDAlLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAED 256
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489997036 259 AAFAGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSR 298
Cdd:cd00424 257 ARPLLRLLLEKLARRLRRDGRGATRLRLWLRTVDGRWSGH 296
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
31-142 |
9.38e-08 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 51.42 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 31 PVAV---TLANRVIACSATARAAGVRRGLRRREAAARCPQLFIATADAD--RDA--RLFEGVIAAVDDLVPRAELLRpgl 103
Cdd:pfam00817 22 PVAVgggNGRGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLElyRRAsrKIFEILRRFSTPKVEQASIDE--- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489997036 104 LVLPVRGPARFFGSEQMAAERLIDAVAAA-GAECQVGIAD 142
Cdd:pfam00817 99 AFLDLTGLEKLFGAEEALAKRLRREIAEEtGLTCSIGIAP 138
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
31-298 |
2.74e-07 |
|
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: 52.52 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 31 PVAV-TLANR--VIACSATARAAGVRRGLRRREAAARCPQLFIATADADR----DARLFEgVIAAVDDLVpraELLrpGL 103
Cdd:cd03586 24 PVAVgGSSDRgvVSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPRFDKyrevSRQIME-ILREYTPLV---EPL--SI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 104 --LVLPVRGPARFFGSEQMAAERLIDAVAAA-GAECQVGIADrlsTAVFAARA-------G-RIVEPGGDARFLSLLSIR 172
Cdd:cd03586 98 deAYLDVTDYVRLFGSATEIAKEIRARIREEtGLTASAGIAP---NKFLAKIAsdlnkpnGlTVIPPEDVEEFLAPLPVR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 173 QL-----ATEPSLSgpgrddltdllwRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARGEPERAPCGREPPPDLAAEL 247
Cdd:cd03586 175 KIpgvgkVTAEKLK------------ELGIKTIGDLAKLDVELLKKLFGKSGRRLYELARGIDNRPVEPDRERKSIGVER 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489997036 248 ACDPPIDRVDAAAFAGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSR 298
Cdd:cd03586 243 TFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVKLKYADFSTRTR 293
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
40-226 |
6.61e-07 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 51.53 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 40 VIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEGVIAAVDDLVPRAELLRPGLLVLPVRGPARFFGSEQ 119
Cdd:PRK03858 38 VLAASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGGLRRISGTPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 120 MAAERLIDAVAA-AGAECQVGIADRLSTAVFAARAGR-----IVEPGGDARFLSLLSIRQLAtepslsGPGrDDLTDLLW 193
Cdd:PRK03858 118 QIAARLRRRVREeVGLPITVGVARTKFLAKVASQVAKpdgllVVPPDRELAFLHPLPVRRLW------GVG-PVTAAKLR 190
|
170 180 190
....*....|....*....|....*....|...
gi 489997036 194 RMGIRTIGQFAALSRTDVASRFGAdAVAAHRFA 226
Cdd:PRK03858 191 AHGITTVGDVAELPESALVSLLGP-AAGRHLHA 222
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
155-280 |
8.11e-07 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 51.47 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 155 RIVEPGGDARFLSLLSIRQL-----ATEPSLSgpgrddltdllwRMGIRTIGQFAALSRTDVASRFG-ADAVAAHRFARG 228
Cdd:PRK03348 166 RVVPPGEERELLAPLPVRRLwgigpVTEEKLH------------RLGIETIGDLAALSEAEVANLLGaTVGPALHRLARG 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489997036 229 EPERAPCGREPPPDLAAELACDPPIDRVDAAAFAGRSLAAELHRALMAAGVG 280
Cdd:PRK03348 234 IDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRG 285
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
31-71 |
5.27e-04 |
|
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: 42.30 E-value: 5.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489997036 31 PVAVTLANRVIACSATARAAGVRRGLRRREAAARCPQLFIA 71
Cdd:cd01702 24 PVAVVQWNSIIAVSYAARAFGVTRFMTIDEAKKKCPDLILA 64
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
192-273 |
1.16e-03 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 41.46 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 192 LWRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARGEPERAPCGREP----------------PPDLAAELA--CDPPI 253
Cdd:PRK02794 225 LARDGIRTIGDLQRADEADLMRRFGSMGLRLWRLARGIDDRKVSPDREaksvsaettfetdlsdFEDLEPILWrlSEKVS 304
|
90 100
....*....|....*....|
gi 489997036 254 DRVDAAAFAGRSLAAELHRA 273
Cdd:PRK02794 305 RRLKAAGLAGRTVTLKLKTA 324
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
35-308 |
2.23e-03 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 40.39 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 35 TLANRVIAC-SATARAAGVRRGLRRREAAARCPQLFIATADADRdarlFEGVIAAVDDlvpraeLLRPGLLVLPVRG-PA 112
Cdd:PRK03352 41 TEPRKVVTCaSYEARAFGVRAGMPLRTAARRCPDAVFLPSDPAA----YDAASEEVMA------TLRDLGVPVEVWGwDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 113 RFFGSE----QMAAERLIDAVAAA-GAECQVGIADRLSTAVFAARAGRivePGGdarflsllsIRQLATEPSLSGPGrDD 187
Cdd:PRK03352 111 AFLGVDtddpEALAEEIRAAVLERtGLSCSVGIGDNKLRAKIATGFAK---PAG---------VFRLTDANWMAVMG-DR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997036 188 LTDLLW-----------RMGIRTIGQFAALSRTDVASRFGAD-AVAAHRFARGEPErAPCGREPPPDLAAELACDPPIDR 255
Cdd:PRK03352 178 PTDALWgvgpktakrlaALGITTVADLAAADPAELAATFGPTtGPWLLLLARGGGD-TEVSAEPWVPRSRSREVTFPQDL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489997036 256 VDAAAFAG--RSLAAELHRALMAAGVGCTRLAIHAVTANGEERSRVWRCAEPLTE 308
Cdd:PRK03352 257 TDRAEVESavRELARRVLDEVVAEGRPVTRVAVKVRTATFYTRTKIRKLPEPTTD 311
|
|
| |
