|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
39-316 |
1.00e-121 |
|
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: 365.64 E-value: 1.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 39 GVQQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSP--VVERLGFDENFVDLT 116
Cdd:cd01703 26 GIQQKYIVVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNGEDLTPFRDMSKKVYRLLRSYSWndRVERLGFDENFMDVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 117 EM-------VEKRLQQLQSDELSAVTVSG--------------HVYNNQC------------------------IGYKTA 151
Cdd:cd01703 106 EMrllvashIAYEMRERIENELGLTCCAGiasnkllaklvgsvNKPNQQTtllppscadlmdfmdlhdlrkipgIGYKTA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 152 KCLEALGINSVRDLQTFSP---------------KILEKELGISVAQRIQKLSFGEDNSPVI-LSGPPQSFSEEDSFKKC 215
Cdd:cd01703 186 AKLEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVKpASDFPQQISIEDSYKKC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 216 SSEV--EAKNKIEELLASLLNRVCQ--------DGRKPHTVRLIIRRYSSEKH-YGRESRQCPIPSHVIQKLGTGNYDVM 284
Cdd:cd01703 266 SLEEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTSTKKhYNRESKQAPIPSHVFQKLTGGNEIAA 345
|
330 340 350
....*....|....*....|....*....|....
gi 1192727683 285 TPMVDILMKLFRNMVNVK--MPFHLTLLSVCFCN 316
Cdd:cd01703 346 RPIEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
46-252 |
5.56e-37 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 140.66 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGeDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMV------ 119
Cdd:COG0389 39 VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPP-DFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSArlfgsa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 120 EKRLQQLQSD--ELSAVTVS-G--------------HVYNNQC---------------------IGYKTAKCLEALGINS 161
Cdd:COG0389 118 EAIARRIRRRirRETGLTVSvGiapnkflakiasdlAKPDGLTvippgevaaflaplpveklwgVGPKTAEKLARLGIRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 162 VRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKcssEVEAKNKIEELLASLLNRVC---- 237
Cdd:COG0389 198 IGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGE---DLTDLEELEAALRRLAERLAerlr 273
|
250
....*....|....*
gi 1192727683 238 QDGRKPHTVRLIIRR 252
Cdd:COG0389 274 RQGLGARTVTVKLRT 288
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
41-261 |
7.00e-26 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 110.12 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 41 QQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNgEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLT---- 116
Cdd:PRK01810 40 ERKGIIVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRR-PNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITdcya 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 117 --------EMVEKRLQQ-------------------------------LQSDELSAVTVSGHVYNNQCIGYKTAKCLEAL 157
Cdd:PRK01810 119 lgspleiaKMIQQRLLTelqlpcsigiapnkflakmasdmkkplgitvLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 158 GINSVRDLQTFSPKILEKELGISvAQRIQKLSFGEDNSPVilsgPPQSFSEEDS------FKKCSSEV-EAKNKIEELLA 230
Cdd:PRK01810 199 GIQTIGDLAKADEHILRAKLGIN-GVRLQRRANGIDDRPV----DPEAIYQFKSvgnsttLSHDMDEEkELLDVLRRLSK 273
|
250 260 270
....*....|....*....|....*....|.
gi 1192727683 231 SLLNRVCQDGRKPHTVRLIIrRYSSEKHYGR 261
Cdd:PRK01810 274 SVSKRLQKKTVVSYNVQIMI-RYHDRRTITR 303
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
46-137 |
2.18e-23 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 96.49 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVnGEDLTRYREMSYKVTELLEEFSPV-VERLGFDENFVDLTEMVE---- 120
Cdd:pfam00817 34 VAAASYEARKYGVRSGMPVFEAKKLCPNLIVV-PPDLELYRRASRKIFEILRRFSTPkVEQASIDEAFLDLTGLEKlfga 112
|
90 100
....*....|....*....|..
gi 1192727683 121 -----KRLQQLQSDELSaVTVS 137
Cdd:pfam00817 113 eealaKRLRREIAEETG-LTCS 133
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
584-609 |
3.89e-03 |
|
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: 35.28 E-value: 3.89e-03
10 20
....*....|....*....|....*.
gi 1192727683 584 PSDIDPQVFYELPEAVQKELLAEWKR 609
Cdd:cd19318 9 FSQVDPSVLAALPPDLQEELEAAYAQ 34
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
39-316 |
1.00e-121 |
|
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: 365.64 E-value: 1.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 39 GVQQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSP--VVERLGFDENFVDLT 116
Cdd:cd01703 26 GIQQKYIVVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNGEDLTPFRDMSKKVYRLLRSYSWndRVERLGFDENFMDVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 117 EM-------VEKRLQQLQSDELSAVTVSG--------------HVYNNQC------------------------IGYKTA 151
Cdd:cd01703 106 EMrllvashIAYEMRERIENELGLTCCAGiasnkllaklvgsvNKPNQQTtllppscadlmdfmdlhdlrkipgIGYKTA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 152 KCLEALGINSVRDLQTFSP---------------KILEKELGISVAQRIQKLSFGEDNSPVI-LSGPPQSFSEEDSFKKC 215
Cdd:cd01703 186 AKLEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVKpASDFPQQISIEDSYKKC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 216 SSEV--EAKNKIEELLASLLNRVCQ--------DGRKPHTVRLIIRRYSSEKH-YGRESRQCPIPSHVIQKLGTGNYDVM 284
Cdd:cd01703 266 SLEEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTSTKKhYNRESKQAPIPSHVFQKLTGGNEIAA 345
|
330 340 350
....*....|....*....|....*....|....
gi 1192727683 285 TPMVDILMKLFRNMVNVK--MPFHLTLLSVCFCN 316
Cdd:cd01703 346 RPIEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
39-315 |
3.37e-76 |
|
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: 246.50 E-value: 3.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 39 GVQQKY----LVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNgEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVD 114
Cdd:cd00424 26 VVVPFNsdstCVIACSYEARKYGVKRGMPVREARKMCPNLILVP-ARLDLYRRLSERLLSELEEVAPLVEVASIDELFLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 115 LTEMVEK---------RLQQLQSDELSAVTVSGHVYNN---------------QC---------------------IGYK 149
Cdd:cd00424 105 LTGSARLlglgsevalRIKRHIAEQLGGITASIGIASNkllaklaakyakpdgLTildpedlpgflsklpltdlpgIGAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 150 TAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKCSSEVE-AKNKIEEL 228
Cdd:cd00424 185 TAKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEdARPLLRLL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 229 LASLLNRVCQDGRKPHTVRLIIRRYSSE--KHYGRESRQCPIPSHViqklgtgnydVMTPMVDILMKLFRNMVNVKMPFH 306
Cdd:cd00424 265 LEKLARRLRRDGRGATRLRLWLRTVDGRwsGHADIPSRSAPRPIST----------EDGELLHALDKLWRALLDDKGPRR 334
|
....*....
gi 1192727683 307 LTLLSVCFC 315
Cdd:cd00424 335 LRRLGVRLS 343
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
46-272 |
1.05e-37 |
|
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: 142.66 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGeDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMVE----- 120
Cdd:cd03586 36 VSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPP-RFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYVRlfgsa 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 121 ----KRLQQLQSDELSaVTVSGHVYNN---------------QC---------------------IGYKTAKCLEALGIN 160
Cdd:cd03586 115 teiaKEIRARIREETG-LTASAGIAPNkflakiasdlnkpngLTvippedveeflaplpvrkipgVGKVTAEKLKELGIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 161 SVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSF-KKCSSEVEAKNKIEELLASLLNRVCQD 239
Cdd:cd03586 194 TIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFsEDLTDPEELLEELLELAEELAERLRKR 272
|
250 260 270
....*....|....*....|....*....|...
gi 1192727683 240 GRKPHTVRLIIRRYSSEKHygreSRQCPIPSHV 272
Cdd:cd03586 273 GLKGRTVTVKLKYADFSTR----TRSRTLPEPT 301
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
46-252 |
5.56e-37 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 140.66 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGeDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMV------ 119
Cdd:COG0389 39 VAAASYEARAFGVRSGMPLFQARRLCPDLVVLPP-DFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSArlfgsa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 120 EKRLQQLQSD--ELSAVTVS-G--------------HVYNNQC---------------------IGYKTAKCLEALGINS 161
Cdd:COG0389 118 EAIARRIRRRirRETGLTVSvGiapnkflakiasdlAKPDGLTvippgevaaflaplpveklwgVGPKTAEKLARLGIRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 162 VRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKcssEVEAKNKIEELLASLLNRVC---- 237
Cdd:COG0389 198 IGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGE---DLTDLEELEAALRRLAERLAerlr 273
|
250
....*....|....*
gi 1192727683 238 QDGRKPHTVRLIIRR 252
Cdd:COG0389 274 RQGLGARTVTVKLRT 288
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
50-316 |
1.92e-26 |
|
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: 111.25 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 50 NYEARKLGVKKLMNVRDAKEKCPQLVLV------NGED----------------LTRYREMSYKVTELLEEFSPVVERLG 107
Cdd:cd01702 37 SYAARAFGVTRFMTIDEAKKKCPDLILAhvatykKGEDeadyhenpsparhkvsLDPYRRASRKILNILKRFGDVVEKAS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 108 FDENFVDLTEMVEKRLQQLQSDELSAVTVSG--------------HVYNNQCI---------------------GYKTAK 152
Cdd:cd01702 117 IDEAYLDLGSRIVEEIRQQVYDELGYTCSAGiahnkmlaklasgmNKPNAQTIlrndavasflsslpitsirglGGKLGE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 153 CL-EALGINSVRDLQTF--SPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSF--KKCSSEVEAKNKIEE 227
Cdd:cd01702 197 EIiDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpgKTALSTEDVQHWLLV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 228 LLASLLNRVCQD----GRKPHTVRLiirRYSSEKHYGRESRQCPIPSHVIQKLgtgnydvMTPMVDILMKLFRNMVNVKM 303
Cdd:cd01702 277 LASELNSRLEDDryenNRRPKTLVL---SLRQRGDGVRRSRSCALPRYDAQKI-------VKDAFKLIKAINEEGLGLAW 346
|
330
....*....|...
gi 1192727683 304 PFHLTLLSVCFCN 316
Cdd:cd01702 347 NYPLTLLSLSFTK 359
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
41-261 |
7.00e-26 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 110.12 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 41 QQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNgEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLT---- 116
Cdd:PRK01810 40 ERKGIIVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRR-PNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITdcya 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 117 --------EMVEKRLQQ-------------------------------LQSDELSAVTVSGHVYNNQCIGYKTAKCLEAL 157
Cdd:PRK01810 119 lgspleiaKMIQQRLLTelqlpcsigiapnkflakmasdmkkplgitvLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 158 GINSVRDLQTFSPKILEKELGISvAQRIQKLSFGEDNSPVilsgPPQSFSEEDS------FKKCSSEV-EAKNKIEELLA 230
Cdd:PRK01810 199 GIQTIGDLAKADEHILRAKLGIN-GVRLQRRANGIDDRPV----DPEAIYQFKSvgnsttLSHDMDEEkELLDVLRRLSK 273
|
250 260 270
....*....|....*....|....*....|.
gi 1192727683 231 SLLNRVCQDGRKPHTVRLIIrRYSSEKHYGR 261
Cdd:PRK01810 274 SVSKRLQKKTVVSYNVQIMI-RYHDRRTITR 303
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
46-137 |
2.18e-23 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 96.49 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVnGEDLTRYREMSYKVTELLEEFSPV-VERLGFDENFVDLTEMVE---- 120
Cdd:pfam00817 34 VAAASYEARKYGVRSGMPVFEAKKLCPNLIVV-PPDLELYRRASRKIFEILRRFSTPkVEQASIDEAFLDLTGLEKlfga 112
|
90 100
....*....|....*....|..
gi 1192727683 121 -----KRLQQLQSDELSaVTVS 137
Cdd:pfam00817 113 eealaKRLRREIAEETG-LTCS 133
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
31-246 |
1.58e-21 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 96.34 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 31 VGAAASSQGVqqkylVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGeDLTRYREMSYKVTELLEEFSPVVERLGFDE 110
Cdd:PRK02406 23 VGGSPGRRGV-----ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPG-RFDVYKEVSRQIREIFRRYTDLIEPLSLDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 111 NFVDLTE---------MVEKRLQQLQSDELSaVTVSGHVYNN---------------QC--------------------- 145
Cdd:PRK02406 97 AYLDVTDnklcigsatLIAQEIRQDIFEELG-LTASAGVAPNkflakiasdwnkpngLFvitpeevdaflatlpvekipg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 146 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKK-CSSEVEAKNK 224
Cdd:PRK02406 176 VGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEdLYDLEACLAE 254
|
250 260
....*....|....*....|....*
gi 1192727683 225 IEEL---LASLLNRVcQDGRKPHTV 246
Cdd:PRK02406 255 LPRLaekLERRLERA-KPDKRIKTV 278
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
43-276 |
6.98e-16 |
|
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: 79.13 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 43 KYLVV-----TC----NYEARKLGVKKLMNVRDAKEKCPQL-VLVNGEDLTRYREMSYKVTELLEEFSPVVERLGFDENF 112
Cdd:cd01700 23 RPLVVlsnndGCviarSPEAKALGIKMGSPYFKVPDLLERHgVAVFSSNYALYGDMSRRIMSILERFSPDVEVYSIDESF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 113 VDLTEM--------VEKRLQQLQSDELS-AVTV---------------------SGHV----YNNQC------------- 145
Cdd:cd01700 103 LDLTGSlrfgdleeLARKIRRRILQETGiPVTVgigptktlaklandlakkknpYGGVvdltDEEVRdkllkilpvgdvw 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 146 -IGYKTAKCLEALGINSVRDLQTFSPKILEKELGIsVAQRIQKLSFGEDNSPVILSGPP-QSFSEEDSFKKcssEVEAKN 223
Cdd:cd01700 183 gIGRRTAKKLNAMGIHTAGDLAQADPDLLRKKFGV-VGERLVRELNGIDCLPLEEYPPPkKSIGSSRSFGR---DVTDLD 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1192727683 224 KIEELLASLLNRVC----QDGRKPHTVRLIIR--RYSSEKHYGRESRQCPIPSHVIQKL 276
Cdd:cd01700 259 ELKQALAEYAERAAeklrRQKSVARTISVFIGtsGFSRQPKYYSATNTLPYPTNDTREI 317
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
46-251 |
7.83e-16 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 79.30 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTC-NYEARKLGVKKLMNVRDAKEKCPQLVLVNgEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLT----EMVE 120
Cdd:PRK03352 46 VVTCaSYEARAFGVRAGMPLRTAARRCPDAVFLP-SDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLGVDtddpEALA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 121 KRLQQLQSDE-------------LSAVTVSGH-----VY----NNQC-------------IGYKTAKCLEALGINSVRDL 165
Cdd:PRK03352 125 EEIRAAVLERtglscsvgigdnkLRAKIATGFakpagVFrltdANWMavmgdrptdalwgVGPKTAKRLAALGITTVADL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 166 QTFSPKILEKELGISVAQRIQKLSFGEDNSPVIlSGP--PQSFSEEDSFKK---CSSEVEAknKIEELLASLLNRVCQDG 240
Cdd:PRK03352 205 AAADPAELAATFGPTTGPWLLLLARGGGDTEVS-AEPwvPRSRSREVTFPQdltDRAEVES--AVRELARRVLDEVVAEG 281
|
250
....*....|.
gi 1192727683 241 RKPHTVRLIIR 251
Cdd:PRK03352 282 RPVTRVAVKVR 292
|
|
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
49-252 |
8.71e-15 |
|
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: 76.58 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 49 CNYEARKLGVKKLMNVRDAKEKCPQLVLVnGEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMVEKR---LQQ 125
Cdd:cd01701 89 CNYEARSYGIKNGMWVGQAKKLCPQLVTL-PYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETyelPEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 126 LQS---DELSAVT-------VSGHVY-----------NNQC---------------------IGYKTA-KCLEALG-INS 161
Cdd:cd01701 168 LAEairNEIRETTgcsasvgIGPNILlarlatrkakpDGQYhlsaekveeflsqlkvgdlpgVGSSLAeKLVKLFGdTCG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 162 VRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDS----FKKcssEVEAKNKIEELLASLLNRVC 237
Cdd:cd01701 248 GLELRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINygirFTN---VDDVEQFLQRLSEELSKRLE 324
|
250
....*....|....*.
gi 1192727683 238 QDGRKPHTVRL-IIRR 252
Cdd:cd01701 325 ESNVTGRQITLkLMKR 340
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
39-258 |
1.64e-14 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 75.14 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 39 GVQQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEdLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEM 118
Cdd:PRK14133 34 GISERGVVSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVR-HERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDITNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 119 VE----------------------------KRLQQLQSDE-----------------LSAVTVSgHVYNnqcIGYKTAKC 153
Cdd:PRK14133 113 KEepikiakyikkkvkketgltlsvgisynKFLAKLASDWnkpdgikiitedmipdiLKPLPIS-KVHG---IGKKSVEK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 154 LEALGINSVRDLQTFSPKILEK---ELGISVAQRIQklsfGEDNSPVILSGPPQSFSEEDSFKKcssEVEAKNKIEELLA 230
Cdd:PRK14133 189 LNNIGIYTIEDLLKLSREFLIEyfgKFGVEIYERIR----GIDYREVEVSRERKSIGKETTLKK---DTKDKEELKKYLK 261
|
250 260 270
....*....|....*....|....*....|..
gi 1192727683 231 SLLNRVCQDGRKPH----TVRLIIRRYSSEKH 258
Cdd:PRK14133 262 DFSNIISEELKKRNlygkTVTVKIKTSDFQTH 293
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
46-253 |
2.16e-14 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 75.74 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEM------- 118
Cdd:PRK03348 43 VAGASYEARVFGARSAMPMHQARRLVGNGAVVLPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEPAELagasaee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 119 VEKRLQQLQS---------------------------------------------DELSAVTVSGhvynnqcIGYKTAKC 153
Cdd:PRK03348 123 VEAFAERLRArvreetglpasvgagsgkqiakiasglakpdgirvvppgeerellAPLPVRRLWG-------IGPVTEEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 154 LEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKK-CSSEVEAKNKIEELLASL 232
Cdd:PRK03348 196 LHRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVdLTTRAQLREAIERIAEHA 275
|
250 260
....*....|....*....|.
gi 1192727683 233 LNRVCQDGRKPHTVRLIIRRY 253
Cdd:PRK03348 276 HRRLLKDGRGARTVTVKLRKS 296
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
46-212 |
3.32e-14 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 74.97 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGeDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDL--TEMVEK-- 121
Cdd:PRK02794 73 VSTACYIARIHGVRSAMPMFKALKLCPDAVVIKP-DMEKYVRVGREVRAMMQALTPLVEPLSIDEAFLDLsgTERLHGap 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 122 ------RLQQLQSDELsAVTVS-GHVYNN-----------------------------------QCIGYKTAKCLEALGI 159
Cdd:PRK02794 152 pavvlaRFARRVEREI-GITVSvGLSYNKflakiasdldkprgfsvigraealaflapkpvgiiWGVGPATAARLARDGI 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1192727683 160 NSVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSF 212
Cdd:PRK02794 231 RTIGDLQRADEADLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTF 282
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
51-271 |
1.43e-11 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 66.56 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 51 YEARKLGVKKLMNVRDAKEKCPQLVLVNGEdLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLT---------EMVEK 121
Cdd:PRK03103 48 PLAKAYGVKTAERLWEAQQKCPDLVVVKPR-MQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTgsqklfgspLEIAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 122 RLQQ--------------------------------------LQSDELSAVTVSGHVYNNQCIGYKTAKCLEALGINSVR 163
Cdd:PRK03103 127 KIQQrimretgvyarvgigpnkllakmacdnfakknpdglftLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 164 DLQTFSPKILEKELGIsVAQRIQKLSFGEDNSPVilsgPPQSFSEEDSFKKCSS---EVEAKNKIEELLASLLNRVCQDG 240
Cdd:PRK03103 207 QLANTPLERLKKRWGI-NGEVLWRTANGIDYSPV----TPHSLDRQKAIGHQMTlprDYRGFEEIKVVLLELCEEVCRRA 281
|
250 260 270
....*....|....*....|....*....|....*.
gi 1192727683 241 RKPH----TVRLIIRrySSEKHYGRE-SRQCPIPSH 271
Cdd:PRK03103 282 RAKGymgrTVSVSLR--GADFDWPTGfSRQMTLPEP 315
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
46-114 |
1.76e-10 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 63.08 E-value: 1.76e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEdLTRYREMSYKVTELLEEFSPVVERLGFDENFVD 114
Cdd:PRK03858 38 VLAASYEAKAYGVRTAMGGRQARRLCPQAVVVPPR-MSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLD 105
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
46-197 |
4.54e-09 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 58.65 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 46 VVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTrYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMVE----- 120
Cdd:PRK01216 43 VATANYEARKLGIKAGMPIVEAKKILPNAVYLPMRKEV-YQQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKnyqda 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 121 -----KRLQQLQSDELSAVTVS--------------------GHVYNNQC--------------IGYKTAKCLEALGINS 161
Cdd:PRK01216 122 ynlglEIKNKILEKEKITVTVGisknkvfakiaadmakpngiKVIDDEEVkrfineldiadipgIGDITAEKLKKLGVNK 201
|
170 180 190
....*....|....*....|....*....|....*.
gi 1192727683 162 VRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPV 197
Cdd:PRK01216 202 LVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPV 237
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
203-317 |
1.13e-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: 47.17 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727683 203 PQSFSEEDSF-KKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYssekHYGRESRQCPIPSHviqklgTGNY 281
Cdd:pfam11799 1 RKSIGAERTFgRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIRYS----DFRTITRSVTLPSP------TDDT 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 1192727683 282 DVMTpmvDILMKLFRNMVNvkmPFHLTLLSVCFCNL 317
Cdd:pfam11799 71 DEIY---RAALRLLRRLYR---GRPVRLLGVSLSNL 100
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
41-116 |
6.95e-05 |
|
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: 45.45 E-value: 6.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1192727683 41 QQKYLVVT-CNYEARKLGVKKLMNVRDAKEKCPQLVLVNgEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLT 116
Cdd:cd03468 30 RKKAGRILaCNAAARAAGVRPGMPLAEALALCPNLQVVE-YDPEADARALQELALWLLRFTPLVALDGPDGLLLDVT 105
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
46-116 |
1.09e-04 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 45.14 E-value: 1.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1192727683 46 VVTCNYEARKLGVK---KLMNVRDAKEKCPQLVLVNGEDLtrYREMSYKVTELLEEFSPVVERLGFDENFVDLT 116
Cdd:PRK03609 37 VIARSAEAKALGIKmgdPWFKQKDLFRRCGVVCFSSNYEL--YADMSNRVMSTLEELSPRVEIYSIDEAFCDLT 108
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
584-609 |
3.89e-03 |
|
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: 35.28 E-value: 3.89e-03
10 20
....*....|....*....|....*.
gi 1192727683 584 PSDIDPQVFYELPEAVQKELLAEWKR 609
Cdd:cd19318 9 FSQVDPSVLAALPPDLQEELEAAYAQ 34
|
|
|