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Conserved domains on  [gi|1907130013|ref|XP_036017052|]
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DNA polymerase iota isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PolY super family cl28996
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ...
 38-277 7.94e-104

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.


The actual alignment was detected with superfamily member cd01703:

Pssm-ID: 452909 [Multi-domain]  Cd Length: 379  Bit Score: 318.26  E-value: 7.94e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  38 RLVVGSQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLI--HSLNHIKEIPGIGYKTAKR 115
Cdd:cd01703   108 RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPPSCADLMdfMDLHDLRKIPGIGYKTAAK 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 116 LEVLGINSVHDLQTFPI---------------KTLEKELGIAIAQRIQQLSFGEDKSPV-TPSGPPQSFSEEDTFKKCSS 179
Cdd:cd01703   188 LEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVkPASDFPQQISIEDSYKKCSL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 180 EV--EAKAKIEELLSSLLTRVCQ--------DGRKPHTVRLVIRRYSD--KHCNRESRQCPIPSHVIQKLGTGNHDSMPP 247
Cdd:cd01703   268 EEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTStkKHYNRESKQAPIPSHVFQKLTGGNEIAARP 347

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907130013 248 LIDILMKLFRNMVNVK--MPFHLTLMSVCFCN 277
Cdd:cd01703   348 IEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
Rev1_UBM2 super family cl41665
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 545-573 6.30e-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.


The actual alignment was detected with superfamily member cd19318:

Pssm-ID: 412037  Cd Length: 36  Bit Score: 34.51  E-value: 6.30e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907130013 545 LPFPPDIDPQVFYELPEEVQKELMAEWER 573
Cdd:cd19318     6 LPSFSQVDPSVLAALPPDLQEELEAAYAQ 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. ...
 38-277 7.94e-104

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: 318.26  E-value: 7.94e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  38 RLVVGSQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLI--HSLNHIKEIPGIGYKTAKR 115
Cdd:cd01703   108 RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPPSCADLMdfMDLHDLRKIPGIGYKTAAK 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 116 LEVLGINSVHDLQTFPI---------------KTLEKELGIAIAQRIQQLSFGEDKSPV-TPSGPPQSFSEEDTFKKCSS 179
Cdd:cd01703   188 LEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVkPASDFPQQISIEDSYKKCSL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 180 EV--EAKAKIEELLSSLLTRVCQ--------DGRKPHTVRLVIRRYSD--KHCNRESRQCPIPSHVIQKLGTGNHDSMPP 247
Cdd:cd01703   268 EEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTStkKHYNRESKQAPIPSHVFQKLTGGNEIAARP 347

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907130013 248 LIDILMKLFRNMVNVK--MPFHLTLMSVCFCN 277
Cdd:cd01703   348 IEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 44-268 3.31e-39

Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];


Pssm-ID: 440158 [Multi-domain]  Cd Length: 336  Bit Score: 146.44  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLnHIKEIPGIGYKTAKRLEVLGINS 123
Cdd:COG0389   119 AIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPL-PVEKLWGVGPKTAEKLARLGIRT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 124 VHDLQTFPIKTLEKELGIAiAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKKcssEVEAKAKIEELLSSLLTRVC---- 199
Cdd:COG0389   198 IGDLAALPRAELRRRFGKV-GERLYRLARGIDPRPVEPRRPRKSIGVERTFGE---DLTDLEELEAALRRLAERLAerlr 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130013 200 QDGRKPHTVRLVIrRYSDKHCNRESRQCPIPShviqklgtgnhDSMPPLIDILMKLFRNMVNVKMPFHL 268
Cdd:COG0389   274 RQGLGARTVTVKL-RTSDFRTTTRSRTLPEPT-----------DDTAELLRAARELLERIYRPGRPVRL 330
PRK02406 PRK02406
DNA polymerase IV; Validated
 45-217 1.35e-32

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 128.31  E-value: 1.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  45 IAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGINSV 124
Cdd:PRK02406  114 IAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLP-VEKIPGVGKVTAEKLHALGIYTC 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 125 HDLQTFPIKTLEKELGiAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKK-CSSEVEAKAKIEEL---LSSLLTRVcQ 200
Cdd:PRK02406  193 ADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEdLYDLEACLAELPRLaekLERRLERA-K 270

                         170
                  ....*....|....*..
gi 1907130013 201 DGRKPHTVRLVIrRYSD 217
Cdd:PRK02406  271 PDKRIKTVGVKL-KFAD 286
IMS_C pfam11799
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
 165-278 3.01e-08

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: 51.79  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 165 PQSFSEEDTF-KKCSSEVEAKAKIEELLSSLLTRVCQDGRKPHTVRLVIrRYSDKHcnRESRQCPIPSHViqklgtgnhD 243
Cdd:pfam11799   1 RKSIGAERTFgRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKI-RYSDFR--TITRSVTLPSPT---------D 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907130013 244 SMPPLIDILMKLFRNMVNvkmPFHLTLMSVCFCNL 278
Cdd:pfam11799  69 DTDEIYRAALRLLRRLYR---GRPVRLLGVSLSNL 100
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 545-573 6.30e-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: 34.51  E-value: 6.30e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907130013 545 LPFPPDIDPQVFYELPEEVQKELMAEWER 573
Cdd:cd19318     6 LPSFSQVDPSVLAALPPDLQEELEAAYAQ 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. ...
 38-277 7.94e-104

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: 318.26  E-value: 7.94e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  38 RLVVGSQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLI--HSLNHIKEIPGIGYKTAKR 115
Cdd:cd01703   108 RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPPSCADLMdfMDLHDLRKIPGIGYKTAAK 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 116 LEVLGINSVHDLQTFPI---------------KTLEKELGIAIAQRIQQLSFGEDKSPV-TPSGPPQSFSEEDTFKKCSS 179
Cdd:cd01703   188 LEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVkPASDFPQQISIEDSYKKCSL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 180 EV--EAKAKIEELLSSLLTRVCQ--------DGRKPHTVRLVIRRYSD--KHCNRESRQCPIPSHVIQKLGTGNHDSMPP 247
Cdd:cd01703   268 EEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTStkKHYNRESKQAPIPSHVFQKLTGGNEIAARP 347

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907130013 248 LIDILMKLFRNMVNVK--MPFHLTLMSVCFCN 277
Cdd:cd01703   348 IEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
PolY cd00424
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ...
 37-276 8.85e-68

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: 223.39  E-value: 8.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  37 RRLVVGSQIAAEMREAMYNQLG-LTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIhSLNHIKEIPGIGYKTAKR 115
Cdd:cd00424   110 RLLGLGSEVALRIKRHIAEQLGgITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFL-SKLPLTDLPGIGAVTAKR 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 116 LEVLGINSVHDLQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKKCSSEVE-AKAKIEELLSSL 194
Cdd:cd00424   189 LEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEdARPLLRLLLEKL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 195 LTRVCQDGRKPHTVRLVIRRYSD---KHCNRESRQCPIPSHViqklgtgnhdSMPPLIDILMKLFRNMVNVKMPFHLTLM 271
Cdd:cd00424   269 ARRLRRDGRGATRLRLWLRTVDGrwsGHADIPSRSAPRPIST----------EDGELLHALDKLWRALLDDKGPRRLRRL 338


                  ....*
gi 1907130013 272 SVCFC 276
Cdd:cd00424   339 GVRLS 343
PolY_Pol_IV_kappa cd03586
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ...
 42-237 2.78e-39

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: 146.51  E-value: 2.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  42 GSQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLnHIKEIPGIGYKTAKRLEVLGI 121
Cdd:cd03586   114 ATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPL-PVRKIPGVGKVTAEKLKELGI 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 122 NSVHDLQTFPIKTLEKELGiAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTF-KKCSSEVEAKAKIEELLSSLLTRVCQ 200
Cdd:cd03586   193 KTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFsEDLTDPEELLEELLELAEELAERLRK 271

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907130013 201 DGRKPHTVRLVIrRYSDKHCNRESRQCPIPSHVIQKL 237
Cdd:cd03586   272 RGLKGRTVTVKL-KYADFSTRTRSRTLPEPTDDAEDI 307
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 44-268 3.31e-39

Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];


Pssm-ID: 440158 [Multi-domain]  Cd Length: 336  Bit Score: 146.44  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLnHIKEIPGIGYKTAKRLEVLGINS 123
Cdd:COG0389   119 AIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPL-PVEKLWGVGPKTAEKLARLGIRT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 124 VHDLQTFPIKTLEKELGIAiAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKKcssEVEAKAKIEELLSSLLTRVC---- 199
Cdd:COG0389   198 IGDLAALPRAELRRRFGKV-GERLYRLARGIDPRPVEPRRPRKSIGVERTFGE---DLTDLEELEAALRRLAERLAerlr 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130013 200 QDGRKPHTVRLVIrRYSDKHCNRESRQCPIPShviqklgtgnhDSMPPLIDILMKLFRNMVNVKMPFHL 268
Cdd:COG0389   274 RQGLGARTVTVKL-RTSDFRTTTRSRTLPEPT-----------DDTAELLRAARELLERIYRPGRPVRL 330
PRK02406 PRK02406
DNA polymerase IV; Validated
 45-217 1.35e-32

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 128.31  E-value: 1.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  45 IAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGINSV 124
Cdd:PRK02406  114 IAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLP-VEKIPGVGKVTAEKLHALGIYTC 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 125 HDLQTFPIKTLEKELGiAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKK-CSSEVEAKAKIEEL---LSSLLTRVcQ 200
Cdd:PRK02406  193 ADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEdLYDLEACLAELPRLaekLERRLERA-K 270

                         170
                  ....*....|....*..
gi 1907130013 201 DGRKPHTVRLVIrRYSD 217
Cdd:PRK02406  271 PDKRIKTVGVKL-KFAD 286
PolY_Pol_eta cd01702
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ...
 41-277 2.06e-25

DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Unlike other Y-family members, Pol eta can efficiently and accurately replicate DNA past UV-induced lesions. Its activity is initiated by two simultaneous interactions: the PIP box in pol eta interacting with PCNA, and the UBZ (ubiquitin-binding zinc finger) in pol eta interacting with monoubiquitin attached to PCNA. Pol eta is more efficient in copying damaged DNA than undamaged DNA and seems to recognize when a lesion has been passed, facilitating a lesion-dependent dissociation from the DNA.


Pssm-ID: 176456 [Multi-domain]  Cd Length: 359  Bit Score: 107.78  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  41 VGSQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRL-EVL 119
Cdd:cd01702   124 LGSRIVEEIRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLP-ITSIRGLGGKLGEEIiDLL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 120 GINSVHDLQTFPIKT--LEKELGIAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTF--KKCSSEVEAKAKIEELLSSLL 195
Cdd:cd01702   203 GLPTEGDVAGFRSSEsdLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpgKTALSTEDVQHWLLVLASELN 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 196 TRVCQD----GRKPHTVRLVIRRYSDKhcNRESRQCPIPSHVIQKLgtgNHDSMppliDILMKLFRNMVNVKMPFHLTLM 271
Cdd:cd01702   283 SRLEDDryenNRRPKTLVLSLRQRGDG--VRRSRSCALPRYDAQKI---VKDAF----KLIKAINEEGLGLAWNYPLTLL 353


                  ....*.
gi 1907130013 272 SVCFCN 277
Cdd:cd01702   354 SLSFTK 359
PolY_Pol_V_umuC cd01700
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ...
 44-257 2.11e-21

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: 95.69  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQT----VLLPESCQHLIHSLNHIKEIPGIGYKTAKRLEVL 119
Cdd:cd01700   116 ELARKIRRRILQETGIPVTVGIGPTKTLAKLANDLAKKKNPYggvvDLTDEEVRDKLLKILPVGDVWGIGRRTAKKLNAM 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 120 GINSVHDLQTFPIKTLEKELGIaIAQRIQQLSFGEDKSPVTPSGPP-QSFseedtfkkCSSE-----VEAKAKIEELLSS 193
Cdd:cd01700   196 GIHTAGDLAQADPDLLRKKFGV-VGERLVRELNGIDCLPLEEYPPPkKSI--------GSSRsfgrdVTDLDELKQALAE 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907130013 194 LLTRVC----QDGRKPHTVRLVIRrysdkhCNRESRQCPIPSHViQKLGTGNHDSMppliDILMKLFR 257
Cdd:cd01700   267 YAERAAeklrRQKSVARTISVFIG------TSGFSRQPKYYSAT-NTLPYPTNDTR----EIVKAALR 323
PRK03348 PRK03348
DNA polymerase IV; Provisional
 44-215 1.64e-19

DNA polymerase IV; Provisional


Pssm-ID: 235118 [Multi-domain]  Cd Length: 454  Bit Score: 91.53  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGINS 123
Cdd:PRK03348  125 AFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLP-VRRLWGIGPVTEEKLHRLGIET 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 124 VHDLQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKK-CSSEVEAKAKIEELLSSLLTRVCQDG 202
Cdd:PRK03348  204 IGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVdLTTRAQLREAIERIAEHAHRRLLKDG 283

                         170
                  ....*....|...
gi 1907130013 203 RKPHTVRLVIRRY 215
Cdd:PRK03348  284 RGARTVTVKLRKS 296
PolY_Rev1 cd01701
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ...
 43-231 2.32e-16

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: 81.21  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  43 SQIAAEMREAmynqlglTGC---AGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVL 119
Cdd:cd01701   170 EAIRNEIRET-------TGCsasVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLK-VGDLPGVGSSLAEKLVKL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 120 GINSVHD--LQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDT----FKKcssEVEAKAKIEELLSS 193
Cdd:cd01701   242 FGDTCGGleLRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINygirFTN---VDDVEQFLQRLSEE 318

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907130013 194 LLTRVCQDGRKPHTVRLVIRRYSDKH------------CNRESRQCPIPS 231
Cdd:cd01701   319 LSKRLEESNVTGRQITLKLMKRAPGApieppkymghgiCDSFSKSSTLGV 368
PRK02794 PRK02794
DNA polymerase IV; Provisional
 40-174 8.91e-16

DNA polymerase IV; Provisional


Pssm-ID: 179473 [Multi-domain]  Cd Length: 419  Bit Score: 79.59  E-value: 8.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  40 VVGSQIAAEMREamynQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSlNHIKEIPGIGYKTAKRLEVL 119
Cdd:PRK02794  154 VVLARFARRVER----EIGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAP-KPVGIIWGVGPATAARLARD 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907130013 120 GINSVHDLQTFPIKTLEKELGiAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTF 174
Cdd:PRK02794  229 GIRTIGDLQRADEADLMRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTF 282
PRK01810 PRK01810
DNA polymerase IV; Validated
 45-217 4.30e-15

DNA polymerase IV; Validated


Pssm-ID: 179337 [Multi-domain]  Cd Length: 407  Bit Score: 77.38  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  45 IAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLnHIKEIPGIGYKTAKRLEVLGINSV 124
Cdd:PRK01810  125 IAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPL-PVGEMHGIGEKTAEKLKDIGIQTI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 125 HDLQTFPIKTLEKELGIAiAQRIQQLSFGEDKSPVTPS--------GPPQSFSEE--------DTFKKCSSEVEAKAKIE 188
Cdd:PRK01810  204 GDLAKADEHILRAKLGIN-GVRLQRRANGIDDRPVDPEaiyqfksvGNSTTLSHDmdeekellDVLRRLSKSVSKRLQKK 282

                         170       180
                  ....*....|....*....|....*....
gi 1907130013 189 ELLSSlltrvcqdgrkphTVRLVIrRYSD 217
Cdd:PRK01810  283 TVVSY-------------NVQIMI-RYHD 297
PRK01216 PRK01216
DNA polymerase IV; Validated
 44-161 1.14e-14

DNA polymerase IV; Validated


Pssm-ID: 179251 [Multi-domain]  Cd Length: 351  Bit Score: 75.60  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGINS 123
Cdd:PRK01216  123 NLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELD-IADIPGIGDITAEKLKKLGVNK 201

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907130013 124 VHDLQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPVTP 161
Cdd:PRK01216  202 LVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRA 239
PRK03352 PRK03352
DNA polymerase IV; Validated
 44-231 1.18e-14

DNA polymerase IV; Validated


Pssm-ID: 179564 [Multi-domain]  Cd Length: 346  Bit Score: 75.44  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGINS 123
Cdd:PRK03352  122 ALAEEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRP-TDALWGVGPKTAKRLAALGITT 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 124 VHDLQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPVTpSGP--PQSFSEEDTFKK---CSSEVEakAKIEELLSSLLTRV 198
Cdd:PRK03352  201 VADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVS-AEPwvPRSRSREVTFPQdltDRAEVE--SAVRELARRVLDEV 277

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907130013 199 CQDGRKPHTVRLVIrRYSDKHCNRESRQCPIPS 231
Cdd:PRK03352  278 VAEGRPVTRVAVKV-RTATFYTRTKIRKLPEPT 309
PRK03103 PRK03103
DNA polymerase IV; Reviewed
 44-232 1.29e-13

DNA polymerase IV; Reviewed


Pssm-ID: 235104 [Multi-domain]  Cd Length: 409  Bit Score: 72.73  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVF---KPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLG 120
Cdd:PRK03103  123 EIAQKIQQRIMRETGVYARVGIGPNKLLAKMACDNFakkNPDGLFTLDKEDVPADLWPLP-VRKLFGVGSRMEKHLRRMG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 121 INSVHDLQTFPIKTLEKELGIaIAQRIQQLSFGEDKSPVTPSGPP--QSFSEEDTFKKCSSEVEakaKIEELLSSLLTRV 198
Cdd:PRK03103  202 IRTIGQLANTPLERLKKRWGI-NGEVLWRTANGIDYSPVTPHSLDrqKAIGHQMTLPRDYRGFE---EIKVVLLELCEEV 277

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907130013 199 CQDGRKPH----TVRLVIRRYSDKHCNRESRQCPIPSH 232
Cdd:PRK03103  278 CRRARAKGymgrTVSVSLRGADFDWPTGFSRQMTLPEP 315
PRK03858 PRK03858
DNA polymerase IV; Validated
 43-159 8.76e-12

DNA polymerase IV; Validated


Pssm-ID: 179663 [Multi-domain]  Cd Length: 396  Bit Score: 66.93  E-value: 8.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  43 SQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGIN 122
Cdd:PRK03858  117 VQIAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLP-VRRLWGVGPVTAAKLRAHGIT 195

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907130013 123 SVHDLQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPV 159
Cdd:PRK03858  196 TVGDVAELPESALVSLLGPAAGRHLHALAHNRDPRRV 232
PRK14133 PRK14133
DNA polymerase IV; Provisional
 44-176 5.49e-11

DNA polymerase IV; Provisional


Pssm-ID: 184529 [Multi-domain]  Cd Length: 347  Bit Score: 64.35  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  44 QIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGINS 123
Cdd:PRK14133  118 KIAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLP-ISKVHGIGKKSVEKLNNIGIYT 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907130013 124 VHDLQTFPIKTLEK---ELGIAIAQRIQqlsfGEDKSPVTPSGPPQSFSEEDTFKK 176
Cdd:PRK14133  197 IEDLLKLSREFLIEyfgKFGVEIYERIR----GIDYREVEVSRERKSIGKETTLKK 248
IMS_C pfam11799
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
 165-278 3.01e-08

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: 51.79  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013 165 PQSFSEEDTF-KKCSSEVEAKAKIEELLSSLLTRVCQDGRKPHTVRLVIrRYSDKHcnRESRQCPIPSHViqklgtgnhD 243
Cdd:pfam11799   1 RKSIGAERTFgRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKI-RYSDFR--TITRSVTLPSPT---------D 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907130013 244 SMPPLIDILMKLFRNMVNvkmPFHLTLMSVCFCNL 278
Cdd:pfam11799  69 DTDEIYRAALRLLRRLYR---GRPVRLLGVSLSNL 100
IMS pfam00817
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
 43-76 3.46e-06

impB/mucB/samB family; These proteins are involved in UV protection (Swiss).


Pssm-ID: 425885 [Multi-domain]  Cd Length: 148  Bit Score: 46.80  E-value: 3.46e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907130013  43 SQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVS 76
Cdd:pfam00817 114 EALAKRLRREIAEETGLTCSIGIAPNKLLAKLAS 147
PTZ00205 PTZ00205
DNA polymerase kappa; Provisional
 45-127 4.23e-06

DNA polymerase kappa; Provisional


Pssm-ID: 140232 [Multi-domain]  Cd Length: 571  Bit Score: 49.63  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  45 IAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVL---LPESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGI 121
Cdd:PTZ00205  252 VASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLnlhTRGDVMTYVRDLG-LRSVPGVGKVTEALLKGLGI 330


                  ....*.
gi 1907130013 122 NSVHDL 127
Cdd:PTZ00205  331 TTLSDI 336
IMS_HHH pfam11798
IMS family HHH motif; These proteins are involved in UV protection, eg.
 89-121 1.00e-05

IMS family HHH motif; These proteins are involved in UV protection, eg.


Pssm-ID: 432081 [Multi-domain]  Cd Length: 32  Bit Score: 42.38  E-value: 1.00e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907130013  89 PESCQHLIHSLNhIKEIPGIGYKTAKRLEVLGI 121
Cdd:pfam11798   1 PDDVPEFLWPLP-ISKIPGIGKKLAEKLKALGI 32
umuC PRK03609
translesion error-prone DNA polymerase V subunit UmuC;
48-154 2.56e-05

translesion error-prone DNA polymerase V subunit UmuC;


Pssm-ID: 179607 [Multi-domain]  Cd Length: 422  Bit Score: 46.68  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  48 EMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKP-NQQT---VLL--PESCQHLIhSLNHIKEIPGIGYKTAKRLEVLGI 121
Cdd:PRK03609  122 EIRATVLQRTHLTVGVGIAQTKTLAKLANHAAKKwQRQTggvVDLsnLERQRKLL-SLQPVEEVWGVGRRISKKLNAMGI 200

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907130013 122 NSVHDLQTFPIKTLEKELGIAIAQRIQQLSfGE 154
Cdd:PRK03609  201 KTALDLADTNIRFIRKHFNVVLERTVRELR-GE 232
HHH_5 pfam14520
Helix-hairpin-helix domain;
104-147 6.31e-04

Helix-hairpin-helix domain;


Pssm-ID: 434010 [Multi-domain]  Cd Length: 57  Bit Score: 37.85  E-value: 6.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907130013 104 EIPGIGYKTAKRLEVLGINSVHDLQTFPIKTLEK--ELGIAIAQRI 147
Cdd:pfam14520   6 SISGIGPKTALALLSAGIGTVEDLAEADVDELAEipGIGEKTAQRI 51
PolY_like cd03468
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ...
 57-169 2.47e-03

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: 40.44  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130013  57 LGLTGCAGVAPNKLLAKLVSgvFKPNQQTVLLPESCQHLIHSLNH-IKEIPGIGYKTAKRLEVLGINSVHDLQTFPIKTL 135
Cdd:cd03468   128 LGLSARAGIADTPGAAWLLA--RAGGGRGVLRREALAAALVLLAPlPVAALRLPPETVELLARLGLRTLGDLAALPRAEL 205

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907130013 136 EKELGIAIAQRIQQLsFGEDKSPVTPSGPPQSFS 169
Cdd:cd03468   206 ARRFGLALLLRLDQA-YGRDPEPLLFSPPPPAFD 238
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 545-573 6.30e-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: 34.51  E-value: 6.30e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907130013 545 LPFPPDIDPQVFYELPEEVQKELMAEWER 573
Cdd:cd19318     6 LPSFSQVDPSVLAALPPDLQEELEAAYAQ 34
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
104-154 9.65e-03

DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 38.63  E-value: 9.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907130013 104 EIPGIGYKTAKRL-EVLGINSVHDlqtfpiktLEKElgiAIAQRIQQLS-FGE 154
Cdd:COG1796    95 RIPGLGPKKVKKLyEELGITSLEE--------LEAA---AEEGRIRELPgFGE 136
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
102-131 9.80e-03

RecG-like helicase [Replication, recombination and repair];


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 38.88  E-value: 9.80e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907130013 102 IKEIPGIGYKTAKRLEVLGINSVHDL-QTFP 131
Cdd:COG1200     8 LTYLKGVGPKRAKLLAKLGIRTVGDLlFHLP 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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