NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1192727316|ref|NP_001338549|]
View 

DNA polymerase iota isoform h [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 7-177 2.14e-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.


The actual alignment was detected with superfamily member cd01703:

Pssm-ID: 452909 [Multi-domain]  Cd Length: 379  Bit Score: 223.50  E-value: 2.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSP---------------KILEKELGISVAQRIQKLSFGEDNSPVI-LSGPPQSFSEE 70
Cdd:cd01703   180 IGYKTAAKLEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVKpASDFPQQISIE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  71 DSFKKCSSEV--EAKNKIEELLASLLNRVCQ--------DGRKPHTVRLIIRRYSSEKH-YGRESRQCPIPSHVIQKLGT 139
Cdd:cd01703   260 DSYKKCSLEEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTSTKKhYNRESKQAPIPSHVFQKLTG 339

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1192727316 140 GNYDVMTPMVDILMKLFRNMVNVK--MPFHLTLLSVCFCN 177
Cdd:cd01703   340 GNEIAARPIEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
Rev1_UBM2 super family cl41665
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 445-470 2.99e-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: 35.28  E-value: 2.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 1192727316 445 PSDIDPQVFYELPEAVQKELLAEWKR 470
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. ...
 7-177 2.14e-68

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: 223.50  E-value: 2.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSP---------------KILEKELGISVAQRIQKLSFGEDNSPVI-LSGPPQSFSEE 70
Cdd:cd01703   180 IGYKTAAKLEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVKpASDFPQQISIE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  71 DSFKKCSSEV--EAKNKIEELLASLLNRVCQ--------DGRKPHTVRLIIRRYSSEKH-YGRESRQCPIPSHVIQKLGT 139
Cdd:cd01703   260 DSYKKCSLEEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTSTKKhYNRESKQAPIPSHVFQKLTG 339

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1192727316 140 GNYDVMTPMVDILMKLFRNMVNVK--MPFHLTLLSVCFCN 177
Cdd:cd01703   340 GNEIAARPIEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 7-113 4.73e-14

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


Pssm-ID: 440158 [Multi-domain]  Cd Length: 336  Bit Score: 73.25  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKcssEVEAKNKI 86
Cdd:COG0389   182 VGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGE---DLTDLEEL 257

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1192727316  87 EELLASLLNRVC----QDGRKPHTVRLIIRR 113
Cdd:COG0389   258 EAALRRLAERLAerlrRQGLGARTVTVKLRT 288
PRK03352 PRK03352
DNA polymerase IV; Validated
 6-112 2.89e-07

DNA polymerase IV; Validated


Pssm-ID: 179564 [Multi-domain]  Cd Length: 346  Bit Score: 52.33  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   6 SIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVIlSGP--PQSFSEEDSFKK---CSSEV 80
Cdd:PRK03352  184 GVGPKTAKRLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVS-AEPwvPRSRSREVTFPQdltDRAEV 262

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1192727316  81 EAknKIEELLASLLNRVCQDGRKPHTVRLIIR 112
Cdd:PRK03352  263 ES--AVRELARRVLDEVVAEGRPVTRVAVKVR 292
IMS_C pfam11799
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
 64-178 6.78e-07

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: 47.55  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  64 PQSFSEEDSF-KKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYssekHYGRESRQCPIPSHviqklgTGNY 142
Cdd:pfam11799   1 RKSIGAERTFgRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIRYS----DFRTITRSVTLPSP------TDDT 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1192727316 143 DVMTpmvDILMKLFRNMVNvkmPFHLTLLSVCFCNL 178
Cdd:pfam11799  71 DEIY---RAALRLLRRLYR---GRPVRLLGVSLSNL 100
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 445-470 2.99e-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: 2.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 1192727316 445 PSDIDPQVFYELPEAVQKELLAEWKR 470
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. ...
 7-177 2.14e-68

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: 223.50  E-value: 2.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSP---------------KILEKELGISVAQRIQKLSFGEDNSPVI-LSGPPQSFSEE 70
Cdd:cd01703   180 IGYKTAAKLEAHGISSVRDLQEFSNrnrqtvgaapsllelLLMVKEFGEGIGQRIWKLLFGRDTSPVKpASDFPQQISIE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  71 DSFKKCSSEV--EAKNKIEELLASLLNRVCQ--------DGRKPHTVRLIIRRYSSEKH-YGRESRQCPIPSHVIQKLGT 139
Cdd:cd01703   260 DSYKKCSLEEirEARNKIEELLASLLERMKQdlqevkagDGRRPHTLRLTLRRYTSTKKhYNRESKQAPIPSHVFQKLTG 339

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1192727316 140 GNYDVMTPMVDILMKLFRNMVNVK--MPFHLTLLSVCFCN 177
Cdd:cd01703   340 GNEIAARPIEKILMRLFRELVPPKnvKGFNLTLLNVCFTN 379
PolY cd00424
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ...
 7-176 6.47e-46

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: 162.92  E-value: 6.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKCSSEVE-AKNK 85
Cdd:cd00424   181 IGAVTAKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEdARPL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  86 IEELLASLLNRVCQDGRKPHTVRLIIRRYSSE--KHYGRESRQCPIPSHViqklgtgnydVMTPMVDILMKLFRNMVNVK 163
Cdd:cd00424   261 LRLLLEKLARRLRRDGRGATRLRLWLRTVDGRwsGHADIPSRSAPRPIST----------EDGELLHALDKLWRALLDDK 330

                         170
                  ....*....|...
gi 1192727316 164 MPFHLTLLSVCFC 176
Cdd:cd00424   331 GPRRLRRLGVRLS 343
PolY_Pol_IV_kappa cd03586
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ...
 7-133 5.65e-15

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: 76.02  E-value: 5.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSF-KKCSSEVEAKNK 85
Cdd:cd03586   179 VGKVTAEKLKELGIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFsEDLTDPEELLEE 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1192727316  86 IEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHygreSRQCPIPSHV 133
Cdd:cd03586   258 LLELAEELAERLRKRGLKGRTVTVKLKYADFSTR----TRSRTLPEPT 301
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 7-113 4.73e-14

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


Pssm-ID: 440158 [Multi-domain]  Cd Length: 336  Bit Score: 73.25  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKcssEVEAKNKI 86
Cdd:COG0389   182 VGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGE---DLTDLEEL 257

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1192727316  87 EELLASLLNRVC----QDGRKPHTVRLIIRR 113
Cdd:COG0389   258 EAALRRLAERLAerlrRQGLGARTVTVKLRT 288
PRK03352 PRK03352
DNA polymerase IV; Validated
 6-112 2.89e-07

DNA polymerase IV; Validated


Pssm-ID: 179564 [Multi-domain]  Cd Length: 346  Bit Score: 52.33  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   6 SIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVIlSGP--PQSFSEEDSFKK---CSSEV 80
Cdd:PRK03352  184 GVGPKTAKRLAALGITTVADLAAADPAELAATFGPTTGPWLLLLARGGGDTEVS-AEPwvPRSRSREVTFPQdltDRAEV 262

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1192727316  81 EAknKIEELLASLLNRVCQDGRKPHTVRLIIR 112
Cdd:PRK03352  263 ES--AVRELARRVLDEVVAEGRPVTRVAVKVR 292
IMS_C pfam11799
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
 64-178 6.78e-07

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: 47.55  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  64 PQSFSEEDSF-KKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYssekHYGRESRQCPIPSHviqklgTGNY 142
Cdd:pfam11799   1 RKSIGAERTFgRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIRYS----DFRTITRSVTLPSP------TDDT 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1192727316 143 DVMTpmvDILMKLFRNMVNvkmPFHLTLLSVCFCNL 178
Cdd:pfam11799  71 DEIY---RAALRLLRRLYR---GRPVRLLGVSLSNL 100
PRK02406 PRK02406
DNA polymerase IV; Validated
 7-107 4.36e-06

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 48.58  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGiSVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKK-CSSEVEAKNK 85
Cdd:PRK02406  176 VGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEdLYDLEACLAE 254

                          90       100
                  ....*....|....*....|....*
gi 1192727316  86 IEEL---LASLLNRVcQDGRKPHTV 107
Cdd:PRK02406  255 LPRLaekLERRLERA-KPDKRIKTV 278
PolY_Pol_eta cd01702
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ...
 15-177 4.25e-05

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: 45.77  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  15 LEALGINSVRDLQTF--SPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSF--KKCSSEVEAKNKIEELL 90
Cdd:cd01702   199 IDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpgKTALSTEDVQHWLLVLA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316  91 ASLLNRVCQD----GRKPHTVRLiirRYSSEKHYGRESRQCPIPSHVIQKLgtgnydvMTPMVDILMKLFRNMVNVKMPF 166
Cdd:cd01702   279 SELNSRLEDDryenNRRPKTLVL---SLRQRGDGVRRSRSCALPRYDAQKI-------VKDAFKLIKAINEEGLGLAWNY 348

                         170
                  ....*....|.
gi 1192727316 167 HLTLLSVCFCN 177
Cdd:cd01702   349 PLTLLSLSFTK 359
PRK01810 PRK01810
DNA polymerase IV; Validated
 7-122 1.93e-03

DNA polymerase IV; Validated


Pssm-ID: 179337 [Multi-domain]  Cd Length: 407  Bit Score: 40.40  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192727316   7 IGYKTAKCLEALGINSVRDLQTFSPKILEKELGISvAQRIQKLSFGEDNSPVilsgPPQSFSEEDS------FKKCSSEV 80
Cdd:PRK01810  187 IGEKTAEKLKDIGIQTIGDLAKADEHILRAKLGIN-GVRLQRRANGIDDRPV----DPEAIYQFKSvgnsttLSHDMDEE 261

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1192727316  81 -EAKNKIEELLASLLNRVCQDGRKPHTVRLIIrRYSSEKHYGR 122
Cdd:PRK01810  262 kELLDVLRRLSKSVSKRLQKKTVVSYNVQIMI-RYHDRRTITR 303
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 445-470 2.99e-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: 2.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 1192727316 445 PSDIDPQVFYELPEAVQKELLAEWKR 470
Cdd:cd19318     9 FSQVDPSVLAALPPDLQEELEAAYAQ 34
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH