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Conserved domains on  [gi|966938977|ref|XP_014991919|]
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DNA polymerase eta isoform X2 [Macaca mulatta]

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 ...
 66-304 3.84e-116

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 cd01702:

Pssm-ID: 452909 [Multi-domain]  Cd Length: 359  Bit Score: 349.30  E-value: 3.84e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  66 LTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEI 145
Cdd:cd01702  122 LDLGSRIVEEIRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 146 LGVEYMGELTQF--TESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATrEQVQWWLLQLAQE 223
Cdd:cd01702  202 LGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFPGKTALST-EDVQHWLLVLASE 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 224 LEERLTKDRNDNDRVATQLAVSIRVQGDKrlSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCAT 303
Cdd:cd01702  281 LNSRLEDDRYENNRRPKTLVLSLRQRGDG--VRRSRSCALPRYDAQKIVKDAFKLIKAINEEGLGLAWNYPLTLLSLSFT 358


                 .
gi 966938977 304 K 304
Cdd:cd01702  359 K 359
zf_UBZ pfam18439
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA ...
 506-536 1.70e-11

Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA polymerase eta (EC:2.7.7.7). It is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. The UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a beta-beta-alpha fold.


:

Pssm-ID: 465769  Cd Length: 32  Bit Score: 58.68  E-value: 1.70e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 966938977  506 DQVPCEKCGSLVPVWDMPEHMDYHFALELQK 536
Cdd:pfam18439   1 DTYVCPRCGKEIPESELPEHEDWHFAKDLQR 31
 
Name Accession Description Interval E-value
PolY_Pol_eta cd01702
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ...
 66-304 3.84e-116

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: 349.30  E-value: 3.84e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  66 LTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEI 145
Cdd:cd01702  122 LDLGSRIVEEIRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 146 LGVEYMGELTQF--TESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATrEQVQWWLLQLAQE 223
Cdd:cd01702  202 LGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFPGKTALST-EDVQHWLLVLASE 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 224 LEERLTKDRNDNDRVATQLAVSIRVQGDKrlSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCAT 303
Cdd:cd01702  281 LNSRLEDDRYENNRRPKTLVLSLRQRGDG--VRRSRSCALPRYDAQKIVKDAFKLIKAINEEGLGLAWNYPLTLLSLSFT 358


                 .
gi 966938977 304 K 304
Cdd:cd01702  359 K 359
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 72-247 3.76e-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: 3.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLgASVIEILGVEYM 151
Cdd:COG0389  120 IARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKT-AEKLARLGIRTI 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 152 GELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKD 231
Cdd:COG0389  199 GDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFG--EDLTDLEELEAALRRLAERLAERLRRQ 275

                        170
                 ....*....|....*.
gi 966938977 232 RndndRVATQLAVSIR 247
Cdd:COG0389  276 G----LGARTVTVKLR 287
PRK02406 PRK02406
DNA polymerase IV; Validated
 72-247 5.32e-30

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 120.99  E-value: 5.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRnlG-GKLGASVIEILGVEY 150
Cdd:PRK02406 114 IAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIP--GvGKVTAEKLHALGIYT 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 151 MGELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTk 230
Cdd:PRK02406 192 CADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFA--EDLYDLEACLAELPRLAEKLERRLE- 267

                        170
                 ....*....|....*..
gi 966938977 231 dRNDNDRVATQLAVSIR 247
Cdd:PRK02406 268 -RAKPDKRIKTVGVKLK 283
zf_UBZ pfam18439
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA ...
 506-536 1.70e-11

Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA polymerase eta (EC:2.7.7.7). It is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. The UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a beta-beta-alpha fold.


Pssm-ID: 465769  Cd Length: 32  Bit Score: 58.68  E-value: 1.70e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 966938977  506 DQVPCEKCGSLVPVWDMPEHMDYHFALELQK 536
Cdd:pfam18439   1 DTYVCPRCGKEIPESELPEHEDWHFAKDLQR 31
IMS pfam00817
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
 50-103 7.27e-08

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


Pssm-ID: 425885 [Multi-domain]  Cd Length: 148  Bit Score: 51.81  E-value: 7.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966938977   50 WLDSLQLDnLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLAC 103
Cdd:pfam00817  95 SIDEAFLD-LTGLEKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLAS 147
 
Name Accession Description Interval E-value
PolY_Pol_eta cd01702
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ...
 66-304 3.84e-116

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: 349.30  E-value: 3.84e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  66 LTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEI 145
Cdd:cd01702  122 LDLGSRIVEEIRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 146 LGVEYMGELTQF--TESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATrEQVQWWLLQLAQE 223
Cdd:cd01702  202 LGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFPGKTALST-EDVQHWLLVLASE 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 224 LEERLTKDRNDNDRVATQLAVSIRVQGDKrlSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCAT 303
Cdd:cd01702  281 LNSRLEDDRYENNRRPKTLVLSLRQRGDG--VRRSRSCALPRYDAQKIVKDAFKLIKAINEEGLGLAWNYPLTLLSLSFT 358


                 .
gi 966938977 304 K 304
Cdd:cd01702  359 K 359
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 72-247 3.76e-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: 3.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLgASVIEILGVEYM 151
Cdd:COG0389  120 IARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKT-AEKLARLGIRTI 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 152 GELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKD 231
Cdd:COG0389  199 GDLAALPRAELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFG--EDLTDLEELEAALRRLAERLAERLRRQ 275

                        170
                 ....*....|....*.
gi 966938977 232 RndndRVATQLAVSIR 247
Cdd:COG0389  276 G----LGARTVTVKLR 287
PolY_Pol_IV_kappa cd03586
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ...
 72-247 4.61e-36

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: 137.65  E-value: 4.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEiLGVEYM 151
Cdd:cd03586  117 IAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKE-LGIKTI 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 152 GELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKD 231
Cdd:cd03586  196 GDLAKLDVELLKKLFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFS--EDLTDPEELLEELLELAEELAERLRKR 272

                        170
                 ....*....|....*.
gi 966938977 232 rndnDRVATQLAVSIR 247
Cdd:cd03586  273 ----GLKGRTVTVKLK 284
PRK02406 PRK02406
DNA polymerase IV; Validated
 72-247 5.32e-30

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 120.99  E-value: 5.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRnlG-GKLGASVIEILGVEY 150
Cdd:PRK02406 114 IAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIP--GvGKVTAEKLHALGIYT 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 151 MGELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTk 230
Cdd:PRK02406 192 CADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFA--EDLYDLEACLAELPRLAEKLERRLE- 267

                        170
                 ....*....|....*..
gi 966938977 231 dRNDNDRVATQLAVSIR 247
Cdd:PRK02406 268 -RAKPDKRIKTVGVKLK 283
PolY cd00424
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ...
 28-280 3.98e-25

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: 106.68  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  28 KFVSPVGKLTSPkgmrkqglfqwlDSLQLDnLTSPDLQLTVGAVIVEEMRAAI-ERETGFQCSAGISHNKVLAKLACGLN 106
Cdd:cd00424   87 EEVAPLVEVASI------------DELFLD-LTGSARLLGLGSEVALRIKRHIaEQLGGITASIGIASNKLLAKLAAKYA 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 107 KPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLgASVIEILGVEYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPV 186
Cdd:cd00424  154 KPDGLTILDPEDLPGFLSKLPLTDLPGIGAVT-AKRLEAVGINPIGDLLAASPDALLALWGGVSGERLWYALRGIDDEPL 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 187 KPRQLPKTIGCSKNFPGKtaLATREQVQWWLLQLAQELEERLTKDrndnDRVATQLAVSIR-VQGDKRLSSLRRCCALTR 265
Cdd:cd00424  233 SPPRPRKSFSHERVLPRD--SRNAEDARPLLRLLLEKLARRLRRD----GRGATRLRLWLRtVDGRWSGHADIPSRSAPR 306

                        250
                 ....*....|....*
gi 966938977 266 YdAHKMSHDAFTVIK 280
Cdd:cd00424  307 P-ISTEDGELLHALD 320
PolY_Rev1 cd01701
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ...
 58-248 1.73e-23

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: 102.78  E-value: 1.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  58 NLTSPDLQLTVGA-VIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGG 136
Cdd:cd01701  153 DITSLLEETYELPeELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGS 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 137 KLGASVIEILGV-EYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQW 215
Cdd:cd01701  233 SLAEKLVKLFGDtCGGLELRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYG--IRFTNVDDVEQ 310

                        170       180       190
                 ....*....|....*....|....*....|...
gi 966938977 216 WLLQLAQELEERLtkdrNDNDRVATQLAVSIRV 248
Cdd:cd01701  311 FLQRLSEELSKRL----EESNVTGRQITLKLMK 339
PolY_Pol_iota cd01703
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ...
 63-259 7.60e-21

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: 94.84  E-value: 7.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  63 DLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQT-LVSHGS--VPQLFSQMPIRKIRNLGGKLG 139
Cdd:cd01703  106 EMRLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTtLLPPSCadLMDFMDLHDLRKIPGIGYKTA 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 140 ASVIEIL------GVEYMGELTQFTESQ--------LQSHFGEKNGSWLYAMCRGIEHDPVKP-RQLPKTIGCSKNFPgK 204
Cdd:cd01703  186 AKLEAHGissvrdLQEFSNRNRQTVGAApsllelllMVKEFGEGIGQRIWKLLFGRDTSPVKPaSDFPQQISIEDSYK-K 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966938977 205 TALATREQVQWWLLQLAQELEERLTKDRNDND----RVATQLAVSIRVQGDKRLSSLRR 259
Cdd:cd01703  265 CSLEEIREARNKIEELLASLLERMKQDLQEVKagdgRRPHTLRLTLRRYTSTKKHYNRE 323
PRK03348 PRK03348
DNA polymerase IV; Provisional
 66-231 5.55e-20

DNA polymerase IV; Provisional


Pssm-ID: 235118 [Multi-domain]  Cd Length: 454  Bit Score: 93.08  E-value: 5.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  66 LTVGAV--IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLG----GKLg 139
Cdd:PRK03348 118 ASAEEVeaFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGpvteEKL- 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 140 asviEILGVEYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPgkTALATREQVQWWLLQ 219
Cdd:PRK03348 197 ----HRLGIETIGDLAALSEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFA--VDLTTRAQLREAIER 270

                        170
                 ....*....|..
gi 966938977 220 LAQELEERLTKD 231
Cdd:PRK03348 271 IAEHAHRRLLKD 282
PRK14133 PRK14133
DNA polymerase IV; Provisional
 72-232 1.64e-17

DNA polymerase IV; Provisional


Pssm-ID: 184529 [Multi-domain]  Cd Length: 347  Bit Score: 84.00  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEIlGVEYM 151
Cdd:PRK14133 119 IAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNI-GIYTI 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 152 GELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTalATREQVQWWLLQLAQELEERLTKD 231
Cdd:PRK14133 198 EDLLKLSREFLIEYFG-KFGVEIYERIRGIDYREVEVSRERKSIGKETTLKKDT--KDKEELKKYLKDFSNIISEELKKR 274


                 .
gi 966938977 232 R 232
Cdd:PRK14133 275 N 275
PRK03103 PRK03103
DNA polymerase IV; Reviewed
 72-196 6.76e-16

DNA polymerase IV; Reviewed


Pssm-ID: 235104 [Multi-domain]  Cd Length: 409  Bit Score: 80.05  E-value: 6.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGL---NKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASvIEILGV 148
Cdd:PRK03103 124 IAQKIQQRIMRETGVYARVGIGPNKLLAKMACDNfakKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKH-LRRMGI 202

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 966938977 149 EYMGELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLP--KTIG 196
Cdd:PRK03103 203 RTIGQLANTPLERLKKRWG-INGEVLWRTANGIDYSPVTPHSLDrqKAIG 251
PRK03352 PRK03352
DNA polymerase IV; Validated
 74-247 7.67e-16

DNA polymerase IV; Validated


Pssm-ID: 179564 [Multi-domain]  Cd Length: 346  Bit Score: 79.30  E-value: 7.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  74 EEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEiLGVEYMGE 153
Cdd:PRK03352 125 EEIRAAVLERTGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAA-LGITTVAD 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 154 LTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPV--KPRQlPKTIGCSKNFPgkTALATREQVQWWLLQLAQeleeRLTKD 231
Cdd:PRK03352 204 LAAADPAELAATFGPTTGPWLLLLARGGGDTEVsaEPWV-PRSRSREVTFP--QDLTDRAEVESAVRELAR----RVLDE 276

                        170
                 ....*....|....*.
gi 966938977 232 RNDNDRVATQLAVSIR 247
Cdd:PRK03352 277 VVAEGRPVTRVAVKVR 292
PolY_Pol_V_umuC cd01700
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ...
 72-247 3.24e-15

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: 77.20  E-value: 3.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQT-----LVSHGSVPQLFSQMPIRKIRNLGGKLGASvIEIL 146
Cdd:cd01700  117 LARKIRRRILQETGIPVTVGIGPTKTLAKLANDLAKKKNPYggvvdLTDEEVRDKLLKILPVGDVWGIGRRTAKK-LNAM 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 147 GVEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGI---EHDPVKPRQlpKTIGCSKNFPGK-TALATREQVqwwLLQLAQ 222
Cdd:cd01700  196 GIHTAGDLAQADPDLLRKKFG-VVGERLVRELNGIdclPLEEYPPPK--KSIGSSRSFGRDvTDLDELKQA---LAEYAE 269

                        170       180
                 ....*....|....*....|....*
gi 966938977 223 ELEERLtkdRNDNdRVATQLAVSIR 247
Cdd:cd01700  270 RAAEKL---RRQK-SVARTISVFIG 290
PRK01810 PRK01810
DNA polymerase IV; Validated
 72-232 2.43e-12

DNA polymerase IV; Validated


Pssm-ID: 179337 [Multi-domain]  Cd Length: 407  Bit Score: 68.90  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLgASVIEILGVEYM 151
Cdd:PRK01810 125 IAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKT-AEKLKDIGIQTI 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 152 GELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQLP--KTIGCSKNFPGKTalaTREQVQWWLL-QLAQELEERL 228
Cdd:PRK01810 204 GDLAKADEHILRAKLG-INGVRLQRRANGIDDRPVDPEAIYqfKSVGNSTTLSHDM---DEEKELLDVLrRLSKSVSKRL 279


                 ....
gi 966938977 229 TKDR 232
Cdd:PRK01810 280 QKKT 283
zf_UBZ pfam18439
Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA ...
 506-536 1.70e-11

Ubiquitin-Binding Zinc Finger; This is ubiquitin-binding zinc finger (UBZ) domain found in DNA polymerase eta (EC:2.7.7.7). It is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. The UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a beta-beta-alpha fold.


Pssm-ID: 465769  Cd Length: 32  Bit Score: 58.68  E-value: 1.70e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 966938977  506 DQVPCEKCGSLVPVWDMPEHMDYHFALELQK 536
Cdd:pfam18439   1 DTYVCPRCGKEIPESELPEHEDWHFAKDLQR 31
PRK02794 PRK02794
DNA polymerase IV; Provisional
 70-195 2.41e-11

DNA polymerase IV; Provisional


Pssm-ID: 179473 [Multi-domain]  Cd Length: 419  Bit Score: 65.72  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  70 AVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASvIEILGVE 149
Cdd:PRK02794 153 AVVLARFARRVEREIGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAAR-LARDGIR 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 966938977 150 YMGELTQFTESQLQSHFGEkNGSWLYAMCRGIEHDPVKPRQLPKTI 195
Cdd:PRK02794 232 TIGDLQRADEADLMRRFGS-MGLRLWRLARGIDDRKVSPDREAKSV 276
PRK01216 PRK01216
DNA polymerase IV; Validated
 75-189 2.05e-10

DNA polymerase IV; Validated


Pssm-ID: 179251 [Multi-domain]  Cd Length: 351  Bit Score: 62.50  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  75 EMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLgGKLGASVIEILGVEYMGEL 154
Cdd:PRK01216 127 EIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGI-GDITAEKLKKLGVNKLVDT 205

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966938977 155 TQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPR 189
Cdd:PRK01216 206 LRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRAR 240
IMS pfam00817
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
 50-103 7.27e-08

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


Pssm-ID: 425885 [Multi-domain]  Cd Length: 148  Bit Score: 51.81  E-value: 7.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966938977   50 WLDSLQLDnLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLAC 103
Cdd:pfam00817  95 SIDEAFLD-LTGLEKLFGAEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLAS 147
PRK03858 PRK03858
DNA polymerase IV; Validated
 72-232 5.53e-07

DNA polymerase IV; Validated


Pssm-ID: 179663 [Multi-domain]  Cd Length: 396  Bit Score: 51.91  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRNLGGKLGASVIEIlGVEYM 151
Cdd:PRK03858 119 IAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAH-GITTV 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 152 GELTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGcsknfpGKTAL----ATREQVQWWLLQLAQELEER 227
Cdd:PRK03858 198 GDVAELPESALVSLLGPAAGRHLHALAHNRDPRRVETGRRRRSVG------AQRALgrgpNSPAEVDAVVVALVDRVARR 271


                 ....*.
gi 966938977 228 L-TKDR 232
Cdd:PRK03858 272 MrAAGR 277
PolY_like cd03468
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ...
 45-271 5.62e-06

DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention.


Pssm-ID: 176458 [Multi-domain]  Cd Length: 335  Bit Score: 48.53  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  45 QGLFQWLD-SLQLDNLTSPD-LQLTVGAV---------IVEEMRAAIEReTGFQCSAGISHNKVLAKLACGLNKP---NR 110
Cdd:cd03468   79 QELALWLLrFTPLVALDGPDgLLLDVTGClhlfggedaLAASLRAALAT-LGLSARAGIADTPGAAWLLARAGGGrgvLR 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 111 QTlvSHGSVPQLFSQMPIRKIRnLGGKLGASvIEILGVEYMGELTQFTESQLQSHFGeKNGSWLYAMCRGIEHDPVKPRQ 190
Cdd:cd03468  158 RE--ALAAALVLLAPLPVAALR-LPPETVEL-LARLGLRTLGDLAALPRAELARRFG-LALLLRLDQAYGRDPEPLLFSP 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 191 LPktigcsKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDNDRVATQLAVSIRvQGDKRLSSLRRCCALTRYDAHK 270
Cdd:cd03468  233 PP------PAFDFRLELQLEEPIARGLLFPLRRLLEQLCAFLALRGLGARRLSLTLF-REDGRVTRVLVGLARPSRDDLP 305


                 .
gi 966938977 271 M 271
Cdd:cd03468  306 L 306
IMS_C pfam11799
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
 192-266 5.72e-06

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


Pssm-ID: 463354 [Multi-domain]  Cd Length: 104  Bit Score: 45.24  E-value: 5.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966938977  192 PKTIGCSKNFPgkTALATREQVQWWLLQLAQELEERLTKDRndndRVATQLAVSIRvqgDKRLSSLRRCCALTRY 266
Cdd:pfam11799   1 RKSIGAERTFG--RDLTDLEELREALLELAEELAERLRRQG----LVARTVTVKIR---YSDFRTITRSVTLPSP 66
PTZ00205 PTZ00205
DNA polymerase kappa; Provisional
 72-247 3.70e-04

DNA polymerase kappa; Provisional


Pssm-ID: 140232 [Multi-domain]  Cd Length: 571  Bit Score: 43.47  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977  72 IVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQ---TLVSHGSVPQLFSQMPIRKIRNLgGKLGASVIEILGV 148
Cdd:PTZ00205 252 VASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQhdlNLHTRGDVMTYVRDLGLRSVPGV-GKVTEALLKGLGI 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938977 149 EYMGELTQfTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLP------------KTIGCSKNFpgkTALATREQVQWW 216
Cdd:PTZ00205 331 TTLSDIYN-RRVELCYILHNNLFRFLLGASIGIMQWPDAATAANtencegatggqrKAISSERSF---TTPRTKEGLQEM 406

                        170       180       190
                 ....*....|....*....|....*....|.
gi 966938977 217 LLQLAQELEERLTKdrndNDRVATQLAVSIR 247
Cdd:PTZ00205 407 VDTVFNGAYEEMRK----SELMCRQISLTIR 433
 
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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