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Conserved domains on  [gi|30681747|ref|NP_172522|]
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DNA polymerase lambda (POLL) [Arabidopsis thaliana]

Protein Classification

type-X family DNA polymerase( domain architecture ID 10207094)

type-X family DNA polymerase which includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT)

EC:  2.7.7.7
Gene Ontology:  GO:0003887|GO:0003677

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
202-527 1.22e-118

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


:

Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 351.88  E-value: 1.22e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 202 RNITEIFGKLINIYRALGEDR-RSFSYYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDe 280
Cdd:cd00141   1 QEIADILEELADLLELLGGNPfRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 281 KVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKN--EDSLTHAQKLGLKYFDDIKTRIPRQEVQEMEQLLQRVGEETLP 358
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKaaGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 359 GVNIVCGGSYRRGKATCGDLDIVVTHPDGQShKGFLTKFVKRLKEMNFLREDLifsthseegtDSGVDTYFGLCTYPGQE 438
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL----------SKGDTKASGILKLPGGW 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 439 LRRRIDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThssSGNRgargtasLKLSTEKQVFDFLG 518
Cdd:cd00141 229 KGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV---DGER-------LPGETEEEIFEALG 298

                ....*....
gi 30681747 519 FPWLEPHER 527
Cdd:cd00141 299 LPYIEPELR 307
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
21-63 1.18e-03

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


The actual alignment was detected with superfamily member cd17711:

Pssm-ID: 469589  Cd Length: 81  Bit Score: 38.01  E-value: 1.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30681747  21 GMVVFMVEIGVQRRRLQI--WKQKLVQMGAVIEEDrVTKKVTHVL 63
Cdd:cd17711   1 GCVFFIADYPEQMGDQEIatWKKVIEEHGGEVVDE-YSPRVTHVI 44
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
202-527 1.22e-118

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 351.88  E-value: 1.22e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 202 RNITEIFGKLINIYRALGEDR-RSFSYYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDe 280
Cdd:cd00141   1 QEIADILEELADLLELLGGNPfRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 281 KVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKN--EDSLTHAQKLGLKYFDDIKTRIPRQEVQEMEQLLQRVGEETLP 358
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKaaGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 359 GVNIVCGGSYRRGKATCGDLDIVVTHPDGQShKGFLTKFVKRLKEMNFLREDLifsthseegtDSGVDTYFGLCTYPGQE 438
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL----------SKGDTKASGILKLPGGW 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 439 LRRRIDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThssSGNRgargtasLKLSTEKQVFDFLG 518
Cdd:cd00141 229 KGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV---DGER-------LPGETEEEIFEALG 298

                ....*....
gi 30681747 519 FPWLEPHER 527
Cdd:cd00141 299 LPYIEPELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
199-528 2.25e-113

DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases


Pssm-ID: 214688  Cd Length: 334  Bit Score: 339.34  E-value: 2.25e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    199 DLNRNITEIFGKLINIYRALGEDRRSFSYY-KAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFE 277
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKCSYFrKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    278 TDEKVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKN--EDSLTHAQKLGLKYFDDIKTRIPRQEVQEMEQLLQRVGEE 355
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKnkELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    356 TLPGVNIVCGGSYRRGKATCGDLDIVVTHPdgQSHKGFLTKFVKRLKEMNFLrEDLIFSTHSEEGTDSGVDTYFGLCTYP 435
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVLDLLLLESTF-EELQLPSIRVATLDHGQKKFMILKLSP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    436 GQELR-------------RRIDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGyRLDDTGLFPATHSSSgnrgargt 502
Cdd:smart00483 238 SREDKeksgkpdekgwkaRRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKF-KLMLDGHELYDKTKE-------- 308
                          330       340
                   ....*....|....*....|....*.
gi 30681747    503 ASLKLSTEKQVFDFLGFPWLEPHERN 528
Cdd:smart00483 309 KFLKVESEEDIFDHLGLPYIEPEERN 334
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
336-449 2.29e-40

DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain.


Pssm-ID: 464318  Cd Length: 110  Bit Score: 141.55  E-value: 2.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747   336 RIPRQEVQEMEQLLQRVGEETLPGVNIVCGGSYRRGKATCGDLDIVVTHPDGQSH---KGFLTKFVKRLKEMNFLREDLI 412
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSEselKGLLDRLVARLKKSGFLTDDLA 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 30681747   413 FsthseegtDSGVDTYFGLCTYPG-QELRRRIDFKVYP 449
Cdd:pfam14792  81 V--------DSGGSKWMGVCRLPGsERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
201-524 1.00e-31

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 128.77  E-value: 1.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 201 NRNITEIFGKLINIYRALGEDR-RSFSYYKAIPVIEKFPTRIESVDQ---LKHLPGIGKAMRDHIQEIVTTGKLSKLEHF 276
Cdd:COG1796   3 NKEIARILEEIADLLELKGENPfKIRAYRRAARAIENLPEDIEELVAegdLTEIPGIGKAIAAKIEELLETGRLEELEEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 277 --ETDEKVRTISlfgEVWGVGPATALKLYEK-GHRTLEDLK---NEDSL---------ThAQKL--GLKYFDDIKTRIPR 339
Cdd:COG1796  83 reEVPPGLLELL---RIPGLGPKKVKKLYEElGITSLEELEaaaEEGRIrelpgfgekT-EENIlkGIELLRKRGGRFLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 340 QEVQEM-EQLLQRVgeETLPGV-NIVCGGSYRRGKATCGDLDIVVTHPDGQshkgfltKFVKRLKEMNFLREDLifsths 417
Cdd:COG1796 159 GEALPLaEEILAYL--RALPGVeRVEVAGSLRRRKETVGDIDILVASDDPE-------AVMDAFVKLPEVKEVL------ 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 418 EEG-TDSGVDTYFGLctypgqelrrRIDFKVYPRDiySFG--LIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThsss 494
Cdd:COG1796 224 AKGdTKASVRLKSGL----------QVDLRVVPPE--SFGaaLQYFTGSKEHNVALRQLAKERGLKLNEYGLFDVG---- 287
                       330       340       350
                ....*....|....*....|....*....|
gi 30681747 495 GNRgargtasLKLSTEKQVFDFLGFPWLEP 524
Cdd:COG1796 288 GER-------IAGETEEEVYAALGLPYIPP 310
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
227-527 2.84e-05

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 46.87  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  227 YYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDEKVRTISLFgEVWGVGPATALKLY-EK 305
Cdd:PRK08609  30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVPEGLLPLL-KLPGLGGKKIAKLYkEL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  306 GHRTLEDLKNEDSLTHAQKL-------------GLKYFDDIKTRIP----RQEVQEMEQLLqrvgeETLPGV-NIVCGGS 367
Cdd:PRK08609 109 GVVDKESLKEACENGKVQALagfgkkteekileAVKELGKRPERLPiaqvLPIAQEIEEYL-----ATIDEIiRFSRAGS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  368 YRRGKATCGDLD--IVVTHPDGqshkgfltkfvkrlkemnfLREDLIFSTHSEEGTDSGvDTYFGLctypgqELRRR--- 442
Cdd:PRK08609 184 LRRARETVKDLDfiIATDEPEA-------------------VREQLLQLPNIVEVIAAG-DTKVSV------ELEYEyti 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  443 -IDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThsssgnrgargTASLK-LSTEKQVFDFLGFP 520
Cdd:PRK08609 238 sVDFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEYGVEQAD-----------TGEVKtFESEEAFFAHFGLP 306

                 ....*..
gi 30681747  521 WLEPHER 527
Cdd:PRK08609 307 FIPPEVR 313
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
21-63 1.18e-03

third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the third BRCT domain.


Pssm-ID: 349343  Cd Length: 81  Bit Score: 38.01  E-value: 1.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30681747  21 GMVVFMVEIGVQRRRLQI--WKQKLVQMGAVIEEDrVTKKVTHVL 63
Cdd:cd17711   1 GCVFFIADYPEQMGDQEIatWKKVIEEHGGEVVDE-YSPRVTHVI 44
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
202-527 1.22e-118

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 351.88  E-value: 1.22e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 202 RNITEIFGKLINIYRALGEDR-RSFSYYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDe 280
Cdd:cd00141   1 QEIADILEELADLLELLGGNPfRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 281 KVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKN--EDSLTHAQKLGLKYFDDIKTRIPRQEVQEMEQLLQRVGEETLP 358
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKaaGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 359 GVNIVCGGSYRRGKATCGDLDIVVTHPDGQShKGFLTKFVKRLKEMNFLREDLifsthseegtDSGVDTYFGLCTYPGQE 438
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL----------SKGDTKASGILKLPGGW 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 439 LRRRIDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThssSGNRgargtasLKLSTEKQVFDFLG 518
Cdd:cd00141 229 KGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV---DGER-------LPGETEEEIFEALG 298

                ....*....
gi 30681747 519 FPWLEPHER 527
Cdd:cd00141 299 LPYIEPELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
199-528 2.25e-113

DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases


Pssm-ID: 214688  Cd Length: 334  Bit Score: 339.34  E-value: 2.25e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    199 DLNRNITEIFGKLINIYRALGEDRRSFSYY-KAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFE 277
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKCSYFrKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    278 TDEKVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKN--EDSLTHAQKLGLKYFDDIKTRIPRQEVQEMEQLLQRVGEE 355
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKnkELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    356 TLPGVNIVCGGSYRRGKATCGDLDIVVTHPdgQSHKGFLTKFVKRLKEMNFLrEDLIFSTHSEEGTDSGVDTYFGLCTYP 435
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVLDLLLLESTF-EELQLPSIRVATLDHGQKKFMILKLSP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747    436 GQELR-------------RRIDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGyRLDDTGLFPATHSSSgnrgargt 502
Cdd:smart00483 238 SREDKeksgkpdekgwkaRRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKF-KLMLDGHELYDKTKE-------- 308
                          330       340
                   ....*....|....*....|....*.
gi 30681747    503 ASLKLSTEKQVFDFLGFPWLEPHERN 528
Cdd:smart00483 309 KFLKVESEEDIFDHLGLPYIEPEERN 334
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
336-449 2.29e-40

DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain.


Pssm-ID: 464318  Cd Length: 110  Bit Score: 141.55  E-value: 2.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747   336 RIPRQEVQEMEQLLQRVGEETLPGVNIVCGGSYRRGKATCGDLDIVVTHPDGQSH---KGFLTKFVKRLKEMNFLREDLI 412
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSEselKGLLDRLVARLKKSGFLTDDLA 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 30681747   413 FsthseegtDSGVDTYFGLCTYPG-QELRRRIDFKVYP 449
Cdd:pfam14792  81 V--------DSGGSKWMGVCRLPGsERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
201-524 1.00e-31

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 128.77  E-value: 1.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 201 NRNITEIFGKLINIYRALGEDR-RSFSYYKAIPVIEKFPTRIESVDQ---LKHLPGIGKAMRDHIQEIVTTGKLSKLEHF 276
Cdd:COG1796   3 NKEIARILEEIADLLELKGENPfKIRAYRRAARAIENLPEDIEELVAegdLTEIPGIGKAIAAKIEELLETGRLEELEEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 277 --ETDEKVRTISlfgEVWGVGPATALKLYEK-GHRTLEDLK---NEDSL---------ThAQKL--GLKYFDDIKTRIPR 339
Cdd:COG1796  83 reEVPPGLLELL---RIPGLGPKKVKKLYEElGITSLEELEaaaEEGRIrelpgfgekT-EENIlkGIELLRKRGGRFLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 340 QEVQEM-EQLLQRVgeETLPGV-NIVCGGSYRRGKATCGDLDIVVTHPDGQshkgfltKFVKRLKEMNFLREDLifsths 417
Cdd:COG1796 159 GEALPLaEEILAYL--RALPGVeRVEVAGSLRRRKETVGDIDILVASDDPE-------AVMDAFVKLPEVKEVL------ 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747 418 EEG-TDSGVDTYFGLctypgqelrrRIDFKVYPRDiySFG--LIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThsss 494
Cdd:COG1796 224 AKGdTKASVRLKSGL----------QVDLRVVPPE--SFGaaLQYFTGSKEHNVALRQLAKERGLKLNEYGLFDVG---- 287
                       330       340       350
                ....*....|....*....|....*....|
gi 30681747 495 GNRgargtasLKLSTEKQVFDFLGFPWLEP 524
Cdd:COG1796 288 GER-------IAGETEEEVYAALGLPYIPP 310
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
457-528 4.29e-19

DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the thumb domain.


Pssm-ID: 464317 [Multi-domain]  Cd Length: 63  Bit Score: 80.88  E-value: 4.29e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681747   457 LIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPathsssgnrgARGTASLKLSTEKQVFDFLGFPWLEPHERN 528
Cdd:pfam14791   2 LLYFTGSKEFNRDLRLLAKKKGLKLNEYGLFD----------LKDGELLEGETEEDIFEALGLPYIPPELRE 63
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
287-333 1.10e-17

Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto the 3-prime ends of DNA chains. There is a general polymerase fold consisting of three subdomains that have been likened to the fingers, palm, and thumb of a right hand. DNA_pol_lambd_f is the central three-helical region of DNA polymerase lambda referred to as the F and G helices of the fingers domain. Contacts with DNA involve this conserved helix-hairpin-helix motif in the fingers region which interacts with the primer strand. This motif is common to several DNA binding proteins and confers a sequence-independent interaction with the DNA backbone.


Pssm-ID: 463069 [Multi-domain]  Cd Length: 51  Bit Score: 76.72  E-value: 1.10e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30681747   287 LFGEVWGVGPATALKLYEKGHRTLEDLKNE--DSLTHAQKLGLKYFDDI 333
Cdd:pfam10391   2 LFTGIYGVGPTTARKWYAQGYRTLDDLREKktAKLTRQQQIGLKYYDDF 50
HHH_8 pfam14716
Helix-hairpin-helix domain;
201-266 9.62e-17

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 74.46  E-value: 9.62e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30681747   201 NRNITEIFGKLINIYRALGEDR-RSFSYYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVT 266
Cdd:pfam14716   1 NQEIADALEELADLLELKGEDPfRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
227-527 2.84e-05

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 46.87  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  227 YYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDEKVRTISLFgEVWGVGPATALKLY-EK 305
Cdd:PRK08609  30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVPEGLLPLL-KLPGLGGKKIAKLYkEL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  306 GHRTLEDLKNEDSLTHAQKL-------------GLKYFDDIKTRIP----RQEVQEMEQLLqrvgeETLPGV-NIVCGGS 367
Cdd:PRK08609 109 GVVDKESLKEACENGKVQALagfgkkteekileAVKELGKRPERLPiaqvLPIAQEIEEYL-----ATIDEIiRFSRAGS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  368 YRRGKATCGDLD--IVVTHPDGqshkgfltkfvkrlkemnfLREDLIFSTHSEEGTDSGvDTYFGLctypgqELRRR--- 442
Cdd:PRK08609 184 LRRARETVKDLDfiIATDEPEA-------------------VREQLLQLPNIVEVIAAG-DTKVSV------ELEYEyti 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681747  443 -IDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPAThsssgnrgargTASLK-LSTEKQVFDFLGFP 520
Cdd:PRK08609 238 sVDFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEYGVEQAD-----------TGEVKtFESEEAFFAHFGLP 306

                 ....*..
gi 30681747  521 WLEPHER 527
Cdd:PRK08609 307 FIPPEVR 313
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
345-413 1.43e-04

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 40.86  E-value: 1.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681747   345 MEQLLQRVGEEtLPGVNIVCGGSYRRGKATCG-DLDIVVTHPDGQSHKGFLT--KFVKRLKEMNFLREDLIF 413
Cdd:pfam01909   1 LRKLREILKEL-FPVAEVVLFGSYARGTALPGsDIDLLVVFPEPVEEERLLKlaKIIKELEELLGLEVDLVT 71
HHH_5 pfam14520
Helix-hairpin-helix domain;
293-328 4.21e-04

Helix-hairpin-helix domain;


Pssm-ID: 434010 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 4.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 30681747   293 GVGPATALKLYEKGHRTLEDLKNED--SLTHAQKLGLK 328
Cdd:pfam14520   9 GIGPKTALALLSAGIGTVEDLAEADvdELAEIPGIGEK 46
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
21-63 1.18e-03

third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the third BRCT domain.


Pssm-ID: 349343  Cd Length: 81  Bit Score: 38.01  E-value: 1.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30681747  21 GMVVFMVEIGVQRRRLQI--WKQKLVQMGAVIEEDrVTKKVTHVL 63
Cdd:cd17711   1 GCVFFIADYPEQMGDQEIatWKKVIEEHGGEVVDE-YSPRVTHVI 44
 
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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