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Conserved domains on  [gi|625203950|ref|XP_007643451|]
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DNA-directed DNA/RNA polymerase mu isoform X2 [Cricetulus griseus]

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 ...
 85-421 4.14e-115

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: 338.79  E-value: 4.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950  85 LSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQLQGLPHFGEHSSRVIQELLEHGACEEVERVRCsERH 163
Cdd:cd00141    3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRE-DVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 164 QTMKLFTQIFGVGVKTANRWYQEGLRTLDELREQPQ-RLTQQQKAGLQYYQDLSTPVGRADAEALQQLVEAAVRQTLPGA 242
Cdd:cd00141   82 PGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 243 TVTLTGGFRRGKSQGHDVDFLITHPeEGQEVGLLPKVMRHLQSQGLVLYhqhhrshldsthllrqnYTMDAFERSFCILC 322
Cdd:cd00141  162 QVEIAGSYRRGKETVGDIDILVTHP-DATSRGLLEKVVDALVELGFVTE-----------------VLSKGDTKASGILK 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 323 LPQpphaalggtlhpcpTWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSrQEKGLWLNSHGLFDPEQKTFFHAT 402
Cdd:cd00141  224 LPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDGERLPGE 288

                        330
                 ....*....|....*....
gi 625203950 403 SEEDIFRLLGLKYLPPEQR 421
Cdd:cd00141  289 TEEEIFEALGLPYIEPELR 307
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 1-52 1.59e-16

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 cd18442:

Pssm-ID: 469589  Cd Length: 98  Bit Score: 74.50  E-value: 1.59e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 625203950   1 MEQTSAKEAICWQ-KDMGAHLPGCPQPILLDISWFTESMAAGQPVPEEVRHRL 52
Cdd:cd18442   46 SEQNSAEEVVSWLeRQMAAAPPACTPPALLDISWFTESMGAGQPVPVECRHRL 98
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 85-421 4.14e-115

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: 338.79  E-value: 4.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950  85 LSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQLQGLPHFGEHSSRVIQELLEHGACEEVERVRCsERH 163
Cdd:cd00141    3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRE-DVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 164 QTMKLFTQIFGVGVKTANRWYQEGLRTLDELREQPQ-RLTQQQKAGLQYYQDLSTPVGRADAEALQQLVEAAVRQTLPGA 242
Cdd:cd00141   82 PGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 243 TVTLTGGFRRGKSQGHDVDFLITHPeEGQEVGLLPKVMRHLQSQGLVLYhqhhrshldsthllrqnYTMDAFERSFCILC 322
Cdd:cd00141  162 QVEIAGSYRRGKETVGDIDILVTHP-DATSRGLLEKVVDALVELGFVTE-----------------VLSKGDTKASGILK 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 323 LPQpphaalggtlhpcpTWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSrQEKGLWLNSHGLFDPEQKTFFHAT 402
Cdd:cd00141  224 LPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDGERLPGE 288

                        330
                 ....*....|....*....
gi 625203950 403 SEEDIFRLLGLKYLPPEQR 421
Cdd:cd00141  289 TEEEIFEALGLPYIEPELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 81-422 5.30e-105

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 314.31  E-value: 5.30e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950    81 HNVILSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQLQGLPHFGEHSSRVIQELLEHGACEEVERVRC 159
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEILN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950   160 SERHQTMKLFTQIFGVGVKTANRWYQEGLRTLDELREQPQ-RLTQQQKAGLQYYQDLSTPVGRADAEALQQLVEAAVRQT 238
Cdd:smart00483  82 DEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKElKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRKI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950   239 LPGATVTLTGGFRRGKSQGHDVDFLITHPeeGQEVGLLPKVMrhlqsqglvlyhqhHRSHLDSTHLLRQNY-----TMDA 313
Cdd:smart00483 162 LPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVL--------------DLLLLESTFEELQLPsirvaTLDH 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950   314 FERSFCILCLPQPPHAALGGTLHPCPTWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSRQEKGLWLNSHGLFDP 393
Cdd:smart00483 226 GQKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDK 305

                          330       340
                   ....*....|....*....|....*....
gi 625203950   394 EQKTFFHATSEEDIFRLLGLKYLPPEQRN 422
Cdd:smart00483 306 TKEKFLKVESEEDIFDHLGLPYIEPEERN 334
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
81-421 2.81e-28

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 116.83  E-value: 2.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950  81 HNVILSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQ---LQGLPHFGEHSSRVIQELLEHGACEEVER 156
Cdd:COG1796    2 DNKEIARILEEIADLLELKGeNPFKIRAYRRAARAIENLPEDIEELVAegdLTEIPGIGKAIAAKIEELLETGRLEELEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 157 VRcSERHQTMKLFTQIFGVGVKTANRWYQE-GLRTLDELRE--QPQRL---------TQQQ-KAGLQYYQDLSTPVGRAD 223
Cdd:COG1796   82 LR-EEVPPGLLELLRIPGLGPKKVKKLYEElGITSLEELEAaaEEGRIrelpgfgekTEENiLKGIELLRKRGGRFLLGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 224 AEALQQLVEAAVRQtLPG-ATVTLTGGFRRGKSQGHDVDFLITHPEEgqevgllPKVMRHLQSQGLVlyhqhhrshldsT 302
Cdd:COG1796  161 ALPLAEEILAYLRA-LPGvERVEVAGSLRRRKETVGDIDILVASDDP-------EAVMDAFVKLPEV------------K 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 303 HLLRQNYTmdafeRSFCILclpqpphaalggtlhpcptWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSrQEKG 382
Cdd:COG1796  221 EVLAKGDT-----KASVRL-------------------KSGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLA-KERG 275

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 625203950 383 LWLNSHGLFDP--EQKTFfhaTSEEDIFRLLGLKYLPPEQR 421
Cdd:COG1796  276 LKLNEYGLFDVggERIAG---ETEEEVYAALGLPYIPPELR 313
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 359-422 4.27e-24

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: 94.36  E-value: 4.27e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625203950  359 ALLGWTGSQLFERELRRFSRQeKGLWLNSHGLFDPEQKTFFHATSEEDIFRLLGLKYLPPEQRN 422
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLAKK-KGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 1-52 1.59e-16

BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; Polymerase Mu (EC 2.7.7.7), also termed Pol mu, or terminal transferase, is a Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). It participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. Polymerase Mu contains a BRCT domain.


Pssm-ID: 349395  Cd Length: 98  Bit Score: 74.50  E-value: 1.59e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 625203950   1 MEQTSAKEAICWQ-KDMGAHLPGCPQPILLDISWFTESMAAGQPVPEEVRHRL 52
Cdd:cd18442   46 SEQNSAEEVVSWLeRQMAAAPPACTPPALLDISWFTESMGAGQPVPVECRHRL 98
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 85-421 4.14e-115

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: 338.79  E-value: 4.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950  85 LSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQLQGLPHFGEHSSRVIQELLEHGACEEVERVRCsERH 163
Cdd:cd00141    3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRE-DVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 164 QTMKLFTQIFGVGVKTANRWYQEGLRTLDELREQPQ-RLTQQQKAGLQYYQDLSTPVGRADAEALQQLVEAAVRQTLPGA 242
Cdd:cd00141   82 PGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 243 TVTLTGGFRRGKSQGHDVDFLITHPeEGQEVGLLPKVMRHLQSQGLVLYhqhhrshldsthllrqnYTMDAFERSFCILC 322
Cdd:cd00141  162 QVEIAGSYRRGKETVGDIDILVTHP-DATSRGLLEKVVDALVELGFVTE-----------------VLSKGDTKASGILK 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 323 LPQpphaalggtlhpcpTWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSrQEKGLWLNSHGLFDPEQKTFFHAT 402
Cdd:cd00141  224 LPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDGERLPGE 288

                        330
                 ....*....|....*....
gi 625203950 403 SEEDIFRLLGLKYLPPEQR 421
Cdd:cd00141  289 TEEEIFEALGLPYIEPELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 81-422 5.30e-105

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 314.31  E-value: 5.30e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950    81 HNVILSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQLQGLPHFGEHSSRVIQELLEHGACEEVERVRC 159
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEILN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950   160 SERHQTMKLFTQIFGVGVKTANRWYQEGLRTLDELREQPQ-RLTQQQKAGLQYYQDLSTPVGRADAEALQQLVEAAVRQT 238
Cdd:smart00483  82 DEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKElKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRKI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950   239 LPGATVTLTGGFRRGKSQGHDVDFLITHPeeGQEVGLLPKVMrhlqsqglvlyhqhHRSHLDSTHLLRQNY-----TMDA 313
Cdd:smart00483 162 LPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVL--------------DLLLLESTFEELQLPsirvaTLDH 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950   314 FERSFCILCLPQPPHAALGGTLHPCPTWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSRQEKGLWLNSHGLFDP 393
Cdd:smart00483 226 GQKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDK 305

                          330       340
                   ....*....|....*....|....*....
gi 625203950   394 EQKTFFHATSEEDIFRLLGLKYLPPEQRN 422
Cdd:smart00483 306 TKEKFLKVESEEDIFDHLGLPYIEPEERN 334
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
81-421 2.81e-28

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 116.83  E-value: 2.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950  81 HNVILSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQ---LQGLPHFGEHSSRVIQELLEHGACEEVER 156
Cdd:COG1796    2 DNKEIARILEEIADLLELKGeNPFKIRAYRRAARAIENLPEDIEELVAegdLTEIPGIGKAIAAKIEELLETGRLEELEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 157 VRcSERHQTMKLFTQIFGVGVKTANRWYQE-GLRTLDELRE--QPQRL---------TQQQ-KAGLQYYQDLSTPVGRAD 223
Cdd:COG1796   82 LR-EEVPPGLLELLRIPGLGPKKVKKLYEElGITSLEELEAaaEEGRIrelpgfgekTEENiLKGIELLRKRGGRFLLGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 224 AEALQQLVEAAVRQtLPG-ATVTLTGGFRRGKSQGHDVDFLITHPEEgqevgllPKVMRHLQSQGLVlyhqhhrshldsT 302
Cdd:COG1796  161 ALPLAEEILAYLRA-LPGvERVEVAGSLRRRKETVGDIDILVASDDP-------EAVMDAFVKLPEV------------K 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625203950 303 HLLRQNYTmdafeRSFCILclpqpphaalggtlhpcptWKAVRVDLVVTPNSQFPFALLGWTGSQLFERELRRFSrQEKG 382
Cdd:COG1796  221 EVLAKGDT-----KASVRL-------------------KSGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLA-KERG 275

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 625203950 383 LWLNSHGLFDP--EQKTFfhaTSEEDIFRLLGLKYLPPEQR 421
Cdd:COG1796  276 LKLNEYGLFDVggERIAG---ETEEEVYAALGLPYIPPELR 313
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 359-422 4.27e-24

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: 94.36  E-value: 4.27e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625203950  359 ALLGWTGSQLFERELRRFSRQeKGLWLNSHGLFDPEQKTFFHATSEEDIFRLLGLKYLPPEQRN 422
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLAKK-KGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
 167-216 8.29e-19

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: 79.42  E-value: 8.29e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 625203950  167 KLFTQIFGVGVKTANRWYQEGLRTLDELRE-QPQRLTQQQKAGLQYYQDLS 216
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREkKTAKLTRQQQIGLKYYDDFN 51
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 1-52 1.59e-16

BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; Polymerase Mu (EC 2.7.7.7), also termed Pol mu, or terminal transferase, is a Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). It participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. Polymerase Mu contains a BRCT domain.


Pssm-ID: 349395  Cd Length: 98  Bit Score: 74.50  E-value: 1.59e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 625203950   1 MEQTSAKEAICWQ-KDMGAHLPGCPQPILLDISWFTESMAAGQPVPEEVRHRL 52
Cdd:cd18442   46 SEQNSAEEVVSWLeRQMAAAPPACTPPALLDISWFTESMGAGQPVPVECRHRL 98
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 221-289 3.60e-13

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: 65.28  E-value: 3.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 625203950  221 RADAEALQQLVEAAVRQTLPGATVTLTGGFRRGKSQGHDVDFLITHPE---EGQEVGLLPKVMRHLQSQGLV 289
Cdd:pfam14792   4 REEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDgtsESELKGLLDRLVARLKKSGFL 75
HHH_8 pfam14716
Helix-hairpin-helix domain;
82-147 4.55e-13

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 63.68  E-value: 4.55e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 625203950   82 NVILSEALETLAEAAGFEG-NEGRLLSFYRAASVLKSLPCPVTSLSQLQGLPHFGEHSSRVIQELLE 147
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
BRCT_polymerase_mu_like cd17713
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu), DNA ...
 1-44 6.70e-11

BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu), DNA nucleotidylexotransferase and similar proteins; The family includes DNA-directed DNA/RNA polymerase mu (polymerase mu) and DNA nucleotidylexotransferase. Polymerase mu (EC 2.7.7.7), also termed Pol mu, or terminal transferase, is a Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). It participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. DNA nucleotidylexotransferase (EC 2.7.7.31), also termed terminal addition enzyme, or terminal deoxynucleotidyltransferase, or terminal transferase, is a template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. It is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. All family members contains a BRCT domain.


Pssm-ID: 349345  Cd Length: 87  Bit Score: 58.17  E-value: 6.70e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 625203950   1 MEQTSAKEAICWQKDMGahLPGCPQPILLDISWFTESMAAGQPV 44
Cdd:cd17713   46 AENNSAEEVLEWLERQK--LQGSSSPELLDISWFTESMGAGKPV 87
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 2-52 1.65e-08

BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), also termed terminal addition enzyme, or terminal deoxynucleotidyltransferase, or terminal transferase, is a template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. It is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. DNA nucleotidylexotransferase contains a BRCT domain.


Pssm-ID: 349396  Cd Length: 95  Bit Score: 51.73  E-value: 1.65e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 625203950   2 EQTSAKEAICWQkdMGAHLPGCPQPILLDISWFTESMAAGQPVPEEVRHRL 52
Cdd:cd18443   47 ENNSGAEVLEWL--QGQKLRDSSRLELLDISWFTECMGAGKPVEIEKRHRL 95
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 234-276 1.05e-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: 1.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 625203950  234 AVRQTLPGATVTLTGGFRRGK-SQGHDVDFLITHPEEGQEVGLL 276
Cdd:pfam01909   7 ILKELFPVAEVVLFGSYARGTaLPGSDIDLLVVFPEPVEEERLL 50
 
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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