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Conserved domains on  [gi|1381931185|ref|NP_001349612|]
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DNA-directed DNA/RNA polymerase mu isoform 4 [Homo sapiens]

Protein Classification

BRCT_polymerase_mu and NT_POLXc domain-containing protein( domain architecture ID 13035154)

BRCT_polymerase_mu and NT_POLXc domain-containing protein

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 ...
 156-467 3.71e-94

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: 291.02  E-value: 3.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRsERY 234
Cdd:cd00141     3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRE-DVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 235 QTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQ-KLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGA 313
Cdd:cd00141    82 PGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 314 TVTLTGGFRRGKLQGHDVDFLITHPkEGQEAGLLPRVMCRLQDQGLILYhqhqhsccesptrlaqqSHMDAFERSFCIFR 393
Cdd:cd00141   162 QVEIAGSYRRGKETVGDIDILVTHP-DATSRGLLEKVVDALVELGFVTE-----------------VLSKGDTKASGILK 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1381931185 394 LPQppgaavggstrpcpSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 467
Cdd:cd00141   224 LPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDG 282
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 26-123 1.64e-56

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: 185.05  E-value: 1.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442     1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                          90
                  ....*....|....*...
gi 1381931185 106 TESLGAGQPVPVECRHRL 123
Cdd:cd18442    81 TESMGAGQPVPVECRHRL 98
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 156-467 3.71e-94

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: 291.02  E-value: 3.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRsERY 234
Cdd:cd00141     3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRE-DVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 235 QTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQ-KLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGA 313
Cdd:cd00141    82 PGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 314 TVTLTGGFRRGKLQGHDVDFLITHPkEGQEAGLLPRVMCRLQDQGLILYhqhqhsccesptrlaqqSHMDAFERSFCIFR 393
Cdd:cd00141   162 QVEIAGSYRRGKETVGDIDILVTHP-DATSRGLLEKVVDALVELGFVTE-----------------VLSKGDTKASGILK 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1381931185 394 LPQppgaavggstrpcpSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 467
Cdd:cd00141   224 LPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDG 282
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 152-463 8.50e-84

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 265.00  E-value: 8.50e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  152 HNTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRR 230
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEILN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  231 SERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQ-KLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQA 309
Cdd:smart00483  82 DEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKElKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRKI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  310 LPGATVTLTGGFRRGKLQGHDVDFLITHPkeGQEAGLLPRVMCRLQ----DQGLILYhqhqhsccesptrLAQQSHMDAF 385
Cdd:smart00483 162 LPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVLDLLLlestFEELQLP-------------SIRVATLDHG 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1381931185  386 ERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFD 463
Cdd:smart00483 227 QKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYD 304
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 26-123 1.64e-56

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: 185.05  E-value: 1.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442     1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                          90
                  ....*....|....*...
gi 1381931185 106 TESLGAGQPVPVECRHRL 123
Cdd:cd18442    81 TESMGAGQPVPVECRHRL 98
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
 238-287 1.86e-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: 81.73  E-value: 1.86e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1381931185 238 KLFTQIFGVGVKTADRWYREGLRTLDDLRE-QPQKLTQQQKAGLQHHQDLS 287
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREkKTAKLTRQQQIGLKYYDDFN 51
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
181-463 1.71e-16

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 82.55  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 181 RAASVLKALPSPVTTLSQ---LQGLPHFGEHSSRVVQELLEHGVCEEVERVRRS------EryqtmklFTQIFGVGVKTA 251
Cdd:COG1796    32 RAARAIENLPEDIEELVAegdLTEIPGIGKAIAAKIEELLETGRLEELEELREEvppgllE-------LLRIPGLGPKKV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 252 DRWYRE-GLRTLDDLRE-----QPQKL------TQQQ-KAGLQHHQDLSTPVLRSDVDALQQVVEEAVgQALPG-ATVTL 317
Cdd:COG1796   105 KKLYEElGITSLEELEAaaeegRIRELpgfgekTEENiLKGIELLRKRGGRFLLGEALPLAEEILAYL-RALPGvERVEV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 318 TGGFRRGKLQGHDVDFLIThpkegqeagllprvmcrlqdqglilyhqhqhscCESPTRLaqqshMDAFERsfcifrlpQP 397
Cdd:COG1796   184 AGSLRRRKETVGDIDILVA---------------------------------SDDPEAV-----MDAFVK--------LP 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381931185 398 PGAAV--GGSTrpcpswKA-------VRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFD 463
Cdd:COG1796   218 EVKEVlaKGDT------KAsvrlksgLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLA-KERGLKLNEYGLFD 285
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 156-467 3.71e-94

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: 291.02  E-value: 3.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRsERY 234
Cdd:cd00141     3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRE-DVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 235 QTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQ-KLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGA 313
Cdd:cd00141    82 PGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 314 TVTLTGGFRRGKLQGHDVDFLITHPkEGQEAGLLPRVMCRLQDQGLILYhqhqhsccesptrlaqqSHMDAFERSFCIFR 393
Cdd:cd00141   162 QVEIAGSYRRGKETVGDIDILVTHP-DATSRGLLEKVVDALVELGFVTE-----------------VLSKGDTKASGILK 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1381931185 394 LPQppgaavggstrpcpSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 467
Cdd:cd00141   224 LPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDG 282
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 152-463 8.50e-84

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 265.00  E-value: 8.50e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  152 HNTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRR 230
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEILN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  231 SERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQ-KLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQA 309
Cdd:smart00483  82 DEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKElKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRKI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  310 LPGATVTLTGGFRRGKLQGHDVDFLITHPkeGQEAGLLPRVMCRLQ----DQGLILYhqhqhsccesptrLAQQSHMDAF 385
Cdd:smart00483 162 LPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVLDLLLlestFEELQLP-------------SIRVATLDHG 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1381931185  386 ERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFD 463
Cdd:smart00483 227 QKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYD 304
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 26-123 1.64e-56

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: 185.05  E-value: 1.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442     1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                          90
                  ....*....|....*...
gi 1381931185 106 TESLGAGQPVPVECRHRL 123
Cdd:cd18442    81 TESMGAGQPVPVECRHRL 98
BRCT_polymerase_mu_like cd17713
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu), DNA ...
 26-115 2.15e-44

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: 152.55  E-value: 2.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAappGCTPPALLDISWL 105
Cdd:cd17713     1 KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQ---GSSSPELLDISWF 77

                          90
                  ....*....|
gi 1381931185 106 TESLGAGQPV 115
Cdd:cd17713    78 TESMGAGKPV 87
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 26-123 2.47e-28

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: 108.74  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSW-QERRMAAAPpgctPPALLDISW 104
Cdd:cd18443     1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWlQGQKLRDSS----RLELLDISW 76

                          90
                  ....*....|....*....
gi 1381931185 105 LTESLGAGQPVPVECRHRL 123
Cdd:cd18443    77 FTECMGAGKPVEIEKRHRL 95
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
 238-287 1.86e-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: 81.73  E-value: 1.86e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1381931185 238 KLFTQIFGVGVKTADRWYREGLRTLDDLRE-QPQKLTQQQKAGLQHHQDLS 287
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREkKTAKLTRQQQIGLKYYDDFN 51
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
181-463 1.71e-16

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 82.55  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 181 RAASVLKALPSPVTTLSQ---LQGLPHFGEHSSRVVQELLEHGVCEEVERVRRS------EryqtmklFTQIFGVGVKTA 251
Cdd:COG1796    32 RAARAIENLPEDIEELVAegdLTEIPGIGKAIAAKIEELLETGRLEELEELREEvppgllE-------LLRIPGLGPKKV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 252 DRWYRE-GLRTLDDLRE-----QPQKL------TQQQ-KAGLQHHQDLSTPVLRSDVDALQQVVEEAVgQALPG-ATVTL 317
Cdd:COG1796   105 KKLYEElGITSLEELEAaaeegRIRELpgfgekTEENiLKGIELLRKRGGRFLLGEALPLAEEILAYL-RALPGvERVEV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381931185 318 TGGFRRGKLQGHDVDFLIThpkegqeagllprvmcrlqdqglilyhqhqhscCESPTRLaqqshMDAFERsfcifrlpQP 397
Cdd:COG1796   184 AGSLRRRKETVGDIDILVA---------------------------------SDDPEAV-----MDAFVK--------LP 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381931185 398 PGAAV--GGSTrpcpswKA-------VRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFD 463
Cdd:COG1796   218 EVKEVlaKGDT------KAsvrlksgLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLA-KERGLKLNEYGLFD 285
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 430-467 2.49e-11

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: 59.31  E-value: 2.49e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1381931185 430 ALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 467
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDG 37
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 292-360 2.99e-11

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: 60.66  E-value: 2.99e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1381931185 292 RSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHP---KEGQEAGLLPRVMCRLQDQGLI 360
Cdd:pfam14792   4 REEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPdgtSESELKGLLDRLVARLKKSGFL 75
HHH_8 pfam14716
Helix-hairpin-helix domain;
153-218 4.51e-10

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 55.59  E-value: 4.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1381931185 153 NTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLE 218
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 302-347 3.70e-05

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: 42.40  E-value: 3.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1381931185 302 VEEAVGQALPGATVTLTGGFRRGK-LQGHDVDFLITHPKEGQEAGLL 347
Cdd:pfam01909   4 LREILKELFPVAEVVLFGSYARGTaLPGSDIDLLVVFPEPVEEERLL 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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