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Conserved domains on  [gi|10434716|dbj|BAB14353|]
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unnamed protein product [Homo sapiens]

Protein Classification

BRCT_polymerase_mu and NT_Pol-beta-like domain-containing protein( domain architecture ID 13035155)

BRCT_polymerase_mu and NT_Pol-beta-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 26-123 9.31e-59

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: 181.20  E-value: 9.31e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434716  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442   1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                        90
                ....*....|....*...
gi 10434716 106 TESLGAGQPVPVECRHRL 123
Cdd:cd18442  81 TESMGAGQPVPVECRHRL 98
NT_Pol-beta-like super family cl11966
Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This ...
 156-222 3.66e-11

Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes.


The actual alignment was detected with superfamily member cd00141:

Pssm-ID: 472251 [Multi-domain]  Cd Length: 307  Bit Score: 61.83  E-value: 3.66e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10434716 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVC 222
Cdd:cd00141   3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKL 70
 
Name Accession Description Interval E-value
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 26-123 9.31e-59

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: 181.20  E-value: 9.31e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434716  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442   1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                        90
                ....*....|....*...
gi 10434716 106 TESLGAGQPVPVECRHRL 123
Cdd:cd18442  81 TESMGAGQPVPVECRHRL 98
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 156-222 3.66e-11

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: 61.83  E-value: 3.66e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10434716 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVC 222
Cdd:cd00141   3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKL 70
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 152-221 1.21e-10

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 60.46  E-value: 1.21e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10434716    152 HNTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGV 221
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGK 72
HHH_8 pfam14716
Helix-hairpin-helix domain;
153-218 1.22e-10

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 55.59  E-value: 1.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10434716   153 NTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLE 218
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
 
Name Accession Description Interval E-value
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 26-123 9.31e-59

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: 181.20  E-value: 9.31e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434716  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442   1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                        90
                ....*....|....*...
gi 10434716 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 3.13e-47

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: 151.39  E-value: 3.13e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434716  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAappGCTPPALLDISWL 105
Cdd:cd17713   1 KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQ---GSSSPELLDISWF 77

                        90
                ....*....|
gi 10434716 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 2.07e-30

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: 2.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434716  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSW-QERRMAAAPpgctPPALLDISW 104
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWlQGQKLRDSS----RLELLDISW 76

                        90
                ....*....|....*....
gi 10434716 105 LTESLGAGQPVPVECRHRL 123
Cdd:cd18443  77 FTECMGAGKPVEIEKRHRL 95
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 156-222 3.66e-11

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: 61.83  E-value: 3.66e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10434716 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVC 222
Cdd:cd00141   3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKL 70
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 152-221 1.21e-10

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 60.46  E-value: 1.21e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10434716    152 HNTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGV 221
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGK 72
HHH_8 pfam14716
Helix-hairpin-helix domain;
153-218 1.22e-10

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 55.59  E-value: 1.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10434716   153 NTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLE 218
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 42-108 7.03e-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.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 34.26  E-value: 7.03e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10434716  42 SRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVswqerrMAAAPPGCTppaLLDISWLTES 108
Cdd:cd00027  11 EEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYY------LAALAWGIP---IVSPEWLLDC 68
 
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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