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Conserved domains on  [gi|547234859|ref|NP_001271259|]
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DNA-directed DNA/RNA polymerase mu isoform 2 [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 7.55e-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: 181.58  E-value: 7.55e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442    1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                         90
                 ....*....|....*...
gi 547234859 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 ...
 156-387 1.21e-26

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: 109.59  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSera 234
Cdd:cd00141    3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 235 pAPP-----------GP------------------EHPSP--------------AVRCRCPAAGGGgscgagpawghRHA 271
Cdd:cd00141   80 -VPPglllllrvpgvGPktarklyelgirtledlrKAAGAkleqniligleyyeDFQQRIPREEAL-----------AIA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 272 D----------------------RRLPQG----LILYHQHQHSCCESP---TRLAQQ-----SHMDAFERSFCIFRLPQp 317
Cdd:cd00141  148 EiikealrevdpvlqveiagsyrRGKETVgdidILVTHPDATSRGLLEkvvDALVELgfvteVLSKGDTKASGILKLPG- 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 318 pgaavggstrpcpSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 387
Cdd:cd00141  227 -------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDG 282
 
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 7.55e-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: 181.58  E-value: 7.55e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442    1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                         90
                 ....*....|....*...
gi 547234859 106 TESLGAGQPVPVECRHRL 123
Cdd:cd18442   81 TESMGAGQPVPVECRHRL 98
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 156-387 1.21e-26

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: 109.59  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSera 234
Cdd:cd00141    3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 235 pAPP-----------GP------------------EHPSP--------------AVRCRCPAAGGGgscgagpawghRHA 271
Cdd:cd00141   80 -VPPglllllrvpgvGPktarklyelgirtledlrKAAGAkleqniligleyyeDFQQRIPREEAL-----------AIA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 272 D----------------------RRLPQG----LILYHQHQHSCCESP---TRLAQQ-----SHMDAFERSFCIFRLPQp 317
Cdd:cd00141  148 EiikealrevdpvlqveiagsyrRGKETVgdidILVTHPDATSRGLLEkvvDALVELgfvteVLSKGDTKASGILKLPG- 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 318 pgaavggstrpcpSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 387
Cdd:cd00141  227 -------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDG 282
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 152-383 1.80e-21

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 95.51  E-value: 1.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859   152 HNTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRR 230
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEILN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859   231 SERAPAPP--------GPEHP-------------------------------------SPAVRCRCPAAGGGGSCGAGPA 265
Cdd:smart00483  82 DEVYKSLKlftnvfgvGPKTAakwyrkgirtleelkknkelkltkqqkaglkyyedilKKVSRAEAFAVEYIVKRAVRKI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859   266 W---------GHRhadRRLPQG----LILYHQHQHSCCESPT---------------RLAQQSHMDAFERSFCIFRLPQP 317
Cdd:smart00483 162 LpdaivtltgSFR---RGKETGhdvdFLITSPHPAKEKELEVldllllestfeelqlPSIRVATLDHGQKKFMILKLSPS 238

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547234859   318 PGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFD 383
Cdd:smart00483 239 REDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYD 304
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 350-387 2.19e-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: 2.19e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 547234859  350 ALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 387
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDG 37
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
335-383 5.56e-05

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 45.57  E-value: 5.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 547234859 335 VRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFD 383
Cdd:COG1796  238 LQVDLRVVPPESFGAALQYFTGSKEHNVALRQLA-KERGLKLNEYGLFD 285
 
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 7.55e-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: 181.58  E-value: 7.55e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWL 105
Cdd:cd18442    1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACTPPALLDISWF 80

                         90
                 ....*....|....*...
gi 547234859 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 6.52e-45

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: 6.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAappGCTPPALLDISWL 105
Cdd:cd17713    1 KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQ---GSSSPELLDISWF 77

                         90
                 ....*....|
gi 547234859 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 1.58e-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: 1.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859  26 RFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSW-QERRMAAAPpgctPPALLDISW 104
Cdd:cd18443    1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWlQGQKLRDSS----RLELLDISW 76

                         90
                 ....*....|....*....
gi 547234859 105 LTESLGAGQPVPVECRHRL 123
Cdd:cd18443   77 FTECMGAGKPVEIEKRHRL 95
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 156-387 1.21e-26

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: 109.59  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 156 LSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSera 234
Cdd:cd00141    3 IADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 235 pAPP-----------GP------------------EHPSP--------------AVRCRCPAAGGGgscgagpawghRHA 271
Cdd:cd00141   80 -VPPglllllrvpgvGPktarklyelgirtledlrKAAGAkleqniligleyyeDFQQRIPREEAL-----------AIA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 272 D----------------------RRLPQG----LILYHQHQHSCCESP---TRLAQQ-----SHMDAFERSFCIFRLPQp 317
Cdd:cd00141  148 EiikealrevdpvlqveiagsyrRGKETVgdidILVTHPDATSRGLLEkvvDALVELgfvteVLSKGDTKASGILKLPG- 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859 318 pgaavggstrpcpSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 387
Cdd:cd00141  227 -------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLA-KEKGLKLNEYGLFDGVDG 282
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 152-383 1.80e-21

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 95.51  E-value: 1.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859   152 HNTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRR 230
Cdd:smart00483   2 LNRGIIDALEILAENYEVFGeNKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEILN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859   231 SERAPAPP--------GPEHP-------------------------------------SPAVRCRCPAAGGGGSCGAGPA 265
Cdd:smart00483  82 DEVYKSLKlftnvfgvGPKTAakwyrkgirtleelkknkelkltkqqkaglkyyedilKKVSRAEAFAVEYIVKRAVRKI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234859   266 W---------GHRhadRRLPQG----LILYHQHQHSCCESPT---------------RLAQQSHMDAFERSFCIFRLPQP 317
Cdd:smart00483 162 LpdaivtltgSFR---RGKETGhdvdFLITSPHPAKEKELEVldllllestfeelqlPSIRVATLDHGQKKFMILKLSPS 238

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547234859   318 PGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFD 383
Cdd:smart00483 239 REDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYD 304
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 350-387 2.19e-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: 2.19e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 547234859  350 ALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFDPEQG 387
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDG 37
HHH_8 pfam14716
Helix-hairpin-helix domain;
153-218 3.88e-10

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 55.59  E-value: 3.88e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547234859  153 NTGLSEALEILAEAAGFEG-SEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLE 218
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
335-383 5.56e-05

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 45.57  E-value: 5.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 547234859 335 VRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSrKEKGLWLNSHGLFD 383
Cdd:COG1796  238 LQVDLRVVPPESFGAALQYFTGSKEHNVALRQLA-KERGLKLNEYGLFD 285
 
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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