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Conserved domains on  [gi|1802876784|ref|XP_032047690|]
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DNA nucleotidylexotransferase isoform X3 [Aythya fuligula]

Protein Classification

BRCT domain-containing protein( domain architecture ID 13042308)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 111-460 2.89e-171

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


:

Pssm-ID: 214688  Cd Length: 334  Bit Score: 484.18  E-value: 2.89e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  111 NCNKKFTDAFEIMAENYE-FKENEIFCLEFLRAASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIEDGESSRAKDVL 189
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  190 NDERYKSFK-FTSVFGVGVKTSEKWFRMGLRTLEEVKADKTLKLSKMQRAGFLYYEDLVSFVSKAEADAVSLIVKNTVCT 268
Cdd:smart00483  81 NDEVYKSLKlFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  269 FLPDALVTITGGFRRGKKIGHDIDFLITNPGPRedDELLHKVVDLWKkqglllycdiIESTFVKEQIPSREVDAMDHFQK 348
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPA--KEKELEVLDLLL----------LESTFEELQLPSIRVATLDHGQK 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  349 CFAILKLYTPSTDNSSYNTSKEcdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHAL 428
Cdd:smart00483 229 KFMILKLSPSREDKEKSGKPDE------KGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHEL 302

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1802876784  429 YDKRKRIFLKAGSEEEIFAHLGLDYLEPWERN 460
Cdd:smart00483 303 YDKTKEKFLKVESEEDIFDHLGLPYIEPEERN 334
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 1-73 2.51e-39

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 cd18443:

Pssm-ID: 469589  Cd Length: 95  Bit Score: 137.24  E-value: 2.51e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802876784   1 MELARSKGFRVESELSDSVTHIVAENNSYLEVLDWLRGQAVGDSSRFELLDISWLTACMEAGRPVDSEMKYRL 73
Cdd:cd18443    23 MELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTECMGAGKPVEIEKRHRL 95
 
Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 111-460 2.89e-171

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 484.18  E-value: 2.89e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  111 NCNKKFTDAFEIMAENYE-FKENEIFCLEFLRAASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIEDGESSRAKDVL 189
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  190 NDERYKSFK-FTSVFGVGVKTSEKWFRMGLRTLEEVKADKTLKLSKMQRAGFLYYEDLVSFVSKAEADAVSLIVKNTVCT 268
Cdd:smart00483  81 NDEVYKSLKlFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  269 FLPDALVTITGGFRRGKKIGHDIDFLITNPGPRedDELLHKVVDLWKkqglllycdiIESTFVKEQIPSREVDAMDHFQK 348
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPA--KEKELEVLDLLL----------LESTFEELQLPSIRVATLDHGQK 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  349 CFAILKLYTPSTDNSSYNTSKEcdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHAL 428
Cdd:smart00483 229 KFMILKLSPSREDKEKSGKPDE------KGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHEL 302

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1802876784  429 YDKRKRIFLKAGSEEEIFAHLGLDYLEPWERN 460
Cdd:smart00483 303 YDKTKEKFLKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 114-459 1.60e-112

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: 333.78  E-value: 1.60e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 114 KKFTDAFEIMAENYEFKENEIF-CLEFLRAASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIEDGESSRAKDVLNDe 192
Cdd:cd00141     1 QEIADILEELADLLELLGGNPFrVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 193 RYKSFK-FTSVFGVGVKTSEKWFRMGLRTLEEVKADKTLKLSKMQRAGFLYYEDLVSFVSKAEADAVSLIVKNTVCTFLP 271
Cdd:cd00141    80 VPPGLLlLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 272 DALVTITGGFRRGKKIGHDIDFLITNPGpREDDELLHKVVDLWKKQGLLLYcdiiestfvkeqipsrevDAMDHFQKCFA 351
Cdd:cd00141   160 VLQVEIAGSYRRGKETVGDIDILVTHPD-ATSRGLLEKVVDALVELGFVTE------------------VLSKGDTKASG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 352 ILKLYtpstdnssyntskecdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKMMLDNHALYDK 431
Cdd:cd00141   221 ILKLP--------------------GGWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAK-EKGLKLNEYGLFDG 279

                         330       340
                  ....*....|....*....|....*...
gi 1802876784 432 RKRIFLKAGSEEEIFAHLGLDYLEPWER 459
Cdd:cd00141   280 VDGERLPGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 1-73 2.51e-39

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: 137.24  E-value: 2.51e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802876784   1 MELARSKGFRVESELSDSVTHIVAENNSYLEVLDWLRGQAVGDSSRFELLDISWLTACMEAGRPVDSEMKYRL 73
Cdd:cd18443    23 MELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTECMGAGKPVEIEKRHRL 95
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 397-460 4.19e-21

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: 86.27  E-value: 4.19e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802876784 397 ALLGWTGSRQFGRDLRRYAtHERKMMLDNHALYDKRKRIFLKAGSEEEIFAHLGLDYLEPWERN 460
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
141-456 2.03e-13

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 72.15  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 141 RAASVLKCLPFPVTRM---KDIQGLPCMGDQVRDVIEEIIEDGESS-----RAK---DVLNderyksfkFTSVFGVGVKT 209
Cdd:COG1796    32 RAARAIENLPEDIEELvaeGDLTEIPGIGKAIAAKIEELLETGRLEeleelREEvppGLLE--------LLRIPGLGPKK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 210 SEK-WFRMGLRTLEEVKA--------------DKT----LK-LSKMQRAG--FLYY------EDLVSFVSKAEAdavsli 261
Cdd:COG1796   104 VKKlYEELGITSLEELEAaaeegrirelpgfgEKTeeniLKgIELLRKRGgrFLLGealplaEEILAYLRALPG------ 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 262 VKNtvctflpdalVTITGGFRRGKKIGHDIDFLITNPGPReddellhKVVDLwkkqglllycdIIESTFVKEQIPSREvd 341
Cdd:COG1796   178 VER----------VEVAGSLRRRKETVGDIDILVASDDPE-------AVMDA-----------FVKLPEVKEVLAKGD-- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 342 amdhfQKCFAILKlytpstdnssyntskecdmaevkdwKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKM 421
Cdd:COG1796   228 -----TKASVRLK-------------------------SGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAK-ERGL 276

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1802876784 422 MLDNHALYDKRKRIfLKAGSEEEIFAHLGLDYLEP 456
Cdd:COG1796   277 KLNEYGLFDVGGER-IAGETEEEVYAALGLPYIPP 310
BRCT smart00292
breast cancer carboxy-terminal domain;
1-59 7.46e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.13  E-value: 7.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784    1 MELARSKGFRVESELS-DSVTHIVAENNSYlEVLDWLRGQAVGdssrFELLDISWLTACM 59
Cdd:smart00292  24 KELIEALGGKVTSSLSsKTTTHVIVGSPEG-GKLELLKAIALG----IPIVKEEWLLDCL 78
 
Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 111-460 2.89e-171

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 484.18  E-value: 2.89e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  111 NCNKKFTDAFEIMAENYE-FKENEIFCLEFLRAASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIEDGESSRAKDVL 189
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  190 NDERYKSFK-FTSVFGVGVKTSEKWFRMGLRTLEEVKADKTLKLSKMQRAGFLYYEDLVSFVSKAEADAVSLIVKNTVCT 268
Cdd:smart00483  81 NDEVYKSLKlFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  269 FLPDALVTITGGFRRGKKIGHDIDFLITNPGPRedDELLHKVVDLWKkqglllycdiIESTFVKEQIPSREVDAMDHFQK 348
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPA--KEKELEVLDLLL----------LESTFEELQLPSIRVATLDHGQK 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  349 CFAILKLYTPSTDNSSYNTSKEcdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHAL 428
Cdd:smart00483 229 KFMILKLSPSREDKEKSGKPDE------KGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHEL 302

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1802876784  429 YDKRKRIFLKAGSEEEIFAHLGLDYLEPWERN 460
Cdd:smart00483 303 YDKTKEKFLKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 114-459 1.60e-112

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: 333.78  E-value: 1.60e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 114 KKFTDAFEIMAENYEFKENEIF-CLEFLRAASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIEDGESSRAKDVLNDe 192
Cdd:cd00141     1 QEIADILEELADLLELLGGNPFrVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 193 RYKSFK-FTSVFGVGVKTSEKWFRMGLRTLEEVKADKTLKLSKMQRAGFLYYEDLVSFVSKAEADAVSLIVKNTVCTFLP 271
Cdd:cd00141    80 VPPGLLlLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 272 DALVTITGGFRRGKKIGHDIDFLITNPGpREDDELLHKVVDLWKKQGLLLYcdiiestfvkeqipsrevDAMDHFQKCFA 351
Cdd:cd00141   160 VLQVEIAGSYRRGKETVGDIDILVTHPD-ATSRGLLEKVVDALVELGFVTE------------------VLSKGDTKASG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 352 ILKLYtpstdnssyntskecdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKMMLDNHALYDK 431
Cdd:cd00141   221 ILKLP--------------------GGWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAK-EKGLKLNEYGLFDG 279

                         330       340
                  ....*....|....*....|....*...
gi 1802876784 432 RKRIFLKAGSEEEIFAHLGLDYLEPWER 459
Cdd:cd00141   280 VDGERLPGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 1-73 2.51e-39

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: 137.24  E-value: 2.51e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802876784   1 MELARSKGFRVESELSDSVTHIVAENNSYLEVLDWLRGQAVGDSSRFELLDISWLTACMEAGRPVDSEMKYRL 73
Cdd:cd18443    23 MELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTECMGAGKPVEIEKRHRL 95
BRCT_polymerase_mu_like cd17713
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu), DNA ...
 1-65 1.65e-35

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: 126.74  E-value: 1.65e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802876784   1 MELARSKGFRVESELSDSVTHIVAENNSYLEVLDWLRGQAVGDSSRFELLDISWLTACMEAGRPV 65
Cdd:cd17713    23 TELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQGSSSPELLDISWFTESMGAGKPV 87
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 3-73 3.75e-22

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: 90.67  E-value: 3.75e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802876784   3 LARSKGFRVESELSDSVTHIVAENNSYLEVLDWLR---GQAVGDSSRFELLDISWLTACMEAGRPVDSEMKYRL 73
Cdd:cd18442    25 LARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLErqmAAAPPACTPPALLDISWFTESMGAGQPVPVECRHRL 98
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 397-460 4.19e-21

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: 86.27  E-value: 4.19e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802876784 397 ALLGWTGSRQFGRDLRRYAtHERKMMLDNHALYDKRKRIFLKAGSEEEIFAHLGLDYLEPWERN 460
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
 199-246 2.81e-16

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: 72.49  E-value: 2.81e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1802876784 199 FTSVFGVGVKTSEKWFRMGLRTLEEVKADKTLKLSKMQRAGFLYYEDL 246
Cdd:pfam10391   3 FTGIYGVGPTTARKWYAQGYRTLDDLREKKTAKLTRQQQIGLKYYDDF 50
HHH_8 pfam14716
Helix-hairpin-helix domain;
113-178 1.55e-13

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 65.22  E-value: 1.55e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802876784 113 NKKFTDAFEIMAENYEFKENEIF-CLEFLRAASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIE 178
Cdd:pfam14716   1 NQEIADALEELADLLELKGEDPFrVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
141-456 2.03e-13

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 72.15  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 141 RAASVLKCLPFPVTRM---KDIQGLPCMGDQVRDVIEEIIEDGESS-----RAK---DVLNderyksfkFTSVFGVGVKT 209
Cdd:COG1796    32 RAARAIENLPEDIEELvaeGDLTEIPGIGKAIAAKIEELLETGRLEeleelREEvppGLLE--------LLRIPGLGPKK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 210 SEK-WFRMGLRTLEEVKA--------------DKT----LK-LSKMQRAG--FLYY------EDLVSFVSKAEAdavsli 261
Cdd:COG1796   104 VKKlYEELGITSLEELEAaaeegrirelpgfgEKTeeniLKgIELLRKRGgrFLLGealplaEEILAYLRALPG------ 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 262 VKNtvctflpdalVTITGGFRRGKKIGHDIDFLITNPGPReddellhKVVDLwkkqglllycdIIESTFVKEQIPSREvd 341
Cdd:COG1796   178 VER----------VEVAGSLRRRKETVGDIDILVASDDPE-------AVMDA-----------FVKLPEVKEVLAKGD-- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 342 amdhfQKCFAILKlytpstdnssyntskecdmaevkdwKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKM 421
Cdd:COG1796   228 -----TKASVRLK-------------------------SGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAK-ERGL 276

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1802876784 422 MLDNHALYDKRKRIfLKAGSEEEIFAHLGLDYLEP 456
Cdd:COG1796   277 KLNEYGLFDVGGER-IAGETEEEVYAALGLPYIPP 310
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 253-320 3.93e-10

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: 56.81  E-value: 3.93e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802876784 253 AEADAVSLIVKNTVCTFLPDALVTITGGFRRGKKIGHDIDFLITNPGPREDDE---LLHKVVDLWKKQGLL 320
Cdd:pfam14792   5 EEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESElkgLLDRLVARLKKSGFL 75
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 262-349 4.85e-07

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: 47.80  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784 262 VKNTVCTFLPDALVTITGGFRRGK-KIGHDIDFLITNPGPREDDELLHKVVDLWKKQGLLLYCDIIeSTFVKEQIPSREV 340
Cdd:pfam01909   4 LREILKELFPVAEVVLFGSYARGTaLPGSDIDLLVVFPEPVEEERLLKLAKIIKELEELLGLEVDL-VTREKIEFPLVKI 82


                  ....*....
gi 1802876784 341 DAMDHFQKC 349
Cdd:pfam01909  83 DILEERILL 91
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 1-65 3.03e-04

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 39.51  E-value: 3.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802876784   1 MELARSKGFRVESELSDSVTHIVAENNSYLEV---LDWLRGQAVGDSsrfeLLDISWLTACMEAGRPV 65
Cdd:cd17734    17 EKLAQLLKAKVVTEFSPEVTHVVVPADERGVCprtMKYLMGILAGKW----IVSFEWVEACLKAKKLV 80
BRCT smart00292
breast cancer carboxy-terminal domain;
1-59 7.46e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.13  E-value: 7.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784    1 MELARSKGFRVESELS-DSVTHIVAENNSYlEVLDWLRGQAVGdssrFELLDISWLTACM 59
Cdd:smart00292  24 KELIEALGGKVTSSLSsKTTTHVIVGSPEG-GKLELLKAIALG----IPIVKEEWLLDCL 78
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 1-63 9.10e-03

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


Pssm-ID: 349343  Cd Length: 81  Bit Score: 35.32  E-value: 9.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802876784   1 MELARSKGFRVESELSDSVTHIVAENNSYLEVLdwlrgQAVGDSSRfeLLDISWLTACMEAGR 63
Cdd:cd17711    22 KKVIEEHGGEVVDEYSPRVTHVICESQDSPEYQ-----QALRDGKR--VVTAYWLNDVLKRGK 77
COG4646 COG4646
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];
127-266 9.64e-03

Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];


Pssm-ID: 443684 [Multi-domain]  Cd Length: 1711  Bit Score: 38.69  E-value: 9.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802876784  127 YEFKENEIFCLEflraASVLKCLPFPVTRMKDIQGLPCMGDQVRDVIEEIIEDGESSRAKDVLNDERYKSfkFTSVFG-V 205
Cdd:COG4646    515 YTFEDGVLYVDE----AHNFKNLEVPATKMRRVAGLIPLRDAVRELIEAQAEDDGSQKALRMRLNCRYDA--FVAKYGpI 588

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802876784  206 GVKTSEKWFRM-----GLRTLEEV-----KADKTLKLSKmqRAGFLYYEDLVSfvSKAEADAVSLIVKNTV 266
Cdd:COG4646    589 NSRPNLRAFRDdpdypLLLSLEEYdeetgTARKADIFTK--RVIRPPTETSVD--TAAEALAVSLNERGRV 655
 
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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