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Conserved domains on  [gi|549065|sp|P36195|]
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RecName: Full=DNA nucleotidylexotransferase; AltName: Full=Terminal addition enzyme; AltName: Full=Terminal deoxynucleotidyltransferase; Short=Terminal transferase

Protein Classification

BRCT domain-containing protein( domain architecture ID 13035160)

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 ...
 163-505 2.71e-169

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


:

Pssm-ID: 214688  Cd Length: 334  Bit Score: 481.10  E-value: 2.71e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      163 NCNKKFTDAFEIMAENYE-FKENEIFCLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDVIEEIIEEGESSRAKDVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      242 NDERYKSFKEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDLVSCVSKAEADAVSSIVKNTVCT 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      322 FLPDALVTITGGFRRGKKIGHDIDFLITSPGQREDDELLHKGLLLycdiIESTFVKEQIPSRHVDAMDHFQKCFAILKLY 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAKEKELEVLDLLL----LESTFEELQLPSIRVATLDHGQKKFMILKLS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      402 QPRVDNSSYNMSKKcdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHALYDKRKRVF 481
Cdd:smart00483 237 PSREDKEKSGKPDE------KGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDKTKEKF 310

                          330       340
                   ....*....|....*....|....
gi 549065      482 LKAGSEEEIFAHLGLDYVEPWERN 505
Cdd:smart00483 311 LKVESEEDIFDHLGLPYIEPEERN 334
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 2.77e-58

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: 187.70  E-value: 2.77e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065    31 KFNKLVIFIMQRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLDWLKGQAVGDSSRFEILDISWLTAC 110
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                        90
                ....*....|....*
gi 549065   111 MEMGRPVDLEKKYHL 125
Cdd:cd18443  81 MGAGKPVEIEKRHRL 95
 
Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 163-505 2.71e-169

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 481.10  E-value: 2.71e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      163 NCNKKFTDAFEIMAENYE-FKENEIFCLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDVIEEIIEEGESSRAKDVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      242 NDERYKSFKEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDLVSCVSKAEADAVSSIVKNTVCT 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      322 FLPDALVTITGGFRRGKKIGHDIDFLITSPGQREDDELLHKGLLLycdiIESTFVKEQIPSRHVDAMDHFQKCFAILKLY 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAKEKELEVLDLLL----LESTFEELQLPSIRVATLDHGQKKFMILKLS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      402 QPRVDNSSYNMSKKcdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHALYDKRKRVF 481
Cdd:smart00483 237 PSREDKEKSGKPDE------KGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDKTKEKF 310

                          330       340
                   ....*....|....*....|....
gi 549065      482 LKAGSEEEIFAHLGLDYVEPWERN 505
Cdd:smart00483 311 LKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 166-504 1.22e-106

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: 320.30  E-value: 1.22e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   166 KKFTDAFEIMAENYEFKENEIF-CLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDVIEEIIEEGESSRAKDVLNDe 244
Cdd:cd00141   1 QEIADILEELADLLELLGGNPFrVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   245 RYKSFKEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDLVSCVSKAEADAVSSIVKNTVCTFLP 324
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   325 DALVTITGGFRRGKKIGHDIDFLITSPGQREDDEL--LHKGLLlycdiiESTFVKEqipsrhvDAMDHFQKCFAILKLYQ 402
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPDATSRGLLekVVDALV------ELGFVTE-------VLSKGDTKASGILKLPG 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   403 prvdnssynmskkcdmaevkDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKMMLDNHALYDKRKRVFL 482
Cdd:cd00141 227 --------------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAK-EKGLKLNEYGLFDGVDGERL 285

                       330       340
                ....*....|....*....|..
gi 549065   483 KAGSEEEIFAHLGLDYVEPWER 504
Cdd:cd00141 286 PGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 2.77e-58

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: 187.70  E-value: 2.77e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065    31 KFNKLVIFIMQRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLDWLKGQAVGDSSRFEILDISWLTAC 110
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                        90
                ....*....|....*
gi 549065   111 MEMGRPVDLEKKYHL 125
Cdd:cd18443  81 MGAGKPVEIEKRHRL 95
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 442-505 5.24e-22

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: 89.35  E-value: 5.24e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549065     442 ALLGWTGSRQFGRDLRRYAtHERKMMLDNHALYDKRKRVFLKAGSEEEIFAHLGLDYVEPWERN 505
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
328-501 1.33e-12

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 69.84  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   328 VTITGGFRRGKKIGHDIDFLITSpgqrEDDEllhkglllycdiiestfvkeqipsrhvDAMDHFqkcfailklyqprvdn 407
Cdd:COG1796 181 VEVAGSLRRRKETVGDIDILVAS----DDPE---------------------------AVMDAF---------------- 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   408 ssynmskkCDMAEVKD-------------WKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKMMLDNHALY 474
Cdd:COG1796 214 --------VKLPEVKEvlakgdtkasvrlKSGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAK-ERGLKLNEYGLF 284

                       170       180
                ....*....|....*....|....*..
gi 549065   475 DKRKRVfLKAGSEEEIFAHLGLDYVEP 501
Cdd:COG1796 285 DVGGER-IAGETEEEVYAALGLPYIPP 310
BRCT smart00292
breast cancer carboxy-terminal domain;
32-111 1.39e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 51.61  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065       32 FNKLVIFIMqRKMGMTRRTFLMELARSKGFRVESELS-DSVTHIVAENNSyPEVLDWLKGQAVGdssrFEILDISWLTAC 110
Cdd:smart00292   4 FKGKTFYIT-GSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPE-GGKLELLKAIALG----IPIVKEEWLLDC 77


                   .
gi 549065      111 M 111
Cdd:smart00292  78 L 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 27-111 6.41e-08

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 49.60  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      27 GYEIKFNKLVIFIMqrKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAEnnsypevlDWLKGQAVGDSSRFEILDISW 106
Cdd:pfam00533   1 PKEKLFSGKTFVIT--GLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE--------ARTKKYLKAKELGIPIVTEEW 70


                  ....*
gi 549065     107 LTACM 111
Cdd:pfam00533  71 LLDCI 75
 
Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 163-505 2.71e-169

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 481.10  E-value: 2.71e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      163 NCNKKFTDAFEIMAENYE-FKENEIFCLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDVIEEIIEEGESSRAKDVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      242 NDERYKSFKEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDLVSCVSKAEADAVSSIVKNTVCT 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      322 FLPDALVTITGGFRRGKKIGHDIDFLITSPGQREDDELLHKGLLLycdiIESTFVKEQIPSRHVDAMDHFQKCFAILKLY 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAKEKELEVLDLLL----LESTFEELQLPSIRVATLDHGQKKFMILKLS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      402 QPRVDNSSYNMSKKcdmaevKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHALYDKRKRVF 481
Cdd:smart00483 237 PSREDKEKSGKPDE------KGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDKTKEKF 310

                          330       340
                   ....*....|....*....|....
gi 549065      482 LKAGSEEEIFAHLGLDYVEPWERN 505
Cdd:smart00483 311 LKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 166-504 1.22e-106

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: 320.30  E-value: 1.22e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   166 KKFTDAFEIMAENYEFKENEIF-CLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDVIEEIIEEGESSRAKDVLNDe 244
Cdd:cd00141   1 QEIADILEELADLLELLGGNPFrVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   245 RYKSFKEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDLVSCVSKAEADAVSSIVKNTVCTFLP 324
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   325 DALVTITGGFRRGKKIGHDIDFLITSPGQREDDEL--LHKGLLlycdiiESTFVKEqipsrhvDAMDHFQKCFAILKLYQ 402
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPDATSRGLLekVVDALV------ELGFVTE-------VLSKGDTKASGILKLPG 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   403 prvdnssynmskkcdmaevkDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKMMLDNHALYDKRKRVFL 482
Cdd:cd00141 227 --------------------GWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAK-EKGLKLNEYGLFDGVDGERL 285

                       330       340
                ....*....|....*....|..
gi 549065   483 KAGSEEEIFAHLGLDYVEPWER 504
Cdd:cd00141 286 PGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 2.77e-58

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: 187.70  E-value: 2.77e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065    31 KFNKLVIFIMQRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLDWLKGQAVGDSSRFEILDISWLTAC 110
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                        90
                ....*....|....*
gi 549065   111 MEMGRPVDLEKKYHL 125
Cdd:cd18443  81 MGAGKPVEIEKRHRL 95
BRCT_polymerase_mu_like cd17713
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu), DNA ...
 31-117 4.86e-52

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: 171.42  E-value: 4.86e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065    31 KFNKLVIFIMQRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLDWLKGQAVGDSSRFEILDISWLTAC 110
Cdd:cd17713   1 KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQGSSSPELLDISWFTES 80


                ....*..
gi 549065   111 MEMGRPV 117
Cdd:cd17713  81 MGAGKPV 87
BRCT_polymerase_mu cd18442
BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins; ...
 31-125 5.31e-31

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: 115.33  E-value: 5.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065    31 KFNKLVIFIMQRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLDWLK---GQAVGDSSRFEILDISWL 107
Cdd:cd18442   1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLErqmAAAPPACTPPALLDISWF 80

                        90
                ....*....|....*...
gi 549065   108 TACMEMGRPVDLEKKYHL 125
Cdd:cd18442  81 TESMGAGQPVPVECRHRL 98
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 442-505 5.24e-22

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: 89.35  E-value: 5.24e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549065     442 ALLGWTGSRQFGRDLRRYAtHERKMMLDNHALYDKRKRVFLKAGSEEEIFAHLGLDYVEPWERN 505
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 ...
 250-299 1.55e-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: 73.26  E-value: 1.55e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 549065     250 KEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDL 299
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREKKTAKLTRQQQIGLKYYDDF 50
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
328-501 1.33e-12

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 69.84  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   328 VTITGGFRRGKKIGHDIDFLITSpgqrEDDEllhkglllycdiiestfvkeqipsrhvDAMDHFqkcfailklyqprvdn 407
Cdd:COG1796 181 VEVAGSLRRRKETVGDIDILVAS----DDPE---------------------------AVMDAF---------------- 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065   408 ssynmskkCDMAEVKD-------------WKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYAThERKMMLDNHALY 474
Cdd:COG1796 214 --------VKLPEVKEvlakgdtkasvrlKSGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAK-ERGLKLNEYGLF 284

                       170       180
                ....*....|....*....|....*..
gi 549065   475 DKRKRVfLKAGSEEEIFAHLGLDYVEP 501
Cdd:COG1796 285 DVGGER-IAGETEEEVYAALGLPYIPP 310
HHH_8 pfam14716
Helix-hairpin-helix domain;
165-224 1.89e-10

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 56.74  E-value: 1.89e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549065     165 NKKFTDAFEIMAENYEFKENEIF-CLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDV 224
Cdd:pfam14716   1 NQEIADALEELADLLELKGEDPFrVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAK 61
BRCT smart00292
breast cancer carboxy-terminal domain;
32-111 1.39e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 51.61  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065       32 FNKLVIFIMqRKMGMTRRTFLMELARSKGFRVESELS-DSVTHIVAENNSyPEVLDWLKGQAVGdssrFEILDISWLTAC 110
Cdd:smart00292   4 FKGKTFYIT-GSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPE-GGKLELLKAIALG----IPIVKEEWLLDC 77


                   .
gi 549065      111 M 111
Cdd:smart00292  78 L 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 27-111 6.41e-08

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 49.60  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065      27 GYEIKFNKLVIFIMqrKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAEnnsypevlDWLKGQAVGDSSRFEILDISW 106
Cdd:pfam00533   1 PKEKLFSGKTFVIT--GLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE--------ARTKKYLKAKELGIPIVTEEW 70


                  ....*
gi 549065     107 LTACM 111
Cdd:pfam00533  71 LLDCI 75
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 306-365 4.82e-07

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: 48.33  E-value: 4.82e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 549065     306 AEADAVSSIVKNTVCTFLPDALVTITGGFRRGKKIGHDIDFLITSPGQREDDEllHKGLL 365
Cdd:pfam14792   5 EEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESE--LKGLL 62
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 52-117 9.02e-06

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: 43.74  E-value: 9.02e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549065    52 LMELARSKGFRVESELSDSVTHIVAENNSY---PEVLDWLKGQAVGDSsrfeILDISWLTACMEMGRPV 117
Cdd:cd17734  16 LEKLAQLLKAKVVTEFSPEVTHVVVPADERgvcPRTMKYLMGILAGKW----IVSFEWVEACLKAKKLV 80
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 313-386 2.19e-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: 43.17  E-value: 2.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549065     313 SIVKNTVCTFLPDALVTITGGFRRGK-KIGHDIDFLITSPGQREDDELLHKGLLLYcdiiestfVKEQIPSRHVD 386
Cdd:pfam01909   2 RKLREILKELFPVAEVVLFGSYARGTaLPGSDIDLLVVFPEPVEEERLLKLAKIIK--------ELEELLGLEVD 68
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 48-110 6.37e-05

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: 41.19  E-value: 6.37e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549065    48 RRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLdwLKGQAVGdssrFEILDISWLTAC 110
Cdd:cd00027  12 EREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYY--LAALAWG----IPIVSPEWLLDC 68
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 41-115 9.10e-05

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: 41.10  E-value: 9.10e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549065    41 QRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLdwlkgQAVGDSSRfeILDISWLTACMEMGR 115
Cdd:cd17711  10 PEQMGDQEIATWKKVIEEHGGEVVDEYSPRVTHVICESQDSPEYQ-----QALRDGKR--VVTAYWLNDVLKRGK 77
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 48-112 1.42e-03

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 37.90  E-value: 1.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549065    48 RRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLdwlkgQAVGDSSRFeILDISWLTACME 112
Cdd:cd17729  32 ERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVK-----QALKMPGIH-VVHPDWLWACAE 90
 
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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