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Conserved domains on  [gi|63054850|ref|NP_004079|]
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DNA nucleotidylexotransferase isoform 1 [Homo sapiens]

Protein Classification

BRCT_DNTT and NT_POLXc domain-containing protein( domain architecture ID 13035160)

BRCT_DNTT and NT_POLXc domain-containing protein

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 ...
 163-508 3.37e-165

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


:

Pssm-ID: 214688  Cd Length: 334  Bit Score: 470.70  E-value: 3.37e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    163 NCNQIFTDAFDILAENCE-FRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    242 NDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWA 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    322 FLPDAFVTMTGGFRRGKKMGHDVDFLITSPGsteDEEQLLQKVMNLWekkglllyydLVESTFEKLRLPSRKVDALDHFQ 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPH---PAKEKELEVLDLL----------LLESTFEELQLPSIRVATLDHGQ 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    402 KCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTK 481
Cdd:smart00483 228 KKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDKTK 307

                          330       340
                   ....*....|....*....|....*..
gi 63054850    482 RIFLKAESEEEIFAHLGLDYIEPWERN 508
Cdd:smart00483 308 EKFLKVESEEDIFDHLGLPYIEPEERN 334
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 1.42e-55

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: 180.77  E-value: 1.42e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  31 KFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIEC 110
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                        90
                ....*....|....*
gi 63054850 111 IRAGKPVEMTGKHQL 125
Cdd:cd18443  81 MGAGKPVEIEKRHRL 95
 
Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 163-508 3.37e-165

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 470.70  E-value: 3.37e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    163 NCNQIFTDAFDILAENCE-FRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    242 NDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWA 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    322 FLPDAFVTMTGGFRRGKKMGHDVDFLITSPGsteDEEQLLQKVMNLWekkglllyydLVESTFEKLRLPSRKVDALDHFQ 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPH---PAKEKELEVLDLL----------LLESTFEELQLPSIRVATLDHGQ 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    402 KCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTK 481
Cdd:smart00483 228 KKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDKTK 307

                          330       340
                   ....*....|....*....|....*..
gi 63054850    482 RIFLKAESEEEIFAHLGLDYIEPWERN 508
Cdd:smart00483 308 EKFLKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 166-507 4.28e-101

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: 306.04  E-value: 4.28e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 166 QIFTDAFDILAENCEFRENED-SCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDe 244
Cdd:cd00141   1 QEIADILEELADLLELLGGNPfRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 245 RYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLP 324
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 325 DAFVTMTGGFRRGKKMGHDVDFLITSPGstEDEEQLLQKVMNLWEKKGLLLYydlvestfeklrlpsrkvDALDHFQKCF 404
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPD--ATSRGLLEKVVDALVELGFVTE------------------VLSKGDTKAS 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 405 LIFKLPrqrvdsdqsswqegKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYAThERKMILDNHALYDKTKRIF 484
Cdd:cd00141 220 GILKLP--------------GGWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAK-EKGLKLNEYGLFDGVDGER 284

                       330       340
                ....*....|....*....|...
gi 63054850 485 LKAESEEEIFAHLGLDYIEPWER 507
Cdd:cd00141 285 LPGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 1.42e-55

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: 180.77  E-value: 1.42e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  31 KFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIEC 110
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                        90
                ....*....|....*
gi 63054850 111 IRAGKPVEMTGKHQL 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 ...
 445-508 6.81e-24

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: 94.36  E-value: 6.81e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054850   445 ALLGWTGSRQFERDLRRYAtHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERN 508
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLA-KKKGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
328-504 1.29e-11

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 66.75  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 328 VTMTGGFRRGKKMGHDVDFLITSpgstEDEEqllqKVMNLwekkglLLYYDLVESTFEKlrlpsrkvdaldhfqkcflif 407
Cdd:COG1796 181 VEVAGSLRRRKETVGDIDILVAS----DDPE----AVMDA------FVKLPEVKEVLAK--------------------- 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 408 klprqrvdsdqsswqeGKTwKA-------IRVDLVLCPYERRAFALLGWTGSRQFERDLRRYAThERKMILDNHALYDKT 480
Cdd:COG1796 226 ----------------GDT-KAsvrlksgLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAK-ERGLKLNEYGLFDVG 287

                       170       180
                ....*....|....*....|....
gi 63054850 481 KRIfLKAESEEEIFAHLGLDYIEP 504
Cdd:COG1796 288 GER-IAGETEEEVYAALGLPYIPP 310
BRCT smart00292
breast cancer carboxy-terminal domain;
32-111 9.45e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 55.07  E-value: 9.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850     32 FQDLVVFILEKkMGTTRRAFLMELARRKGFRVENELS-DSVTHIVAENNSGSdVLEWLQAQKVQVssqpELLDVSWLIEC 110
Cdd:smart00292   4 FKGKTFYITGS-FDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGG-KLELLKAIALGI----PIVKEEWLLDC 77


                   .
gi 63054850    111 I 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 6.08e-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: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    27 PQDIKFQDLVVFILEKKMgtTRRAFLMELARRKGFRVENELSDSVTHIVAEnnsgSDVLEWLQAQKVQVssqpELLDVSW 106
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDG--LERDELKELIEKLGGKVTDSLSKKTTHVIVE----ARTKKYLKAKELGI----PIVTEEW 70


                  ....*
gi 63054850   107 LIECI 111
Cdd:pfam00533  71 LLDCI 75
 
Name Accession Description Interval E-value
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 163-508 3.37e-165

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 470.70  E-value: 3.37e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    163 NCNQIFTDAFDILAENCE-FRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    242 NDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWA 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    322 FLPDAFVTMTGGFRRGKKMGHDVDFLITSPGsteDEEQLLQKVMNLWekkglllyydLVESTFEKLRLPSRKVDALDHFQ 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPH---PAKEKELEVLDLL----------LLESTFEELQLPSIRVATLDHGQ 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    402 KCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTK 481
Cdd:smart00483 228 KKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFKLMLDGHELYDKTK 307

                          330       340
                   ....*....|....*....|....*..
gi 63054850    482 RIFLKAESEEEIFAHLGLDYIEPWERN 508
Cdd:smart00483 308 EKFLKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 166-507 4.28e-101

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: 306.04  E-value: 4.28e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 166 QIFTDAFDILAENCEFRENED-SCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDe 244
Cdd:cd00141   1 QEIADILEELADLLELLGGNPfRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 245 RYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLP 324
Cdd:cd00141  80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 325 DAFVTMTGGFRRGKKMGHDVDFLITSPGstEDEEQLLQKVMNLWEKKGLLLYydlvestfeklrlpsrkvDALDHFQKCF 404
Cdd:cd00141 160 VLQVEIAGSYRRGKETVGDIDILVTHPD--ATSRGLLEKVVDALVELGFVTE------------------VLSKGDTKAS 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 405 LIFKLPrqrvdsdqsswqegKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYAThERKMILDNHALYDKTKRIF 484
Cdd:cd00141 220 GILKLP--------------GGWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAK-EKGLKLNEYGLFDGVDGER 284

                       330       340
                ....*....|....*....|...
gi 63054850 485 LKAESEEEIFAHLGLDYIEPWER 507
Cdd:cd00141 285 LPGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 1.42e-55

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: 180.77  E-value: 1.42e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  31 KFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIEC 110
Cdd:cd18443   1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                        90
                ....*....|....*
gi 63054850 111 IRAGKPVEMTGKHQL 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 3.57e-50

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: 166.41  E-value: 3.57e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  31 KFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIEC 110
Cdd:cd17713   1 KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQGSSSPELLDISWFTES 80


                ....*..
gi 63054850 111 IRAGKPV 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 9.34e-33

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: 120.33  E-value: 9.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  31 KFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWL---QAQKVQVSSQPELLDVSWL 107
Cdd:cd18442   1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLerqMAAAPPACTPPALLDISWF 80

                        90
                ....*....|....*...
gi 63054850 108 IECIRAGKPVEMTGKHQL 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 ...
 445-508 6.81e-24

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: 94.36  E-value: 6.81e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054850   445 ALLGWTGSRQFERDLRRYAtHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERN 508
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 9.14e-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: 71.33  E-value: 9.14e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 63054850   250 KLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDL 299
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREKKTAKLTRQQQIGLKYYDDF 50
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 315-403 9.53e-12

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: 61.28  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850   315 VKEAVWAFLPDAFVTMTGGFRRGK-KMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVesTFEKLRLPSRK 393
Cdd:pfam01909   4 LREILKELFPVAEVVLFGSYARGTaLPGSDIDLLVVFPEPVEEERLLKLAKIIKELEELLGLEVDLV--TREKIEFPLVK 81

                          90
                  ....*....|
gi 63054850   394 VDALDHFQKC 403
Cdd:pfam01909  82 IDILEERILL 91
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
328-504 1.29e-11

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 66.75  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 328 VTMTGGFRRGKKMGHDVDFLITSpgstEDEEqllqKVMNLwekkglLLYYDLVESTFEKlrlpsrkvdaldhfqkcflif 407
Cdd:COG1796 181 VEVAGSLRRRKETVGDIDILVAS----DDPE----AVMDA------FVKLPEVKEVLAK--------------------- 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850 408 klprqrvdsdqsswqeGKTwKA-------IRVDLVLCPYERRAFALLGWTGSRQFERDLRRYAThERKMILDNHALYDKT 480
Cdd:COG1796 226 ----------------GDT-KAsvrlksgLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAK-ERGLKLNEYGLFDVG 287

                       170       180
                ....*....|....*....|....
gi 63054850 481 KRIfLKAESEEEIFAHLGLDYIEP 504
Cdd:COG1796 288 GER-IAGETEEEVYAALGLPYIPP 310
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 305-374 7.28e-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: 56.42  E-value: 7.28e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054850   305 RAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQ--LLQKVMNLWEKKGLL 374
Cdd:pfam14792   4 REEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESELkgLLDRLVARLKKSGFL 75
BRCT smart00292
breast cancer carboxy-terminal domain;
32-111 9.45e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 55.07  E-value: 9.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850     32 FQDLVVFILEKkMGTTRRAFLMELARRKGFRVENELS-DSVTHIVAENNSGSdVLEWLQAQKVQVssqpELLDVSWLIEC 110
Cdd:smart00292   4 FKGKTFYITGS-FDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGG-KLELLKAIALGI----PIVKEEWLLDC 77


                   .
gi 63054850    111 I 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 6.08e-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: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850    27 PQDIKFQDLVVFILEKKMgtTRRAFLMELARRKGFRVENELSDSVTHIVAEnnsgSDVLEWLQAQKVQVssqpELLDVSW 106
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDG--LERDELKELIEKLGGKVTDSLSKKTTHVIVE----ARTKKYLKAKELGI----PIVTEEW 70


                  ....*
gi 63054850   107 LIECI 111
Cdd:pfam00533  71 LLDCI 75
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 48-110 5.04e-07

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: 46.97  E-value: 5.04e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054850  48 RRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVssqpelLDVSWLIEC 110
Cdd:cd00027  12 EREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPI------VSPEWLLDC 68
BRCT_TopBP1_rpt3 cd17718
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 52-115 2.56e-06

third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain.


Pssm-ID: 349350  Cd Length: 83  Bit Score: 45.28  E-value: 2.56e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054850  52 LMELARR-----KGFRvENELSDSVTHIVAENNSGSDVLEWLQAQkvqvsSQPELLDVSWLIECIRAGK 115
Cdd:cd17718  21 ELDKLRRiinagGGTR-FNQLNESVTHVVVGESSEELLKELAKLA-----GRPHVVTPSWLLECFKQGK 83
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 32-115 1.23e-05

BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 43.71  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  32 FQDLVVFILekkmGTT--RRAFLMELARRKGFRVENELS-DSVTHIVAENNSGSDVLEWLQAQKVQVSSqPElldvsWLI 108
Cdd:cd17719   2 FKGVVIYVN----GYTdpSADELKRLILLHGGQYEHYYSrSRVTHIIATNLPGSKIKKLKKARNYKVVR-PE-----WIV 71


                ....*..
gi 63054850 109 ECIRAGK 115
Cdd:cd17719  72 DSIKAGR 78
HHH_8 pfam14716
Helix-hairpin-helix domain;
165-220 2.17e-05

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 42.11  E-value: 2.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054850   165 NQIFTDAFDILAENCEF-RENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSK 220
Cdd:pfam14716   1 NQEIADALEELADLLELkGEDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKK 57
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 36-115 9.81e-04

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: 38.01  E-value: 9.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054850  36 VVFILE--KKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSsqpelldVSWLIECIRA 113
Cdd:cd17711   3 VFFIADypEQMGDQEIATWKKVIEEHGGEVVDEYSPRVTHVICESQDSPEYQQALRDGKRVVT-------AYWLNDVLKR 75


                ..
gi 63054850 114 GK 115
Cdd:cd17711  76 GK 77
BRCT_PAXIP1_rpt1 cd17714
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; ...
 54-115 3.55e-03

first (N-terminal) 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 first BRCT domain.


Pssm-ID: 349346  Cd Length: 76  Bit Score: 36.53  E-value: 3.55e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054850  54 ELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQA-QKVQVSSQpelldvsWLIECIRAGK 115
Cdd:cd17714  18 QLLKNGGAKEVSYLSDMATHVIVDDNDNPEVGEARDLfELPVVTSS-------WVILSIKAGK 73
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 52-117 7.33e-03

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: 35.65  E-value: 7.33e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054850  52 LMELARRKGFRVENELSDSVTHIVAENNSGSDV---LEWLQAqkvqVSSQPELLDVSWLIECIRAGKPV 117
Cdd:cd17734  16 LEKLAQLLKAKVVTEFSPEVTHVVVPADERGVCprtMKYLMG----ILAGKWIVSFEWVEACLKAKKLV 80
 
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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