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Conserved domains on  [gi|1907132104|ref|XP_036017403|]
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DNA nucleotidylexotransferase isoform X2 [Mus musculus]

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 ...
 163-508 2.19e-173

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


:

Pssm-ID: 214688  Cd Length: 334  Bit Score: 491.50  E-value: 2.19e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  163 NYNQLFTDALDILAENDE-LRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  242 NDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVT 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  322 FLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEdeeqQLLHKVTDFWKqqglllycdiLESTFEKFKQPSRKVDALDHF 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAK----EKELEVLDLLL----------LESTFEELQLPSIRVATLDHG 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  402 QKCFLILKLDHGRVHSEKSGQQEGKGWKAIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYATHERKMMLDNHALYDRT 480
Cdd:smart00483 227 QKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKqFNRDLRRYATSKFKLMLDGHELYDKT 306

                          330       340
                   ....*....|....*....|....*...
gi 1907132104  481 KRVFLEAESEEEIFAHLGLDYIEPWERN 508
Cdd:smart00483 307 KEKFLKVESEEDIFDHLGLPYIEPEERN 334
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 31-125 1.78e-53

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: 175.38  E-value: 1.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  31 RFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIEC 110
Cdd:cd18443     1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                          90
                  ....*....|....*
gi 1907132104 111 MGAGKPVEMMGRHQL 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 2.19e-173

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 491.50  E-value: 2.19e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  163 NYNQLFTDALDILAENDE-LRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  242 NDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVT 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  322 FLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEdeeqQLLHKVTDFWKqqglllycdiLESTFEKFKQPSRKVDALDHF 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAK----EKELEVLDLLL----------LESTFEELQLPSIRVATLDHG 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  402 QKCFLILKLDHGRVHSEKSGQQEGKGWKAIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYATHERKMMLDNHALYDRT 480
Cdd:smart00483 227 QKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKqFNRDLRRYATSKFKLMLDGHELYDKT 306

                          330       340
                   ....*....|....*....|....*...
gi 1907132104  481 KRVFLEAESEEEIFAHLGLDYIEPWERN 508
Cdd:smart00483 307 KEKFLKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 166-507 7.01e-117

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: 346.49  E-value: 7.01e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 166 QLFTDALDILAENDELR-ENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDe 244
Cdd:cd00141     1 QEIADILEELADLLELLgGNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 245 RYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVTFLP 324
Cdd:cd00141    80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 325 DALVTMTGGFRRGKMTGHDVDFLITSPEATedeEQQLLHKVTDFWKQQGLLLYcdilestfekfkqpsrkvDALDHFQKC 404
Cdd:cd00141   160 VLQVEIAGSYRRGKETVGDIDILVTHPDAT---SRGLLEKVVDALVELGFVTE------------------VLSKGDTKA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 405 FLILKLDHgrvhseksgqqegkGWKAIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYAThERKMMLDNHALYDRTKRV 483
Cdd:cd00141   219 SGILKLPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKqFNRALRRLAK-EKGLKLNEYGLFDGVDGE 283

                         330       340
                  ....*....|....*....|....
gi 1907132104 484 FLEAESEEEIFAHLGLDYIEPWER 507
Cdd:cd00141   284 RLPGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 1.78e-53

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: 175.38  E-value: 1.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  31 RFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIEC 110
Cdd:cd18443     1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                          90
                  ....*....|....*
gi 1907132104 111 MGAGKPVEMMGRHQL 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 ...
 446-508 1.26e-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: 90.89  E-value: 1.26e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132104 446 ALLGWTGSR-FERDLRRYAtHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYIEPWERN 508
Cdd:pfam14791   1 ALLYFTGSKeFNRDLRLLA-KKKGLKLNEYGLFDLKDGELLEGETEEDIFEALGLPYIPPELRE 63
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
190-504 8.29e-10

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 60.98  E-value: 8.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 190 AFMRASSVLKSLPFPITSM---KDTEGIPCLGDKVKSIIEGIIEDGESSEAkavlndERYKS------FKLfTSVFGVGL 260
Cdd:COG1796    29 AYRRAARAIENLPEDIEELvaeGDLTEIPGIGKAIAAKIEELLETGRLEEL------EELREevppglLEL-LRIPGLGP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 261 KTAEKWFR------------------------MGFRTLSKIqsDKSLRFTQMQKAGFLYYEdlvscvNRPEAEAVSMLVK 316
Cdd:COG1796   102 KKVKKLYEelgitsleeleaaaeegrirelpgFGEKTEENI--LKGIELLRKRGGRFLLGE------ALPLAEEILAYLR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 317 --EAVVTflpdalVTMTGGFRRGKMTGHDVDFLItspeATEDEEqqllhKVTDFWKQQGLLLycDILES--Tfekfkqps 392
Cdd:COG1796   174 alPGVER------VEVAGSLRRRKETVGDIDILV----ASDDPE-----AVMDAFVKLPEVK--EVLAKgdT-------- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 393 rkvdaldhfqKCFLILKldhgrvhsekSGqqegkgwkaIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYAThERKMML 471
Cdd:COG1796   229 ----------KASVRLK----------SG---------LQVDLRVVPPESFGAALQYFTGSKeHNVALRQLAK-ERGLKL 278

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1907132104 472 DNHALYDRTKRVfLEAESEEEIFAHLGLDYIEP 504
Cdd:COG1796   279 NEYGLFDVGGER-IAGETEEEVYAALGLPYIPP 310
BRCT smart00292
breast cancer carboxy-terminal domain;
32-111 8.28e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.38  E-value: 8.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104   32 FRDLVLFILEKkMGTTRRAFLMELARRKGFRVENELS-DSVTHIVAENNSGSDVLEWLQLQNikassELELLDISWLIEC 110
Cdd:smart00292   4 FKGKTFYITGS-FDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELLKAIAL-----GIPIVKEEWLLDC 77


                   .
gi 1907132104  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 8.30e-07

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: 46.52  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  27 PYDIRFRDLVLFILEKKMgtTRRAFLMELARRKGFRVENELSDSVTHIVAEnnsgsdvlEWLQLQNIKASSELELLDISW 106
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDG--LERDELKELIEKLGGKVTDSLSKKTTHVIVE--------ARTKKYLKAKELGIPIVTEEW 70


                  ....*
gi 1907132104 107 LIECM 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 2.19e-173

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 491.50  E-value: 2.19e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  163 NYNQLFTDALDILAENDE-LRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVL 241
Cdd:smart00483   1 NLNRGIIDALEILAENYEvFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  242 NDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVT 321
Cdd:smart00483  81 NDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKELKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  322 FLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEdeeqQLLHKVTDFWKqqglllycdiLESTFEKFKQPSRKVDALDHF 401
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAK----EKELEVLDLLL----------LESTFEELQLPSIRVATLDHG 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  402 QKCFLILKLDHGRVHSEKSGQQEGKGWKAIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYATHERKMMLDNHALYDRT 480
Cdd:smart00483 227 QKKFMILKLSPSREDKEKSGKPDEKGWKARRVDIVLCPEDQYPTALLGWTGSKqFNRDLRRYATSKFKLMLDGHELYDKT 306

                          330       340
                   ....*....|....*....|....*...
gi 1907132104  481 KRVFLEAESEEEIFAHLGLDYIEPWERN 508
Cdd:smart00483 307 KEKFLKVESEEDIFDHLGLPYIEPEERN 334
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 166-507 7.01e-117

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: 346.49  E-value: 7.01e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 166 QLFTDALDILAENDELR-ENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDe 244
Cdd:cd00141     1 QEIADILEELADLLELLgGNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELRED- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 245 RYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVTFLP 324
Cdd:cd00141    80 VPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 325 DALVTMTGGFRRGKMTGHDVDFLITSPEATedeEQQLLHKVTDFWKQQGLLLYcdilestfekfkqpsrkvDALDHFQKC 404
Cdd:cd00141   160 VLQVEIAGSYRRGKETVGDIDILVTHPDAT---SRGLLEKVVDALVELGFVTE------------------VLSKGDTKA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 405 FLILKLDHgrvhseksgqqegkGWKAIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYAThERKMMLDNHALYDRTKRV 483
Cdd:cd00141   219 SGILKLPG--------------GWKGRRVDLRVVPPEEFGAALLYFTGSKqFNRALRRLAK-EKGLKLNEYGLFDGVDGE 283

                         330       340
                  ....*....|....*....|....
gi 1907132104 484 FLEAESEEEIFAHLGLDYIEPWER 507
Cdd:cd00141   284 RLPGETEEEIFEALGLPYIEPELR 307
BRCT_DNTT cd18443
BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins; DNTT (EC 2.7.7.31), ...
 31-125 1.78e-53

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: 175.38  E-value: 1.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  31 RFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIEC 110
Cdd:cd18443     1 KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLELLDISWFTEC 80

                          90
                  ....*....|....*
gi 1907132104 111 MGAGKPVEMMGRHQL 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 4.52e-49

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: 163.33  E-value: 4.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  31 RFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIEC 110
Cdd:cd17713     1 KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQGSSSPELLDISWFTES 80


                  ....*..
gi 1907132104 111 MGAGKPV 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 1.10e-34

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: 125.34  E-value: 1.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  31 RFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQN---IKASSELELLDISWL 107
Cdd:cd18442     1 RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMaaaPPACTPPALLDISWF 80

                          90
                  ....*....|....*...
gi 1907132104 108 IECMGAGKPVEMMGRHQL 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 ...
 446-508 1.26e-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: 90.89  E-value: 1.26e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132104 446 ALLGWTGSR-FERDLRRYAtHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYIEPWERN 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 2.16e-15

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: 70.17  E-value: 2.16e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907132104 250 KLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDL 299
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREKKTAKLTRQQQIGLKYYDDF 50
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 313-404 2.48e-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: 62.82  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 313 MLVKEAVVTFLPDALVTMTGGFRRGKMT-GHDVDFLITSPEATEDEEQQLLHKVtDFWKQQGLLLYCDIleSTFEKFKQP 391
Cdd:pfam01909   2 RKLREILKELFPVAEVVLFGSYARGTALpGSDIDLLVVFPEPVEEERLLKLAKI-IKELEELLGLEVDL--VTREKIEFP 78

                          90
                  ....*....|...
gi 1907132104 392 SRKVDALDHFQKC 404
Cdd:pfam01909  79 LVKIDILEERILL 91
HHH_8 pfam14716
Helix-hairpin-helix domain;
165-230 9.32e-11

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 57.51  E-value: 9.32e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132104 165 NQLFTDALDILAENDEL-RENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIE 230
Cdd:pfam14716   1 NQEIADALEELADLLELkGEDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 305-375 2.57e-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: 57.58  E-value: 2.57e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907132104 305 RPEAEAVSMLVKEAVVTFLPDALVTMTGGFRRGKMTGHDVDFLITSPEAT-EDEEQQLLHKVTDFWKQQGLL 375
Cdd:pfam14792   4 REEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTsESELKGLLDRLVARLKKSGFL 75
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
190-504 8.29e-10

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 60.98  E-value: 8.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 190 AFMRASSVLKSLPFPITSM---KDTEGIPCLGDKVKSIIEGIIEDGESSEAkavlndERYKS------FKLfTSVFGVGL 260
Cdd:COG1796    29 AYRRAARAIENLPEDIEELvaeGDLTEIPGIGKAIAAKIEELLETGRLEEL------EELREevppglLEL-LRIPGLGP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 261 KTAEKWFR------------------------MGFRTLSKIqsDKSLRFTQMQKAGFLYYEdlvscvNRPEAEAVSMLVK 316
Cdd:COG1796   102 KKVKKLYEelgitsleeleaaaeegrirelpgFGEKTEENI--LKGIELLRKRGGRFLLGE------ALPLAEEILAYLR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 317 --EAVVTflpdalVTMTGGFRRGKMTGHDVDFLItspeATEDEEqqllhKVTDFWKQQGLLLycDILES--Tfekfkqps 392
Cdd:COG1796   174 alPGVER------VEVAGSLRRRKETVGDIDILV----ASDDPE-----AVMDAFVKLPEVK--EVLAKgdT-------- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104 393 rkvdaldhfqKCFLILKldhgrvhsekSGqqegkgwkaIRVDLVMCPYDRRAFALLGWTGSR-FERDLRRYAThERKMML 471
Cdd:COG1796   229 ----------KASVRLK----------SG---------LQVDLRVVPPESFGAALQYFTGSKeHNVALRQLAK-ERGLKL 278

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1907132104 472 DNHALYDRTKRVfLEAESEEEIFAHLGLDYIEP 504
Cdd:COG1796   279 NEYGLFDVGGER-IAGETEEEVYAALGLPYIPP 310
BRCT smart00292
breast cancer carboxy-terminal domain;
32-111 8.28e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.38  E-value: 8.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104   32 FRDLVLFILEKkMGTTRRAFLMELARRKGFRVENELS-DSVTHIVAENNSGSDVLEWLQLQNikassELELLDISWLIEC 110
Cdd:smart00292   4 FKGKTFYITGS-FDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELLKAIAL-----GIPIVKEEWLLDC 77


                   .
gi 1907132104  111 M 111
Cdd:smart00292  78 L 78
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 48-110 3.41e-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: 47.36  E-value: 3.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907132104  48 RRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKasseleLLDISWLIEC 110
Cdd:cd00027    12 EREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIP------IVSPEWLLDC 68
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 27-111 8.30e-07

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: 46.52  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  27 PYDIRFRDLVLFILEKKMgtTRRAFLMELARRKGFRVENELSDSVTHIVAEnnsgsdvlEWLQLQNIKASSELELLDISW 106
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDG--LERDELKELIEKLGGKVTDSLSKKTTHVIVE--------ARTKKYLKAKELGIPIVTEEW 70


                  ....*
gi 1907132104 107 LIECM 111
Cdd:pfam00533  71 LLDCI 75
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 32-115 1.66e-03

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: 37.55  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  32 FRDLVLFILekkmGTT--RRAFLMELARRKGFRVENELS-DSVTHIVAENNSGSDVLEWLQLQNIKASSElelldiSWLI 108
Cdd:cd17719     2 FKGVVIYVN----GYTdpSADELKRLILLHGGQYEHYYSrSRVTHIIATNLPGSKIKKLKKARNYKVVRP------EWIV 71


                  ....*..
gi 1907132104 109 ECMGAGK 115
Cdd:cd17719    72 DSIKAGR 78
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 48-111 1.80e-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: 1.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132104  48 RRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKasseleLLDISWLIECM 111
Cdd:cd17729    32 ERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPGIH------VVHPDWLWACA 89
BRCT_TopBP1_rpt3 cd17718
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 52-115 5.53e-03

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: 36.03  E-value: 5.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132104  52 LMELARR-----KGFRvENELSDSVTHIVAennsgSDVLEWLqLQNIKASSEL-ELLDISWLIECMGAGK 115
Cdd:cd17718    21 ELDKLRRiinagGGTR-FNQLNESVTHVVV-----GESSEEL-LKELAKLAGRpHVVTPSWLLECFKQGK 83
 
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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