NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568953307|ref|XP_006508853|]
View 

microcephalin isoform X15 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 29-402 4.32e-169

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


:

Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 488.46  E-value: 4.32e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307   29 ESFASGSHSSFGD-----SCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQK 103
Cdd:pfam12258   1 ESFAGGLHSSFDDlcgnsECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  104 DATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRL-GPKNSSAKRKRAA-DLGSSPKGKL-KKRYKRKSALA- 179
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHsRPKSSSAKRKRTSeDLNSPPKEKLkKKRSSRKSAMPr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  180 IQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCI 259
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  260 GEKHRsISSISDLISKSASSLEKPVKEEVNTASTCLLLVETS-ANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHI 338
Cdd:pfam12258 241 GKKPR-SVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSEGTPaAEETPGCCRQAGPQKREDAGPEGNSHSHTTDEPALPS 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953307  339 ------TPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHI-CNLSLGEDCNVEKSVEEKENIATGYS 402
Cdd:pfam12258 320 ghhgdlTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSdYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 475-550 1.42e-36

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


:

Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 131.17  E-value: 1.42e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953307 475 RTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 550
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 576-652 3.06e-24

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


:

Pssm-ID: 349382  Cd Length: 75  Bit Score: 96.53  E-value: 3.06e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953307 576 QQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARiqYLSEKWVLDSITQHKI 652
Cdd:cd17751    1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKP--SVSEKWLLDSITNHKL 75
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 29-402 4.32e-169

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 488.46  E-value: 4.32e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307   29 ESFASGSHSSFGD-----SCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQK 103
Cdd:pfam12258   1 ESFAGGLHSSFDDlcgnsECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  104 DATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRL-GPKNSSAKRKRAA-DLGSSPKGKL-KKRYKRKSALA- 179
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHsRPKSSSAKRKRTSeDLNSPPKEKLkKKRSSRKSAMPr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  180 IQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCI 259
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  260 GEKHRsISSISDLISKSASSLEKPVKEEVNTASTCLLLVETS-ANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHI 338
Cdd:pfam12258 241 GKKPR-SVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSEGTPaAEETPGCCRQAGPQKREDAGPEGNSHSHTTDEPALPS 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953307  339 ------TPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHI-CNLSLGEDCNVEKSVEEKENIATGYS 402
Cdd:pfam12258 320 ghhgdlTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSdYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 475-550 1.42e-36

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 131.17  E-value: 1.42e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953307 475 RTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 550
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 576-652 3.06e-24

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


Pssm-ID: 349382  Cd Length: 75  Bit Score: 96.53  E-value: 3.06e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953307 576 QQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARiqYLSEKWVLDSITQHKI 652
Cdd:cd17751    1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKP--SVSEKWLLDSITNHKL 75
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 579-658 3.58e-06

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 45.43  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  579 QGTLFanQPKMF-IAPASSPPRAKLCELVLLCGGQVSPAPQLA-SLIIGPY----KGKKKARIQYLSEKWVLDSITQHKI 652
Cdd:pfam16589   1 LPNLF--EPLRFyINAIPSPSRSKLKRLIEANGGTVVDNINPAvYIVIAPYnktdKLAENTKLGVVSPQWIFDCVKKGKL 78


                  ....*.
gi 568953307  653 CDFNNY 658
Cdd:pfam16589  79 LPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
465-541 3.83e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.36  E-value: 3.83e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953307   465 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCE-TTTHVLVGK-SARTLNVLMGIARGCWILSYEWVL 541
Cdd:smart00292   4 FKGKTF-------YITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGSpEGGKLELLKAIALGIPIVKEEWLL 75
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 465-544 3.86e-03

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: 36.50  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  465 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLkGFSFAPEVCETTTHVLVGKsaRTLNVLMGIARGCWILSYEWVLLSL 544
Cdd:pfam00533   6 FSGKTF-------VITGLDGLERDELKELIEKL-GGKVTDSLSKKTTHVIVEA--RTKKYLKAKELGIPIVTEEWLLDCI 75
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 29-402 4.32e-169

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 488.46  E-value: 4.32e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307   29 ESFASGSHSSFGD-----SCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQK 103
Cdd:pfam12258   1 ESFAGGLHSSFDDlcgnsECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  104 DATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRL-GPKNSSAKRKRAA-DLGSSPKGKL-KKRYKRKSALA- 179
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHsRPKSSSAKRKRTSeDLNSPPKEKLkKKRSSRKSAMPr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  180 IQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCI 259
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  260 GEKHRsISSISDLISKSASSLEKPVKEEVNTASTCLLLVETS-ANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHI 338
Cdd:pfam12258 241 GKKPR-SVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSEGTPaAEETPGCCRQAGPQKREDAGPEGNSHSHTTDEPALPS 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953307  339 ------TPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHI-CNLSLGEDCNVEKSVEEKENIATGYS 402
Cdd:pfam12258 320 ghhgdlTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSdYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 475-550 1.42e-36

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 131.17  E-value: 1.42e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953307 475 RTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 550
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 576-652 3.06e-24

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


Pssm-ID: 349382  Cd Length: 75  Bit Score: 96.53  E-value: 3.06e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953307 576 QQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARiqYLSEKWVLDSITQHKI 652
Cdd:cd17751    1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKP--SVSEKWLLDSITNHKL 75
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 478-550 4.15e-13

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: 64.93  E-value: 4.15e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953307 478 VMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLV-----GKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 550
Cdd:cd17734    3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVpaderGVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 476-543 1.02e-10

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: 57.76  E-value: 1.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953307 476 TLVMTSMPSEKQTLIIQVVSTLkGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLS 543
Cdd:cd00027    2 VICFSGLDDEEREELKKLIEAL-GGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 476-556 4.52e-10

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 56.97  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307 476 TLVMTSMpSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSA-----RTLNVLMGIARGCWILSYEWVLLSLELGHWI 550
Cdd:cd17735    2 SMVASGL-TPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAelvceRTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80


                 ....*.
gi 568953307 551 SEEPFE 556
Cdd:cd17735   81 PEHDFE 86
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 579-658 3.58e-06

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 45.43  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  579 QGTLFanQPKMF-IAPASSPPRAKLCELVLLCGGQVSPAPQLA-SLIIGPY----KGKKKARIQYLSEKWVLDSITQHKI 652
Cdd:pfam16589   1 LPNLF--EPLRFyINAIPSPSRSKLKRLIEANGGTVVDNINPAvYIVIAPYnktdKLAENTKLGVVSPQWIFDCVKKGKL 78


                  ....*.
gi 568953307  653 CDFNNY 658
Cdd:pfam16589  79 LPLENY 84
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 479-547 7.16e-06

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; 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 seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 44.10  E-value: 7.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307 479 MTSMPSEKQTLIIQVVSTLKG-FSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELG 547
Cdd:cd17738    6 LSGFSEDEKKELISIIEKLGGkVLDSDEFDPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
BRCT smart00292
breast cancer carboxy-terminal domain;
465-541 3.83e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.36  E-value: 3.83e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953307   465 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCE-TTTHVLVGK-SARTLNVLMGIARGCWILSYEWVL 541
Cdd:smart00292   4 FKGKTF-------YITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGSpEGGKLELLKAIALGIPIVKEEWLL 75
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 465-544 3.86e-03

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: 36.50  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  465 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLkGFSFAPEVCETTTHVLVGKsaRTLNVLMGIARGCWILSYEWVLLSL 544
Cdd:pfam00533   6 FSGKTF-------VITGLDGLERDELKELIEKL-GGKVTDSLSKKTTHVIVEA--RTKKYLKAKELGIPIVTEEWLLDCI 75
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 511-547 5.56e-03

fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contain six BRCT domains. This family corresponds to the fifth one.


Pssm-ID: 349374  Cd Length: 70  Bit Score: 36.07  E-value: 5.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568953307 511 THVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELG 547
Cdd:cd17743   34 THLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 479-552 8.16e-03

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349381  Cd Length: 81  Bit Score: 35.95  E-value: 8.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953307 479 MTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWISE 552
Cdd:cd17750    8 LTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 508-550 9.07e-03

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375 [Multi-domain]  Cd Length: 72  Bit Score: 35.29  E-value: 9.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568953307 508 ETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 550
Cdd:cd17744   30 EDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
Herpes_LMP1 pfam05297
Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane ...
 297-396 9.57e-03

Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane protein 1 or LMP1s mostly from Epstein-Barr virus. LMP1 of EBV is a 62-65 kDa plasma membrane protein possessing six membrane spanning regions, a short cytoplasmic N-terminus and a long cytoplasmic carboxy tail of 200 amino acids. EBV latent membrane protein 1 (LMP1) is essential for EBV-mediated transformation and has been associated with several cases of malignancies. EBV-like viruses in Cynomolgus monkeys (Macaca fascicularis) have been associated with high lymphoma rates in immunosuppressed monkeys


Pssm-ID: 283060  Cd Length: 386  Bit Score: 38.86  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953307  297 LVETSANDSPGLCS----------QPGPQLRDDTGPEGSSHPD-TLSSSAHHITPLKGNSTETRDPGDGKGSPKEGSTPP 365
Cdd:pfam05297 226 LLVSGAGDGPPLCSqnlgapgggpDNGPQDPDNTDDNGPQDPDnTDDNGPHDPLPQDPDNTDDNGPQDPDNTADNGPHDP 305

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568953307  366 ASASPEDevhicnlSLGEDCNVEKSVEEKEN 396
Cdd:pfam05297 306 LPHNPSD-------SAGNDGGPPNLTEEVEN 329
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH