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Conserved domains on  [gi|1039789899|ref|XP_017168281|]
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microcephalin isoform X19 [Mus musculus]

Protein Classification

BRCT domain-containing protein( domain architecture ID 13026374)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways; similar to vertebrate microcephalin implicated in chromosome condensation and DNA damage induced cellular responses

Gene Symbol:  MCPH1
Gene Ontology:  GO:0003677
PubMed:  14576433|10946236

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
14-92 1.69e-36

first (N-terminal) 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 first repeat.


:

Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 129.62  E-value: 1.69e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039789899  14 DVVAYVEVWSSKGtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALV 92
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
313-388 1.87e-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: 129.25  E-value: 1.87e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789899 313 RTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 388
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
414-490 2.16e-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: 96.15  E-value: 2.16e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789899 414 QQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARiqYLSEKWVLDSITQHKI 490
Cdd:cd17751     1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKP--SVSEKWLLDSITNHKL 75
 
Name Accession Description Interval E-value
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
14-92 1.69e-36

first (N-terminal) 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 first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 129.62  E-value: 1.69e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039789899  14 DVVAYVEVWSSKGtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALV 92
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
313-388 1.87e-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: 129.25  E-value: 1.87e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789899 313 RTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 388
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
414-490 2.16e-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: 96.15  E-value: 2.16e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789899 414 QQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARiqYLSEKWVLDSITQHKI 490
Cdd:cd17751     1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKP--SVSEKWLLDSITNHKL 75
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
15-81 2.32e-15

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 70.31  E-value: 2.32e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789899  15 VVAYVEVWSskgtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLW 81
Cdd:pfam12738   1 LVICVTGFD----GDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
417-496 2.66e-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: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899 417 QGTLFanQPKMF-IAPASSPPRAKLCELVLLCGGQVSPAPQLA-SLIIGPY----KGKKKARIQYLSEKWVLDSITQHKI 490
Cdd:pfam16589   1 LPNLF--EPLRFyINAIPSPSRSKLKRLIEANGGTVVDNINPAvYIVIAPYnktdKLAENTKLGVVSPQWIFDCVKKGKL 78

                  ....*.
gi 1039789899 491 CDFNNY 496
Cdd:pfam16589  79 LPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
11-85 1.16e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.52  E-value: 1.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789899   11 FLKDVVAYVevwSSKGTENYSRTFAKQLEDMGATVSKTLN-KQVTHVIFKDGYQST--WDKAQKTGAKLVSVLWVEKC 85
Cdd:smart00292   3 LFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT smart00292
breast cancer carboxy-terminal domain;
303-379 3.89e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 41.98  E-value: 3.89e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039789899  303 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCE-TTTHVLVGK-SARTLNVLMGIARGCWILSYEWVL 379
Cdd:smart00292   4 FKGKTF-------YITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGSpEGGKLELLKAIALGIPIVKEEWLL 75
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
303-382 4.70e-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: 36.12  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899 303 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLkGFSFAPEVCETTTHVLVGKsaRTLNVLMGIARGCWILSYEWVLLSL 382
Cdd:pfam00533   6 FSGKTF-------VITGLDGLERDELKELIEKL-GGKVTDSLSKKTTHVIVEA--RTKKYLKAKELGIPIVTEEWLLDCI 75
 
Name Accession Description Interval E-value
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
14-92 1.69e-36

first (N-terminal) 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 first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 129.62  E-value: 1.69e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039789899  14 DVVAYVEVWSSKGtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALV 92
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
313-388 1.87e-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: 129.25  E-value: 1.87e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789899 313 RTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 388
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
414-490 2.16e-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: 96.15  E-value: 2.16e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789899 414 QQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARiqYLSEKWVLDSITQHKI 490
Cdd:cd17751     1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKP--SVSEKWLLDSITNHKL 75
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
15-81 2.32e-15

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 70.31  E-value: 2.32e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789899  15 VVAYVEVWSskgtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLW 81
Cdd:pfam12738   1 LVICVTGFD----GDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
316-388 3.54e-12

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: 61.85  E-value: 3.54e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789899 316 VMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLV-----GKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 388
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVpaderGVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
314-381 1.44e-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: 56.99  E-value: 1.44e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789899 314 TLVMTSMPSEKQTLIIQVVSTLkGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLS 381
Cdd:cd00027     2 VICFSGLDDEEREELKKLIEAL-GGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
314-394 3.34e-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: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899 314 TLVMTSMpSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSA-----RTLNVLMGIARGCWILSYEWVLLSLELGHWI 388
Cdd:cd17735     2 SMVASGL-TPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAelvceRTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80

                  ....*.
gi 1039789899 389 SEEPFE 394
Cdd:cd17735    81 PEHDFE 86
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
32-85 8.82e-08

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: 49.28  E-value: 8.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039789899  32 RTFAKQLEDMGATVSKTLNKQVTHVIFK-DGYQSTWDKAQKTGAKLVSVLWVEKC 85
Cdd:cd00027    14 EELKKLIEALGGKVSESLSSKVTHLIAKsPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
417-496 2.66e-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: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899 417 QGTLFanQPKMF-IAPASSPPRAKLCELVLLCGGQVSPAPQLA-SLIIGPY----KGKKKARIQYLSEKWVLDSITQHKI 490
Cdd:pfam16589   1 LPNLF--EPLRFyINAIPSPSRSKLKRLIEANGGTVVDNINPAvYIVIAPYnktdKLAENTKLGVVSPQWIFDCVKKGKL 78

                  ....*.
gi 1039789899 491 CDFNNY 496
Cdd:pfam16589  79 LPLENY 84
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
11-85 2.88e-06

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: 44.98  E-value: 2.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789899  11 FLKDVVAYVevwssKGTENYSRTFAKQ-LEDMGATVSKTLNKQVTHVIFKDGyQSTWDKAQKTGAKLVSVLWVEKC 85
Cdd:pfam00533   5 LFSGKTFVI-----TGLDGLERDELKElIEKLGGKVTDSLSKKTTHVIVEAR-TKKYLKAKELGIPIVTEEWLLDC 74
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
317-385 5.94e-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: 5.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899 317 MTSMPSEKQTLIIQVVSTLKG-FSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELG 385
Cdd:cd17738     6 LSGFSEDEKKELISIIEKLGGkVLDSDEFDPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
BRCT smart00292
breast cancer carboxy-terminal domain;
11-85 1.16e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.52  E-value: 1.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789899   11 FLKDVVAYVevwSSKGTENYSRTFAKQLEDMGATVSKTLN-KQVTHVIFKDGYQST--WDKAQKTGAKLVSVLWVEKC 85
Cdd:smart00292   3 LFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT smart00292
breast cancer carboxy-terminal domain;
303-379 3.89e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 41.98  E-value: 3.89e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039789899  303 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCE-TTTHVLVGK-SARTLNVLMGIARGCWILSYEWVL 379
Cdd:smart00292   4 FKGKTF-------YITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGSpEGGKLELLKAIALGIPIVKEEWLL 75
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
28-85 1.36e-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: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899  28 ENYSRTFAKQL-EDMGATVSKTLNKQVTHVIF-KDGYQSTWDKAQKTGAKLVSVLWVEKC 85
Cdd:cd17729    29 IDPERSRLWKLaESLGAKVVTDLSPRTTHLVAaKLGTEKVKQALKMPGIHVVHPDWLWAC 88
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
32-97 3.47e-03

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: 36.57  E-value: 3.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789899  32 RTFAKQLEDMGATVSKTLNKQVTHVIFKdgYQSTWDKAQKTGAKLVSVLWVEKCRMAGALVDESLF 97
Cdd:pfam16589  21 SKLKRLIEANGGTVVDNINPAVYIVIAP--YNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLENY 84
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
38-93 4.53e-03

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


Pssm-ID: 349343  Cd Length: 81  Bit Score: 36.09  E-value: 4.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789899  38 LEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALVD 93
Cdd:cd17711    25 IEEHGGEVVDEYSPRVTHVICESQDSPEYQQALRDGKRVVTAYWLNDVLKRGKLLP 80
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
303-382 4.70e-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: 36.12  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789899 303 FKSCSFlqptrtlVMTSMPSEKQTLIIQVVSTLkGFSFAPEVCETTTHVLVGKsaRTLNVLMGIARGCWILSYEWVLLSL 382
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 ...
349-385 5.15e-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: 35.68  E-value: 5.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1039789899 349 THVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELG 385
Cdd:cd17743    34 THLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
42-93 5.54e-03

BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 36.11  E-value: 5.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039789899  42 GATVSKTLNKQVTHVIFKD-GYQSTW--DKAQKTGAKLVSVLWVEKCRMAGALVD 93
Cdd:cd17726    31 GGIISYIINKKCTHVVVNNaKALSSYkcRMAQKYGIPVVSLDYIWKCVEAGKLLD 85
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
346-388 8.91e-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: 34.90  E-value: 8.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1039789899 346 ETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWI 388
Cdd:cd17744    30 EDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
12-86 9.33e-03

sixth 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 sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 35.27  E-value: 9.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789899  12 LKDVVAYVevwsSKGTENYSRTFAKQLEDMGATVSKTLNKQVTHVIF--KDGYQSTWDKAQKT-GAKLVSVLWVEKCR 86
Cdd:cd17727     1 LKGVVICV----SKKLSKRQGELNKIAASLGAEYRWTYDESCTHFIYqgKANDTNREYKSAKEqGKFIVSPHWLYACK 74
 
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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