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Conserved domains on  [gi|270047576|pdb|2WT8|C]
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Chain C, MICROCEPHALIN

Protein Classification

BRCT domain-containing protein( domain architecture ID 13026369)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways; similar to Schizosaccharomyces pombe meiotically up-regulated gene 176 protein that has a role in meiosis

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 ...
10-88 1.93e-37

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: 120.38  E-value: 1.93e-37
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WT8_C      10 DVVAYVEVWSSNGtENYSKTFTTQLVD*GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHI 88
Cdd:cd17716  1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
 
Name Accession Description Interval E-value
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
10-88 1.93e-37

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: 120.38  E-value: 1.93e-37
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WT8_C      10 DVVAYVEVWSSNGtENYSKTFTTQLVD*GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHI 88
Cdd:cd17716  1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
15-77 8.21e-17

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: 68.00  E-value: 8.21e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
2WT8_C        15 VEVWSSNGTENYSKTFTTQLVD*GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLW 77
Cdd:pfam12738  1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT smart00292
breast cancer carboxy-terminal domain;
6-81 8.19e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.75  E-value: 8.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WT8_C          6 PILKDVVAYVevwSSNGTENYSKTFTTQLVD*GAKVSKTFN-KQVTHVIFKDGYQST--WDKAQKRGVKLVSVLWVEKC 81
Cdd:smart00292  2 KLFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
 
Name Accession Description Interval E-value
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
10-88 1.93e-37

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: 120.38  E-value: 1.93e-37
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WT8_C      10 DVVAYVEVWSSNGtENYSKTFTTQLVD*GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHI 88
Cdd:cd17716  1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
15-77 8.21e-17

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: 68.00  E-value: 8.21e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
2WT8_C        15 VEVWSSNGTENYSKTFTTQLVD*GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLW 77
Cdd:pfam12738  1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
20-81 4.09e-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: 45.82  E-value: 4.09e-08
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|...
2WT8_C      20 SNGTENYSKTFTTQLVD*GAKVSKTFNKQVTHVIFK-DGYQSTWDKAQKRGVKLVSVLWVEKC 81
Cdd:cd00027  6 SGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKsPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT smart00292
breast cancer carboxy-terminal domain;
6-81 8.19e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.75  E-value: 8.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WT8_C          6 PILKDVVAYVevwSSNGTENYSKTFTTQLVD*GAKVSKTFN-KQVTHVIFKDGYQST--WDKAQKRGVKLVSVLWVEKC 81
Cdd:smart00292  2 KLFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
6-81 2.79e-05

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: 38.81  E-value: 2.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2WT8_C         6 PILKDVVAYVevwssNGTENYSKTFTTQLV-D*GAKVSKTFNKQVTHVIFKDGyQSTWDKAQKRGVKLVSVLWVEKC 81
Cdd:pfam00533  4 KLFSGKTFVI-----TGLDGLERDELKELIeKLGGKVTDSLSKKTTHVIVEAR-TKKYLKAKELGIPIVTEEWLLDC 74
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
38-90 3.46e-05

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: 39.05  E-value: 3.46e-05
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|....
2WT8_C      38 GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKR-GVKLVSVLWVEKCRTAGAHIDE 90
Cdd:cd17729 44 GAKVVTDLSPRTTHLVAAKLGTEKVKQALKMpGIHVVHPDWLWACAERWERVDE 97
BRCT_BRC1_like_rpt1 cd18435
first (N-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) ...
7-93 4.08e-04

first (N-terminal) 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. Members in this family contains six BRCT domains. This family corresponds to the fourth repeat.


Pssm-ID: 349388  Cd Length: 107  Bit Score: 36.54  E-value: 4.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WT8_C        7 ILKDVVAYVEV---WSSNGTENYSKTFTTQ---------LVD*GAKV-SKTFNKQVTHVIFKD----GYQSTWDK-AQKR 68
Cdd:cd18435   1 IFKHLAFYLDSpanAQRHGMARPKYEAAITksfeeveklFIDNGGKIlDLPYDPKLTHVILDDfdspRVVELMKRtGKPR 80
                        90       100
                ....*....|....*....|....*
2WT8_C       69 GVKLVSVLWVEKCRTAGAHIDESLF 93
Cdd:cd18435  81 RLHLVKTKWIEDCVDENTLLDEEEY 105
BRCT_DNA_ligase_IV_rpt2 cd17717
second BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ...
38-79 8.70e-04

second BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the second one.


Pssm-ID: 349349  Cd Length: 88  Bit Score: 35.11  E-value: 8.70e-04
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
2WT8_C      38 GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGV-----KLVSVLWVE 79
Cdd:cd17717 37 GGKVVSELAEGISHVVVDSDHSRVVDFKELRRLlkkkfKIVSESWVT 83
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
35-82 1.23e-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: 34.49  E-value: 1.23e-03
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|.
2WT8_C      35 VD*GAKVSKTFNKQVTHVIFK---DGYQSTWDKAQKRGVKLVSVLWVEKCR 82
Cdd:cd17727 24 ASLGAEYRWTYDESCTHFIYQgkaNDTNREYKSAKEQGKFIVSPHWLYACK 74
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
38-93 4.99e-03

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: 33.47  E-value: 4.99e-03
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|..
2WT8_C      38 GAKVSKTFNKQVTHVIFKDGYQSTWDKAQK-----RGVK-LVSVLWVEKCRTAGAHIDESLF 93
Cdd:cd17735 24 GSTLTSQFTEETTHVIMKTDAELVCERTLKyflgiAGRKwVVSYQWITQSIKEGKILPEHDF 85
 
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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