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Conserved domains on  [gi|767950164|ref|XP_011533059|]
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microcephalin isoform X6 [Homo sapiens]

Protein Classification

BRCT domain-containing protein( domain architecture ID 13026448)

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

Graphical summary

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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 ...
 225-607 0e+00

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: 613.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  225 EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQR 304
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  305 NIAGKVVTPDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPR 384
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHSRPKSSSAKRKRTSEDLNSPPKEKLKKKRSSRKSAMPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  385 LQLCRSEDRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCV 464
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  465 GKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTS----APEEALRCCRQAG---KEDACPEGNGFSYTIEDPALPKG 537
Cdd:pfam12258 241 GKKPRSVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSegtpAAEETPGCCRQAGpqkREDAGPEGNSHSHTTDEPALPSG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  538 HDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYS 607
Cdd:pfam12258 321 HHGDLTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSDYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 648-723 8.14e-39

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: 138.11  E-value: 8.14e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950164 648 RTLVMTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWI 723
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 8-86 1.11e-38

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: 137.71  E-value: 1.11e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950164   8 DVVAYVEVWSSNGtENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHI 86
Cdd:cd17716    1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 225-607 0e+00

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: 613.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  225 EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQR 304
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  305 NIAGKVVTPDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPR 384
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHSRPKSSSAKRKRTSEDLNSPPKEKLKKKRSSRKSAMPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  385 LQLCRSEDRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCV 464
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  465 GKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTS----APEEALRCCRQAG---KEDACPEGNGFSYTIEDPALPKG 537
Cdd:pfam12258 241 GKKPRSVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSegtpAAEETPGCCRQAGpqkREDAGPEGNSHSHTTDEPALPSG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  538 HDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYS 607
Cdd:pfam12258 321 HHGDLTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSDYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 648-723 8.14e-39

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: 138.11  E-value: 8.14e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950164 648 RTLVMTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWI 723
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 8-86 1.11e-38

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: 137.71  E-value: 1.11e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950164   8 DVVAYVEVWSSNGtENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHI 86
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. ...
 13-75 4.42e-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: 75.70  E-value: 4.42e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950164   13 VEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLW 75
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT smart00292
breast cancer carboxy-terminal domain;
4-79 2.09e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.21  E-value: 2.09e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950164     4 PILKDVVAYVevwSSNGTENYSKTFTTQLVDMGAKVSKTFN-KQVTHVIFKDGYQST--WDKAQKRGVKLVSVLWVEKC 79
Cdd:smart00292   2 KLFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT smart00292
breast cancer carboxy-terminal domain;
669-714 4.69e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 36.58  E-value: 4.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767950164   669 KLKGFSIAPDVCE-TTTHVLSGKPL-RTLNVLLGIARGCWVLSYDWVL 714
Cdd:smart00292  28 EALGGKVTSSLSSkTTTHVIVGSPEgGKLELLKAIALGIPIVKEEWLL 75
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 225-607 0e+00

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: 613.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  225 EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQR 304
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  305 NIAGKVVTPDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPR 384
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHSRPKSSSAKRKRTSEDLNSPPKEKLKKKRSSRKSAMPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  385 LQLCRSEDRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCV 464
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  465 GKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTS----APEEALRCCRQAG---KEDACPEGNGFSYTIEDPALPKG 537
Cdd:pfam12258 241 GKKPRSVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSegtpAAEETPGCCRQAGpqkREDAGPEGNSHSHTTDEPALPSG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164  538 HDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYS 607
Cdd:pfam12258 321 HHGDLTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSDYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 648-723 8.14e-39

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: 138.11  E-value: 8.14e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950164 648 RTLVMTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWI 723
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 8-86 1.11e-38

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: 137.71  E-value: 1.11e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950164   8 DVVAYVEVWSSNGtENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHI 86
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. ...
 13-75 4.42e-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: 75.70  E-value: 4.42e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950164   13 VEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLW 75
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 653-723 1.47e-10

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: 58.00  E-value: 1.47e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950164 653 TSMPSEKQNVVIQVVDKLKGfSIAPDVCETTTHVL-----SGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWI 723
Cdd:cd17734    6 SGLSSEQKKLLEKLAQLLKA-KVVTEFSPEVTHVVvpadeRGVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 649-716 1.61e-09

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: 54.68  E-value: 1.61e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950164 649 TLVMTSMPSEKQNVVIQVVDKLkGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWS 716
Cdd:cd00027    2 VICFSGLDDEEREELKKLIEAL-GGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 18-79 2.03e-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: 51.59  E-value: 2.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950164  18 SNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFK-DGYQSTWDKAQKRGVKLVSVLWVEKC 79
Cdd:cd00027    6 SGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKsPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 649-729 2.27e-08

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: 52.35  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164 649 TLVMTSMPSEKQNVVIQVVDKLkGFSIAPDVCETTTHVL--SGKPL---RTLNVLLGIARGCWVLSYDWVLWSLELGHWI 723
Cdd:cd17735    2 SMVASGLTPEELMLVQKFARKT-GSTLTSQFTEETTHVImkTDAELvceRTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80


                 ....*.
gi 767950164 724 SEEPFE 729
Cdd:cd17735   81 PEHDFE 86
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 652-720 2.07e-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: 46.02  E-value: 2.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950164 652 MTSMPSEKQNVVIQVVDKLKGFSIAPDVC-ETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELG 720
Cdd:cd17738    6 LSGFSEDEKKELISIIEKLGGKVLDSDEFdPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
BRCT smart00292
breast cancer carboxy-terminal domain;
4-79 2.09e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.21  E-value: 2.09e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950164     4 PILKDVVAYVevwSSNGTENYSKTFTTQLVDMGAKVSKTFN-KQVTHVIFKDGYQST--WDKAQKRGVKLVSVLWVEKC 79
Cdd:smart00292   2 KLFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 4-79 6.15e-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: 41.90  E-value: 6.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950164    4 PILKDVVAYVevwssNGTENYSKTFTTQLV-DMGAKVSKTFNKQVTHVIFKDGyQSTWDKAQKRGVKLVSVLWVEKC 79
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 ...
 35-88 7.50e-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: 42.13  E-value: 7.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767950164  35 MGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKR-GVKLVSVLWVEKCRTAGAHIDE 88
Cdd:cd17729   43 LGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMpGIHVVHPDWLWACAERWERVDE 97
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 651-713 8.90e-05

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: 41.06  E-value: 8.90e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950164 651 VMTSMPSEKQNVViQVVDKLKGfSIAPDVcETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWV 713
Cdd:cd17744    3 VLFTGVSDKEEGE-KIIKKLGG-SVVDSV-EDCTHLVTDKVRRTVKFLCALARGIPIVSPDWL 62
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 33-80 8.27e-04

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: 38.73  E-value: 8.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767950164  33 VDMGAKVSKTFNKQVTHVIfkdgYQST-------WDKAQKRGVKLVSVLWVEKCR 80
Cdd:cd17727   24 ASLGAEYRWTYDESCTHFI----YQGKandtnreYKSAKEQGKFIVSPHWLYACK 74
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 652-725 1.47e-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: 38.26  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950164 652 MTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWISE 725
Cdd:cd17750    8 LTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
BRCT smart00292
breast cancer carboxy-terminal domain;
669-714 4.69e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 36.58  E-value: 4.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767950164   669 KLKGFSIAPDVCE-TTTHVLSGKPL-RTLNVLLGIARGCWVLSYDWVL 714
Cdd:smart00292  28 EALGGKVTSSLSSkTTTHVIVGSPEgGKLELLKAIALGIPIVKEEWLL 75
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 667-720 4.85e-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: 36.45  E-value: 4.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950164 667 VDKLK--GFSIA--PDVCettTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELG 720
Cdd:cd17743   16 IKKLKklGISIVedPDEC---THLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
 
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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