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Conserved domains on  [gi|1907189053|ref|XP_036009913|]
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microcephalin isoform X14 [Mus musculus]

Protein Classification

BRCT_microcephalin_rpt1 and Microcephalin domain-containing protein( domain architecture ID 13026447)

BRCT_microcephalin_rpt1 and Microcephalin domain-containing protein

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 ...
 250-623 1.80e-168

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: 487.31  E-value: 1.80e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 250 ESFASGSHSSFGD-----SCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQK 324
Cdd:pfam12258   1 ESFAGGLHSSFDDlcgnsECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 325 DATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRL-GPKNSSAKRKRAA-DLGSSPKGKL-KKRYKRKSALA- 400
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHsRPKSSSAKRKRTSeDLNSPPKEKLkKKRSSRKSAMPr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 401 IQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCI 480
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 481 GEKHRsISSISDLISKSASSLEKPVKEEVNTASTCLLLVETS-ANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHI 559
Cdd:pfam12258 241 GKKPR-SVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSEGTPaAEETPGCCRQAGPQKREDAGPEGNSHSHTTDEPALPS 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189053 560 ------TPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHI-CNLSLGEDCNVEKSVEEKENIATGYS 623
Cdd:pfam12258 320 ghhgdlTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSdYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 14-92 1.68e-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: 131.16  E-value: 1.68e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189053  14 DVVAYVEVWSSKGtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALV 92
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 ...
 250-623 1.80e-168

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: 487.31  E-value: 1.80e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 250 ESFASGSHSSFGD-----SCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQK 324
Cdd:pfam12258   1 ESFAGGLHSSFDDlcgnsECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 325 DATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRL-GPKNSSAKRKRAA-DLGSSPKGKL-KKRYKRKSALA- 400
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHsRPKSSSAKRKRTSeDLNSPPKEKLkKKRSSRKSAMPr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 401 IQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCI 480
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 481 GEKHRsISSISDLISKSASSLEKPVKEEVNTASTCLLLVETS-ANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHI 559
Cdd:pfam12258 241 GKKPR-SVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSEGTPaAEETPGCCRQAGPQKREDAGPEGNSHSHTTDEPALPS 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189053 560 ------TPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHI-CNLSLGEDCNVEKSVEEKENIATGYS 623
Cdd:pfam12258 320 ghhgdlTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSdYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 14-92 1.68e-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: 131.16  E-value: 1.68e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189053  14 DVVAYVEVWSSKGtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALV 92
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. ...
 15-81 2.41e-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: 70.70  E-value: 2.41e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189053  15 VVAYVEVWSskgtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLW 81
Cdd:pfam12738   1 LVICVTGFD----GDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT smart00292
breast cancer carboxy-terminal domain;
11-85 1.10e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.90  E-value: 1.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189053   11 FLKDVVAYVevwSSKGTENYSRTFAKQLEDMGATVSKTLN-KQVTHVIFKDGYQST--WDKAQKTGAKLVSVLWVEKC 85
Cdd:smart00292   3 LFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 250-623 1.80e-168

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: 487.31  E-value: 1.80e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 250 ESFASGSHSSFGD-----SCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQK 324
Cdd:pfam12258   1 ESFAGGLHSSFDDlcgnsECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 325 DATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRL-GPKNSSAKRKRAA-DLGSSPKGKL-KKRYKRKSALA- 400
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHsRPKSSSAKRKRTSeDLNSPPKEKLkKKRSSRKSAMPr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 401 IQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCI 480
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 481 GEKHRsISSISDLISKSASSLEKPVKEEVNTASTCLLLVETS-ANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHI 559
Cdd:pfam12258 241 GKKPR-SVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSEGTPaAEETPGCCRQAGPQKREDAGPEGNSHSHTTDEPALPS 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189053 560 ------TPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHI-CNLSLGEDCNVEKSVEEKENIATGYS 623
Cdd:pfam12258 320 ghhgdlTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSdYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 14-92 1.68e-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: 131.16  E-value: 1.68e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189053  14 DVVAYVEVWSSKGtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALV 92
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. ...
 15-81 2.41e-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: 70.70  E-value: 2.41e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189053  15 VVAYVEVWSskgtENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLW 81
Cdd:pfam12738   1 LVICVTGFD----GDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 32-85 6.85e-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: 49.67  E-value: 6.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907189053  32 RTFAKQLEDMGATVSKTLNKQVTHVIFK-DGYQSTWDKAQKTGAKLVSVLWVEKC 85
Cdd:cd00027    14 EELKKLIEALGGKVSESLSSKVTHLIAKsPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 11-85 2.03e-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: 45.75  E-value: 2.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189053  11 FLKDVVAYVevwssKGTENYSRTFAKQ-LEDMGATVSKTLNKQVTHVIFKDGyQSTWDKAQKTGAKLVSVLWVEKC 85
Cdd:pfam00533   5 LFSGKTFVI-----TGLDGLERDELKElIEKLGGKVTDSLSKKTTHVIVEAR-TKKYLKAKELGIPIVTEEWLLDC 74
BRCT smart00292
breast cancer carboxy-terminal domain;
11-85 1.10e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.90  E-value: 1.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189053   11 FLKDVVAYVevwSSKGTENYSRTFAKQLEDMGATVSKTLN-KQVTHVIFKDGYQST--WDKAQKTGAKLVSVLWVEKC 85
Cdd:smart00292   3 LFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 28-85 1.38e-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: 38.28  E-value: 1.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053  28 ENYSRTFAKQL-EDMGATVSKTLNKQVTHVIF-KDGYQSTWDKAQKTGAKLVSVLWVEKC 85
Cdd:cd17729    29 IDPERSRLWKLaESLGAKVVTDLSPRTTHLVAaKLGTEKVKQALKMPGIHVVHPDWLWAC 88
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 42-93 3.57e-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: 36.88  E-value: 3.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907189053  42 GATVSKTLNKQVTHVIFKD-GYQSTW--DKAQKTGAKLVSVLWVEKCRMAGALVD 93
Cdd:cd17726    31 GGIISYIINKKCTHVVVNNaKALSSYkcRMAQKYGIPVVSLDYIWKCVEAGKLLD 85
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 38-93 4.52e-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: 36.47  E-value: 4.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189053  38 LEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALVD 93
Cdd:cd17711    25 IEEHGGEVVDEYSPRVTHVICESQDSPEYQQALRDGKRVVTAYWLNDVLKRGKLLP 80
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 32-97 4.75e-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: 4.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189053  32 RTFAKQLEDMGATVSKTLNKQVTHVIFKdgYQSTWDKAQKTGAKLVSVLWVEKCRMAGALVDESLF 97
Cdd:pfam16589  21 SKLKRLIEANGGTVVDNINPAVYIVIAP--YNKTDKLAENTKLGVVSPQWIFDCVKKGKLLPLENY 84
Herpes_LMP1 pfam05297
Herpesvirus latent membrane protein 1 (LMP1); This family consists of several latent membrane ...
 518-617 4.86e-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: 39.63  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189053 518 LVETSANDSPGLCS----------QPGPQLRDDTGPEGSSHPD-TLSSSAHHITPLKGNSTETRDPGDGKGSPKEGSTPP 586
Cdd:pfam05297 226 LLVSGAGDGPPLCSqnlgapgggpDNGPQDPDNTDDNGPQDPDnTDDNGPHDPLPQDPDNTDDNGPQDPDNTADNGPHDP 305

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907189053 587 ASASPEDevhicnlSLGEDCNVEKSVEEKEN 617
Cdd:pfam05297 306 LPHNPSD-------SAGNDGGPPNLTEEVEN 329
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 12-86 8.24e-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: 35.65  E-value: 8.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189053  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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