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pfam00533: BRCT 
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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.
Statistics
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PSSM-Id: 249937
View PSSM: pfam00533
Aligned: 114 rows
Threshold Bit Score: 29.2458
Threshold Setting Gi: 88191904
Created: 28-Mar-2013
Updated: 4-Apr-2013
Structure
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Program:
Drawing:
Aligned Rows:

pfam00533 is a member of the superfamily cl00038.
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z56_C         1 PISNIFAGLLFYVlsdyvtedTGIRITRAELEKTIVEHGGKLiynviLKRHSIGDVRLIscktt------teckALIDRG 74
1L7B_A         3 KGGEALKGLTFVIt------gELSR-PREEVKALLRRLGAKV-----TDSVSRKTSYLVvgenp-----gskleKARALG 65
gi 7673992   619 KVADVLKGKTFVFt------gTLDCCSREKAGEIVEMLGGKF-----SNSVTSKTDYLVvgkdpg----atklsKAKKYG 683
gi 3182983   577 KSSSVFNNKTIVLt------gTLSK-PRQEYAQMLENLGAKI-----SSSVSAKTDFLIagenp-----gsklaLAQKHG 639
gi 75478497   36 IIDAPLLGKTVVIt------gTLPSLSRAEAQKRLETLGAKV-----TSQVSRQTDFLLlgada-----gsklaRAQAFS 99
gi 2506362   593 EIDSPFAGKTVVLt------gSLSQMSRDDAKARLVELGAKV-----AGSVSKKTDLVIageaa-----gsklaKAQELG 656
gi 166214918 592 ASENLFKDKTVVLt------gTLTQMGRNEAKALLQQLGAKV-----SGSVSSKTDFVIagdaa-----gsklaKAQELN 655
gi 59802648  645 LASSPLSGKIIVFt------gSLQKITRDEAKRQAENLGAKV-----ASSVSKKTNLVVageaa-----gsklsKAKELD 708
gi 6225281   610 REQNILTGKIVVFt------gSLSTISRVEAKEIAEKLGAKV-----TASVSLNTDLVIagvng-----gsklkKAKELN 673
gi 6014987   562 QAESPLRGKSFCFs------gSLRNGDRATIH-RIRALGGVV-----RTSVTRDLSYLIfeslsqpyrtaqklkKEQGVA 629
                         90
                 ....*....|...
1Z56_C        75 YDILHPNWVLDCI 87
1L7B_A        66 VPTLTEEELYRLL 78
gi 7673992   684 VKTITEEEFVNMI 696
gi 3182983   640 VSVLNEEELLKRL 652
gi 75478497  100 VRLLMKRSSNVVA 112
gi 2506362   657 IEVIDEAEMLRLL 669
gi 166214918 656 ITVLTEEEFLAQI 668
gi 59802648  709 ISIIDEDRWHRIV 721
gi 6225281   674 IKIIDEVEWLAFI 686
gi 6014987   630 LEIISEDEFCRLL 642
Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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