Conserved Protein Domain Family
SH3_Fus1p

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cd11854: SH3_Fus1p 
Src homology 3 domain of yeast cell fusion protein Fus1p
Fus1p is required at the cell surface for cell fusion during the mating response in yeast. It requires Bch1p and Bud7p, which are Chs5p-Arf1p binding proteins, for localization to the plasma membrane. It acts as a scaffold protein to assemble a cell surface complex which is involved in septum degradation and inhibition of the NOG pathway to promote cell fusion. The SH3 domain of Fus1p interacts with Bin1p, a formin that controls the assembly of actin cables in response to Cdc42 signaling. It has been shown to bind the motif, R(S/T)(S/T)SL, instead of PxxP motifs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Statistics
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PSSM-Id: 212788
Aligned: 13 rows
Threshold Bit Score: 86.2192
Created: 29-Nov-2011
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
peptide ligand
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Comment:The Fus1p SH3 domain recognizes and binds the R(S/T)(S/T)SL motif, instead of the PxxP motif preferentially recognized by most SH3 domains.
  • Comment:based on the structures of other SH3 domains bound to peptide ligands
  • Citation:PMID 7664083
  • Comment:flanking hinge and loops (RT and n-Src) confer sequence specificity for ligand residues outside the core binding motif

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1             # #  #   #                 ##                                  # # ##  
P11710       440 TYTVIQDYEPRLTDEIRISLGEKVKILATHTDGWCLVEKCntqkgsihv------svddkrylnEDRGIVPGDCLQ 509 baker's yeast
XP_452264    441 LYRVVKDYQAVLMDEIDIRGGELVRVLARHTDGWCLVERSniqnhssl---------dgptylnENRGIVPGLCLQ 507 Kluyveromyces lacti...
NP_986247    432 LCVVIKPFSPRLLDEIELNIDEQVRVLARHTDGWCLVEKCdsaksadsds----dnisapnylnERRGIVPQMCLK 503 Ashbya gossypii ATC...
XP_445013    344 QYRVREEYVPSLSDEIHVTVGETVRVLASHNDGWALVERIeasdgkrl--------vssgsyinENRGIIPNKCLL 411 Candida glabrata CB...
XP_002474292 238 AMFVESTFKPSLSDELLVKPGETVRMLEEYEDEWCLVQRGsp--------------------edGQKGVVPRFCLR 293 Postia placenta Mad...
XP_001832914 375 LMTAITRFVPTLDDELLLQVGDTVRVIEEYRDGWCLVQQVgr--------------------idSPRGVVPAVCLQ 430 Coprinopsis cinerea...
XP_001646985 420 IKQVVEQYEARLTDEIDLKVGEYVKILATHTDGWCLLEKCtgngtaiskyhlvdvdvtdkrylnDDRGIAPGRCIA 495 Vanderwaltozyma pol...
EGN95764      84 LMVVTSVFEPAMKDELLIKLGETLTMLEEYEDEWCLVRRHd-----------------------RVMGMIPCFCLS 136 Serpula lacrymans v...
EGO21187      11 ETTVKYSFIPSLPDELSISTGERVTVSGRYDDGWALCINGr-----------------------GEQGMVPQECLE 63  Serpula lacrymans v...
XP_001886115 264 GATVIYTFITSLPDELSIRVGETIRVLAEYDDGWALSLNAg-----------------------GEQGMVPLQCLD 316 Laccaria bicolor S2...
EGU76295     531 VHRVQLDFKPTMDDELELRAGDLVRLLHEYDDGWALCIRLd----------------------rSRQGVVPRTCLS 584 Fusarium oxysporum ...
XP_003034841 276 MATVSSTYTPSMPDELGVTVGDKLKVVREFDDGWCECVNAa-----------------------GKKGMVPIECLE 328 Schizophyllum commu...
XP_002398036 235 GTIVRRTFIPNMDDELWITTGETIKVLQDYDDGWALCENAq-----------------------MQRGMVPLECLD 287 Moniliophthora pern...

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