1VFY


Conserved Protein Domain Family
FYVE_scVPS27p_Vac1p_like

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cd15736: FYVE_scVPS27p_Vac1p_like 
Click on image for an interactive view with Cn3D
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins
The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.
Statistics
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PSSM-Id: 277275
Aligned: 3 rows
Threshold Bit Score: 71.4457
Created: 6-Aug-2013
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C C C H C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:1VFY; Saccharomyces Cerevisiae Vps27p binds two Zn2+ ions through its FYVE domain.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1      #    #            #  #    #  #                       #  # 
1VFY_A     13 ACm--ICSKKFsllnRKHHCRSCGGVFCQEHSSnsiplpd-----lgiyepvRVCDSCF 64  baker's yeast
P32609     77 CCh--TCGRTLnnniGAINCRKCGKLYCRRHLPnmiklnlsaqydprngkwyNCCHDCF 133 Saccharomyces cerevisiae S288c
NP_595745 159 VCsfpSCSVRFglfdRRHHCRRCGDIFCALHCDrnipltmdv-kfclagslyRSCVSCF 216 Schizosaccharomyces pombe 972h-

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