Conserved Protein Domain Family
RING-H2_Vps11

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cd16688: RING-H2_Vps11 
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins
Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole.
Statistics
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PSSM-Id: 438349
Aligned: 37 rows
Threshold Bit Score: 63.5203
Created: 2-May-2013
Updated: 17-Oct-2022
Structure
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Aligned Rows:
 
Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C H H C C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structures of other RING-H2 fingers with bound zinc
  • Comment:C3H2C3-type RING-H2 finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, where X is any amino acid and the number of X residues varies in different fingers
  • Comment:A RING finger typically binds two zinc atoms, with its Cys and/or His side chains in a unique "cross-brace" arrangement.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #  #            # #  #  #                                   #  #   
Q9H270     820 TKCSICNsaLELPSVHFLCGHSFHQHCFESyse-------------------------sdaDCPTCLPE 863  human
EME30156   951 DRCSKCGveLTVPLIHFLCGHSYHIDCLVDmqsstrsvstalgnstysgqtselrvdtstlSCSLCERE 1019 Galdieria sulphuraria
EFX87578   782 SKCNVCNqpLELPSVHFLCLHSFHQHCFDSyad-------------------------nenECPACHTE 825  common water flea
CBY17744   319 SKCKLCGkdLSLPSVHFLCGHSFHHHCFTTyid-------------------------qdgECPICAQQ 362  Oikopleura dioica
EAY22269   752 AYCDKCHdtLEIPIRHFLCGHSYHLACLGEvi----------------------------eFCPICHER 792  Trichomonas vaginalis G3
CAK67595   864 TKCNCCDaiLSLPSYHFLCGHSYHEHCIHTe-----------------------------rACLLCPQD 903  Paramecium tetraurelia stra...
Q09600     801 TKCSACDtpLQLPTVHFLCKHAYHVHCFESynmd------------------------gsdKCPACQTT 845  Caenorhabditis elegans
KFM62525    61 SKCSGCThqLELPSVHFLCGHSYHQQCFESysae------------------------hdsECPLCLTE 105  Stegodyphus mimosarum
Q8I480    1187 AYCSICKeiLSVPMIHFLCKHSYHSYCLKDn-----------------------------nVCILCHNK 1226 Plasmodium falciparum 3D7
NP_730776  731 DKCDICRemLSMQSIYFLCQHSFHEECLNYkstkr----------------------qekfLCIICKTR 777  fruit fly

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