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) protein complexes. 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 absent of Vps11, resulting in a 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 in Saccharomyces cerevisiae. 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: 319602
View PSSM: cd16688
Aligned: 42 rows
Threshold Bit Score: 61.9371
Threshold Setting Gi: 452823143
Created: 2-May-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding siteRING-H2 finger
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Oryza sativa El5 (1IYM) binds two Zn2+ ions through its RING-H2 finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
Feature 1           #  #            # #  #  #                                   #  #   
gi 23396928   820 TKCSICNsaLELPSVHFLCGHSFHQHCFESyse-------------------------sdaDCPTCLPE 863
gi 452823143  951 DRCSKCGveLTVPLIHFLCGHSYHIDCLVDmqsstrsvstalgnstysgqtselrvdtstlSCSLCERE 1019
gi 313239141  319 SKCKLCGkdLSLPSVHFLCGHSFHHHCFTTyid-------------------------qdgECPICAQQ 362
gi 465797053  816 PECGLCKqaLELPAVHFMCRHSFHLRCLPEgea--------------------------arECPLCARA 858
gi 262103748  904 TKCDLCNhdLDLPAVHFMCQHSFHLNCISEtd----------------------------rECITCSMD 944
gi 163773545  638 GRCELCPerLRLPAIHFLCGHSYHQRCILNa-----------------------------eECTICHDR 677
gi 121917495  752 AYCDKCHdtLEIPIRHFLCGHSYHLACLGEvi----------------------------eFCPICHER 792
gi 124402120  864 TKCNCCDaiLSLPSYHFLCGHSYHEHCIHTe-----------------------------rACLLCPQD 903
gi 672299937   26 TRCDACGnaLDLPSVHFACCHSFHLVCLASgetdpssaremvp------gtvvgpgkapeySCPVCTPQ 88
gi 75015175  1187 AYCSICKeiLSVPMIHFLCKHSYHSYCLKDn-----------------------------nVCILCHNK 1226

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