Conserved Protein Domain Family
RING-HC_SHPRH-like
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cd16569: RING-HC_SHPRH-like 
RING finger, HC subclass, found in SNF2 histone-linker PHD finger RING finger helicase (SHPRH) and similar proteins
SHPRH is a yeast RAD5 homolog found in mammals. It functions as an E3 ubiquitin-protein ligase that associates with proliferating cell nuclear antigen (PCNA), RAD18, and the ubiquitin-conjugating enzyme UBC13 (E2), and suppresses genomic instability by proliferating methyl methanesulfonate (MMS)-induced PCNA polyubiquitination. SHPRH contains a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a linker histone domain (H15), a PHD-finger, and a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA. This subfamily also includes tripartite motif-containing protein 15 (TRIM15). TRIM15, also known as RING finger protein 93 (RNF93), zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM15 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.
Links
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Statistics
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PSSM-Id: 438231
Aligned: 16 rows
Threshold Bit Score: 72.7614
Created: 2-May-2013
Updated: 17-Oct-2022
Structure
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Aligned Rows:
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Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C H C C C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structures of other RING-HC fingers with bound zinc
  • Comment:C3HC4-type RING-HC finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-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.
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1            #  #            # #  #  #                    #  #    
Q149N8       1429 PEPCPICARQLgkqWAVLTCGHCFCNECISIIIeqysvg--shrssIKCAICRQTT 1482 human
EFX71612      757 PDPCPVCHCELgdkWSVLVCGHSFCMECIQLLVaqgpn---nvmkkLRCAICRETT 809  common water flea
XP_007892672 1435 PEPCPICARPLgqqWAVLTCGHCFCNDCIAIIIeqystg--arrsaIKCAVCRQTT 1488 elephant shark
XP_006814870 1029 FITCPICDRRLgdqWCVLCCGHCFCNDCMSILIkqy-------rinIKCAICREKT 1077 Saccoglossus kowalevskii
XP_013421638 1683 PEPCPICQKELgreWSVLHCGHCYCLDCMRILIdgyscg--grqtrVKCAICRQTT 1736 Lingula anatina
EEC02206      198 PEPCPICQNPLgerWSVMQCGHNFCIGCIQMMLrtpac---trgggLLCAVCRSIS 250  black-legged tick
KDR15144     1481 PDPCPICQTNLgdkWSVLQCGHCYCLECVRYMIdqshg---grkvnVKCPICRETT 1533 Zootermopsis nevadensis
XP_002109608 1190 EDSCPICVRKLgkeWTVLGCGHCYCYDCTDVMIkkcaqn-dmrqqsVKCPLCRIKT 1244 Trichoplax adhaerens
XP_013060626  639 PDTCPVCQFGLgfeWSVLLCGHCFCLRCIRTLIdrnligghlmdrrLKCPLCRHLT 694  Biomphalaria glabrata
Q9C019         13 LPACTLCAGPLe-dAVTIPCGHTFCRLCLPALSqmgaq---ssgkiLLCPLCQEEE 64   human

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