2CSY


Conserved Protein Domain Family
RING-HC_RNF113A_B
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cd16539: RING-HC_RNF113A_B 
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RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins
RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.
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Statistics
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PSSM-Id: 438201
Aligned: 47 rows
Threshold Bit Score: 65.6909
Created: 2-May-2013
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
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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 H C C C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:2CSY; Homo sapiens RNF113B (also known as ZNF183-like 1) binds two Zn2+ ions through its RING-HC finger.
  • 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.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1               #  #              # #  #  #               #  #         
2CSY_A        11 EEEIPFRCFICRQA---FQNPVVTKCRHYFCESCALEHFra-----tpRCYICDQPTGGIFN 64  human
EFC50166     201 EEQVPHACFICKKT---FNDPVVTICGHYFCSKCALEKYnag---knpNCQCCGNNTKGVFN 256 Naegleria gruberi strain NEG-M
Q6CB23       199 DSGIPDTCPICQGE---FKSPVVTQCCHYFCEKCFLAKHkk-----kqNCFVCGKNTNGVCK 252 Yarrowia lipolytica CLIB122
P53769       192 LEKIPFKCTLCKED---YKSPVVTNCGHYFCGSCFAKDMkk-----gtKCFICHKETHGSAK 245 Saccharomyces cerevisiae S288c
EAY23242     137 TVEHIDICAICKGT---FKNPVQTKCGHVFCQNCAFERFkt-----dkTCAVCGANTEGIFN 190 Trichomonas vaginalis G3
CEF99873     261 ENDLPESCSICNTPwldAKFPVATSCGHCFCERCALQHNak-----dtTCFTCGKDTGGTFN 317 Ostreococcus tauri
NP_585862     46 ISGPGPLCGICKKT---FEERVVAECGHSFCSLCAIRKYqd-----gdECGVCGKAMYGRFW 99  Encephalitozoon cuniculi GB-M1
NP_564172      3 APPENELCSICHGH---FNAPCQSNCSHWFCGNCIMLVWrhgstlrpcKCPLCRRPISLLVP 61  thale cress
XP_024373824  84 SPPDNDCCSVCHDS---FTMPCQANCAHWFCGECILRVWqhssvlqpcKCPICRRAITLLIP 142 Physcomitrium patens
EFJ32206       3 APDENDCCSVCHDT---FTLPCQANCAHWFCGECILRVWqhsaalqpcKCPICRRTINLLIP 61  Selaginella moellendorffii

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