Conserved Protein Domain Family
mRING-HC-C3HC5_MAPL

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cd16648: mRING-HC-C3HC5_MAPL 
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins
MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.
Statistics
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PSSM-Id: 438310
Aligned: 9 rows
Threshold Bit Score: 103.316
Created: 3-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 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:modified RING-HC finger (C3HC5-type), extra conserved cysteine is not involved in Zn binding
  • Comment:The C3HC5-type RING finger is distinguished from typical C3HC4 RING-HC finger and C3H2C3 RING-H2 finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.
  • 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.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #  #           # #   #  #         #  #           
Q969V5       299 KSACVVCLSSfKSCVFLECGHVCSCTECYRALPepkKCPICRQAITRVIPLY 350  human
Q6NTT6       300 QNPCSICLSTeKSCVFLECGHVCSCISCYQALPspkKCPICRNFIDRIVPLY 351  African clawed frog
Q5M7X9       289 ENACVICLSNpRGCVLLDCGHVCCCFRCYQALPq-pFCPICRQHIKRVVPLY 339  zebrafish
XP_007900255 300 PAACSICLASeRSCVFLECGHVCSCHECYRALPspkKCPICRDFISRVVPLY 351  elephant shark
XP_005988768 299 LNACVICLSTaRSCVFLECGHVCSCDECYQALLapkKCPICRKLISRVVPLY 350  coelacanth
KFP43502     232 KNACVICLSDtKSCVFLECGHVCSCNDCYRALPepkRCPICRQPISRVVPLY 283  Chlamydotis undulata macqueenii
XP_002124214 307 DNSCVVCLTNpRECILLDCGHICVCIDCLEALPspkQCPVCRSDVARSLPIF 358  vase tunicate
CAD5116326   290 DNSCTVCLSNpRDLIILECGHVCICVECYEALPspkLCPVCRSSIARVALVY 341 
XP_001708458 913 DTACIICMSWaVECIFIPCGHACCCRYCLEFSSh--RCPICRSEIKDFLMLP 962  Giardia lamblia ATCC 50803

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