1BOR


Conserved Protein Domain Family
RING-HC_PML_C-V
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cd16579: RING-HC_PML_C-V 
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RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins
Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.
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Statistics
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PSSM-Id: 438241
Aligned: 9 rows
Threshold Bit Score: 51.7877
Created: 21-Mar-2015
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:1BOR; Homo sapiens transcription factor PML binds two Zn2+ ions through its RING-HC finger.
    - View structure with Cn3D
  • Citation:PMID 8317827
  • Citation:PMID 7729428
  • 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              #  #               # #  #  #                    #  #   
1BOR_A         3 EFQFLRCQQCQAEa----KCPKLLPCLHTLCSGCLEAsg-------------mQCPICQAP 46  human
P29590        51 EFQFLRCQQCQAEa----KCPKLLPCLHTLCSGCLEAsg-------------mQCPICQAP 94  human
XP_014347087  52 IRKQLICKSCKLAy----VEPKLLSCQHSVCSYCLEKlkseatlq-edgyydvKCPICKSS 107 coelacanth
XP_007478198  91 EFCFLLCHVCKMEs----KCPKLLSCLHTVCSKCLEShep-----------agQCPICRDS 136 gray short-tailed opossum
Q60953        56 EFQFLRCPSCQAQa----KCPKLLPCLHTLCSGCLEApg-------------lQCPICKAP 99  house mouse
XP_003728139  34 RDKHLVCAGCKQRfvtsvYTPTLLPCLHSVCPTCFDAstskds-----etlctVCPSCKQQ 89  purple sea urchin
CAD5117956    81 SKDIFNCPGCSKPl----AQPKLLPCAHTICHQCLKTlaeq---------tefKCPVCKMN 128
NP_001040817  19 SETFLTCSTCLYTydgntRKPKLLPCSHSVCLFCVTQlaelspe---tqpptlRCPLCREV 76  Caenorhabditis elegans
KPM08360      18 TEGFLTCGTCLYTydaeeHTPKLLPCSHTVCKVCLEKiaataairdpassgnfRCPICREL 78  Sarcoptes scabiei

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