4TKP,2EGP,2ECW,2ECV


Conserved Protein Domain Family
RING-HC_TRIM5_like-C-IV

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cd16591: RING-HC_TRIM5_like-C-IV 
Click on image for an interactive view with Cn3D
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins
TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of 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 B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.
Statistics
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PSSM-Id: 319505
View PSSM: cd16591
Aligned: 10 rows
Threshold Bit Score: 72.5189
Threshold Setting Gi: 159164390
Created: 15-Apr-2016
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:2EGP; Homo sapiens TRIM34 binds two Zn2+ ions through its RING-HC finger.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
Feature 1           #  #           # #  #  #                 # ##  
4TKP_B        13 EVTCPICLELLtePLSLHCGHSFCQACITANHKKsmlykegerSCPVCRI 62
2EGP_A        12 EVTCPICLELLtePLSLDCGHSLCRACITVSNKEavtsmggksSCPVCGI 61
2ECW_A        19 EVTCPICLELLkePVSADCNHSFCRACITLNYESnrnt-dgkgNCPVCRV 67
2ECV_A        19 EVTCPICLELLtqPLSLDCGHSFCQACLTANHKKsmld-kgesSCPVCRI 67
gi 25009488   12 EVTCPICLELLtePLSIDCGHSFCQACITPNGREsvigqegerSCPVCQT 61
gi 38605459   12 EVTCPICLELLtqPLSLDCGHSFCQACLTANHKKsmld-kgesSCPVCRI 60
gi 47606181   12 EVTCPICLELLtePLSLDCGHSFCQACITAKIKEsviisrgesSCPVCQT 61
gi 55976584   12 EVTCPICLELLtePLSLDCGHSLCRACITVSNKEavtsmggksSCPVCGI 61
gi 20141865   12 EVTCPICLELLkePVSADCNHSFCRACITLNYESnrnt-dgkgNCPVCRV 60
gi 632990461  11 DLNCPLCLEIFtdPVTLDCGHSFCRSCIACTQSWekk---ernACPECRT 57

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