Conserved Protein Domain Family
RING-HC_TRIM41_like_C-IV

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cd16602: RING-HC_TRIM41_like_C-IV 
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins
TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs 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. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.
Statistics
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PSSM-Id: 319516
View PSSM: cd16602
Aligned: 4 rows
Threshold Bit Score: 69.8955
Threshold Setting Gi: 465954398
Created: 15-Apr-2016
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding siteRING-HC finger
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Homo sapiens TRIM34 (2EGP) binds two Zn2+ ions through its RING-HC finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            #  #           # #  #  #                                                    
gi 116242826  16 EEAVCAICLDYFtDPVSIGCGHNFCRVCVTQLWggedeedrdeldreeeeedgeeeeveavgagagwdtpmrdedyegdm 95
gi 71897261   22 EEAICAICLDYFvEPVSIGCGHNFCRVCIAQLWgggeaeveesggaaaleeeeeeleeeeedelgeeeldelwdgvvqg- 100
gi 47606198   16 EEAVCAICLDYFkDPVSISCGHNFCRGCVTQLWskedeedqneeedeweeeedeeavgamdgwdgsirevlyrgnadeel 95
gi 465954398  12 EETNCPICLEYLrDPVTVQCGHNFCQVCITQLWggeeegegqaeyeaagddvgmggeeddvdelddddnveyneeeegdg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
gi 116242826  96 eeeveeeeegvfwtsgms---rsswdnmdyvweeedeeedldyylgdmeeedlrgedeedeeevleeveeedldpvtplp 172
gi 71897261  101 ----------------------------------------elyfgdddydedvmeedveeeeeeedeaqsppppvlparp 140
gi 47606198   96 fqdqdddelwlgdsgitnwdnvdymwdeeeeeeeedqdyylgglrpdlridvyreeeileaydededeelypdihpppsl 175
gi 465954398  92 dngaeeeddmwseeded-----tdlwddpgeddmwedevgdelffeeddydeevmeeedleeeeeeplpppppaavvtrp 166
                        170
                 ....*....|...
Feature 1               #  #  
gi 116242826 173 pppapRRCFTCPQ 185
gi 71897261  141 rrlqtFTCPQCRK 153
gi 47606198  176 plpgqFTCPQCRK 188
gi 465954398 167 rhpttFTCPQCRK 179

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