Conserved Protein Domain Family
mRING-HC-C3HC3D_TRAF7

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cd16644: mRING-HC-C3HC3D_TRAF7 
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins
TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor through promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.
Statistics
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PSSM-Id: 319558
View PSSM: cd16644
Aligned: 19 rows
Threshold Bit Score: 64.2308
Threshold Setting Gi: 585660826
Created: 7-May-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding sitemodified
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Homo sapiens LNX2 (5DIN) binds two Zn2+ ions through its modified RING-HC finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
Feature 1           #  #            # #  #  #            #  # 
gi 54036486   129 LCCQLCCs-VFKDPVITTCGHTFCRRCALks------eKCPVDN 165
gi 190588434   10 LRCLLCQr-IMKEPVVASCGHTFCKRCIEtsvl--gneRCPSDN 50
gi 585707497   86 LYCILCKk-VYKDPVITQCGHTYCKQCVTrgg----hdKCPIDE 124
gi 780150898  173 LYCLLCRs-VFQDPVITQCGHTYCRKCVTsrq----feKCPVDT 211
gi 443720995   54 LYCLLCNk-VFTEPVIVSCGHSFCRRCVLdri----nePCPVDR 92
gi 405970764  147 LFCKMCNk-VYKDPVMVTCGHSYCKRCVTrqs----egTCPIDN 185
gi 92081520   157 LYCKICQq-VYKDPVIMSCGHSYCKHCSVsv------dACPVDN 193
gi 340370614   20 LICPICRrvFTAPVISVQCGHTFCRPCIDpke---gsnSCPLDG 60
gi 585660826   16 LLCPICQklFTDPVISVNCGHTFCRACILnreseestrSCPLDE 59
gi 765554321  262 LYCGMCGk-IFTDPVIAQCGHTFCRHCVEhap---agrGCPTHK 301

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