Conserved Protein Domain Family
RING-HC_RBR_TRIAD1_like

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cd16623: RING-HC_RBR_TRIAD1_like 
RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1), ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar proteins
TRIAD1, also known as ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is a RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48 as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. ANKIB1 is a RBR-type E3 ubiquitin-protein ligase that may function as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. Both TRIAD1 and ANKIB1 contain a RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This family corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination. In contrast to TRIAD1, ANKIB1 harbors an extra N-terminal ankyrin repeats domain.
Statistics
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PSSM-Id: 319537
View PSSM: cd16623
Aligned: 20 rows
Threshold Bit Score: 58.8915
Threshold Setting Gi: 121959574
Created: 29-Jan-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 HHARI (4KBL) 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
                  ....*....|....*....|....*....|....*....|....*....|...
Feature 1         #  #              # #  #  #                    #    #
gi 18202259   139 CAVCMqfvrk-enllsLACQHQFCRSCWEQHCsvlvkd--gvgvgVSCMaqDC 188
gi 158937428  333 CDICMcsisvfedpvdMPCGHDFCRGCWESFLnlkiqe--geahnIFCPayDC 383
gi 284089961  105 CPLCYddvpadqctklPACSHAFCNNCWKAHIeskik---egklqILCPelGC 154
gi 585659564  655 CAICYddisdhdgtclMRCRHWFCNTCWKMHLasrvr---qgdmkIMCPeyKC 704
gi 262111609  162 CDICCdgypa-neifgMGCGHVYCLNCWKPYLslkiqe-gpicvtTTCPahGC 212
gi 358342131  350 CDICCmnfph-dqmqgLACRHYFCLACWQRYLewkime-esqgdrIYCPsyGC 400
gi 340369537  307 CEICYeaisl-nerteVPCGHHFCRDCWASYLevsvke--gggkdISCPghDC 356
gi 440797095  159 CEICYgeisp-desyaVSCGHTFCGDCWGNYLtlkineegqksshLTCMghKC 210
gi 765548994   79 CEICYvdypr-kdmtgLPCNHRFCRHCWVSYLqskimd-egtgekITCPahQC 129
gi 321462893  348 CDICLevieqgssrvyISCDHSFCRRCWSSYLtlkiie--gdanhVTCPalGC 398

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