4UI9,2MT5,4R2Y,5G04,4R2Y


Conserved Protein Domain Family
RING-H2_APC11
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cd16456: RING-H2_APC11 
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RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar proteins
APC11, also known as cyclosome subunit 11, or hepatocellular carcinoma-associated RING finger protein, is a C3H2C3-type RING-H2 protein that facilitates ubiquitin chain formation by recruiting ubiquitin-charged ubiquitin conjugating enzymes (E2) through its RING-H2 domain. APC11 and its partner, the cullin-like subunit APC2, form the dynamic catalytic core of the gigantic, multisubunit 1.2-MDa anaphase-promoting complex/cyclosome (APC), also known as the cyclosome, which is a ubiquitin-protein ligase (E3) composed of at least 12 subunits and controls cell division by ubiquitinating cell cycle regulators, such as cyclin B and securin, to drive their timely degradation. APC11 can be inhibited by hydrogen peroxide, which may contribute to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress. APC11 contains a canonical RING-H2-finger that coordinate two Zn2+ ions. In addition, it contains a third Zn2+-binding site that is not essential for its ligase activity.
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Statistics
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PSSM-Id: 438120
Aligned: 42 rows
Threshold Bit Score: 83.0995
Created: 22-Dec-2011
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
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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 H C C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:4R2Y; Homo sapiens APC11 swapped dimer binds four Zn2+ ions; two per canonical C3H2C3-type RING-H2 finger
  • Structure:2MT5; Homo sapiens APC11 binds two Zn2+ ions through its RING-H2 finger.
  • Comment:C3H2C3-type RING-H2 finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-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           #  #                          # #  #  #                #  #      
4UI9_B        20 DENCGICRmaFNGCCP--DCKvPGDDCPLVWGqCSHCFHMHCILKWLhaqq---vqqhCPMCRQEWKF 82  human
4R2Y_A         4 DENCGICRmaFNGCCP--DCKvPGDDCPLVWGqCSHCFHMHCILKWLhaqq---vqqhCPMCRQEWKF 66  human
NP_497937     69 EDTCGICRmeFESACN--MCKfPGDDCPLVLGiCRHAFHRHCIDKWIaaptn-qpraqCPLCRQDWTI 133 Caenorhabditis elegans
Q54L48        21 EECCGICRmaFDGCCV--DCKiPGDDCPPVWGvCNHAFHMHCILKWLnane----lqqCPMCRSEWRF 82  Dictyostelium discoideum AX4
ABK22931      20 DELCAICKlpFDGCCT--ECKyPGDDCPLVWGaCSHPFHLHCIVKWTgtqn----rahCPLCRRDWQI 81  Sitka spruce
XP_002785341 223 EEDCAICCqpFDATCG--ECRiPGDDCPPVWGqCGHHFHVHCISRWIndq------kpCPMCRREFKP 282 Perkinsus marinus ATCC 50983
CBY14436      19 DQKCAVCRvdFEATCNtgICKfPGDDCPVIRGaCKHPFHLHCINKWLasleenrqekvCPLCRQVWSI 86  Oikopleura dioica
BAM82956      20 DDLCGICRlpFDGTCN--ACKtPGDDCPLALGeCRHAFHLHCILKWLsset---srnhCPLCRQEWQF 82  Cyanidioschyzon merolae str...
XP_004338596  55 EDSCGICRmqFDTYCV--DCKkPGDECPPIWGkCNHIFHLHCILKWIqqqg---aeahCPMCRQPWEF 117 Acanthamoeba castellanii st...
ETP33918      36 EECCGICRyaFEACCP--ECTmPGDGCPPVWGaCNHAFHMHCLVKWLeslqs--mrqhCPMCRQDWKF 99  Phytophthora parasitica P10297

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