1GQP


Conserved Protein Domain Family
APC10-like

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cd08159: APC10-like 
Click on image for an interactive view with Cn3D
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination.
This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.
Statistics
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PSSM-Id: 176482
View PSSM: cd08159
Aligned: 5 rows
Threshold Bit Score: 189.605
Threshold Setting Gi: 20149882
Created: 1-Oct-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative ligand
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:putative ligand binding site [chemical binding site]
Evidence:
  • Comment:based on sequence homology to the protein structure of APC10 subunit of the human anaphase-promoting complex.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                     #                           #      # #           
1GQP_B      53 INVth-lALWKPSSFKlgnPVDFALDdnyDTFWQSDGgqPHQLDIMFs-KRMDICVMAIFFSmiaDESYAPSLVKVYAGh 130  baker's yeast
NP_078878  241 KQYv---ESIDVSSYTeefNVSCLTDsnaDTYWESDGsqCQHWVRLTmkKGTIVKKLLLTVDt-tDDNFMPKRVVVYGGe 316  human
Q5SSH7     251 KCY----AYIETSSNPa--DIYRMTNgetSSYWQSDGsaRSHWIRLKmkPDVVLRHLSIAVAa-tDQSYMPQQVTVAVGr 323  house mouse
AAH33647   839 KCW----EKVEVSSNPh--RASKLTDhnpKTYWESNGsaGSHYITLHmrRGILIRQLTLLVAs-eDSSYMPARVVVCGGd 911  human
O95714    2780 DSWsrmvKSLNVSSSVn--QASRLIDg-sEPCWQSSGsqGKHWIRLEifPDVLVHRLKMIVDp-aDSSYMPSLVVVSGGn 2855 human
Feature 1                                                             #       
1GQP_B     131 s-psDARFYKMLEVRnv-nGWVALRfldnreddqllKCQFIRLLFPVNHENGKDTHLRGIRLY 191  baker's yeast
NP_078878  317 g--dNLKKLSDVSIDetliGDVCVLedm------tvHLPIIEIRIVECRDDGIDVRLRGVKIK 371  human
Q5SSH7     324 s-asDLQEVRDVHIPsnvtGYVTLLena------niSQLYVQINIKRCLSDGCDTRIHGLRAV 379  house mouse
AAH33647   912 stssLHTELNSVNVMps-aSRVILLenl------trFWPIIQIRIKRCQQGGIDTRIRGLEIL 967  human
O95714    2856 s-lnNLIELKTININps-dTTVPLLndy------teYHRYIEIAIKQCRSSGIDCKIHGLILL 2910 human

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