ID A0A165MM38_9APHY Unreviewed; 191 AA.
AC A0A165MM38;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Anaphase-promoting complex subunit 10 {ECO:0000256|PIRNR:PIRNR028841};
GN ORFNames=DAEQUDRAFT_730915 {ECO:0000313|EMBL:KZT65866.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT65866.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT65866.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT65866.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. {ECO:0000256|PIRNR:PIRNR028841}.
CC -!- SIMILARITY: Belongs to the APC10 family.
CC {ECO:0000256|ARBA:ARBA00006762, ECO:0000256|PIRNR:PIRNR028841}.
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DR EMBL; KV429098; KZT65866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165MM38; -.
DR STRING; 1314783.A0A165MM38; -.
DR OrthoDB; 20429at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd08366; APC10; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR016901; APC10/Doc1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR12936; ANAPHASE-PROMOTING COMPLEX 10; 1.
DR PANTHER; PTHR12936:SF0; ANAPHASE-PROMOTING COMPLEX SUBUNIT 10; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR PIRSF; PIRSF028841; APC10_sub; 1.
DR SMART; SM01337; APC10; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51284; DOC; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR028841};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|PIRNR:PIRNR028841};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|PIRNR:PIRNR028841};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR028841}.
FT DOMAIN 1..189
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 191 AA; 21077 MW; 8845909A8CA2D863 CRC64;
MPADGTPTVH SGKKPPQLPW PDIGHLAKWS VSSHKFGFGP ECLTDDQPDT FWHSDGPQPH
FVTIEFPRKV AVQKLSVYLS FPLDDSYTPA TIAVRAGTGP ADLQDVRILT LDKPDGWITF
DVSAEPNEDG DGCKSVNAYV VQVIILANHM NGKDTHVRGL HILGPIEDTP ANNEEPFSWI
SPVFKMHECI R
//
