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Database: UniProt
Entry: A0A1Y2X441_9PEZI
LinkDB: A0A1Y2X441_9PEZI
Original site: A0A1Y2X441_9PEZI 
ID   A0A1Y2X441_9PEZI        Unreviewed;       337 AA.
AC   A0A1Y2X441;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   RecName: Full=DOC domain-containing protein {ECO:0000259|PROSITE:PS51284};
GN   ORFNames=K445DRAFT_317197 {ECO:0000313|EMBL:OTB16217.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB16217.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB16217.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB16217.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SIMILARITY: Belongs to the APC10 family.
CC       {ECO:0000256|ARBA:ARBA00006762}.
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DR   EMBL; KZ112936; OTB16217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2X441; -.
DR   STRING; 1001832.A0A1Y2X441; -.
DR   OrthoDB; 20429at2759; -.
DR   Proteomes; UP000243732; 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   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};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732}.
FT   DOMAIN          98..286
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..89
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  38071 MW;  35BF1786FEDF1597 CRC64;
     MDNPDFGRGR SASAPSGYGQ PQPAVTQDQL WRVLLRVRGE SAVQEDQRND ASSHTSSDQS
     SYDVTAATEE DTEHFEDDEG EDEGHDFEGI EGNDLEQELD EEEEDRNEDP AFDASLVGLK
     EISNLASFTV SSYKPGCGVK ELRDDDVNHY WQSDGPQPHR LNIHFIKRVE IRKLRLYLDY
     ELDESYTPTK IQITAGFSPN MTIPYTMMEF NQPKGWVDVP IEGAGGGHDG NSLCCWFIRV
     IVLENHQNGK DTHIRGVEVY ALDDSADTAE NNPVEDMVEA IDDYRDRMAA MSIHDYDEEA
     VSRLAAEKRD RKARSRKYTP GDGGLSIPDF MREPEIR
//
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