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Database: UniProt
Entry: A5DU25_LODEL
LinkDB: A5DU25_LODEL
Original site: A5DU25_LODEL 
ID   A5DU25_LODEL            Unreviewed;       690 AA.
AC   A5DU25;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   22-FEB-2023, entry version 75.
DE   RecName: Full=DOC domain-containing protein {ECO:0000259|PROSITE:PS51284};
GN   ORFNames=LELG_00861 {ECO:0000313|EMBL:EDK42683.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK42683.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK42683.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the APC10 family.
CC       {ECO:0000256|ARBA:ARBA00006762}.
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DR   EMBL; CH981524; EDK42683.1; -; Genomic_DNA.
DR   RefSeq; XP_001528341.1; XM_001528291.1.
DR   AlphaFoldDB; A5DU25; -.
DR   STRING; 379508.A5DU25; -.
DR   GeneID; 5235673; -.
DR   KEGG; lel:LELG_00861; -.
DR   VEuPathDB; FungiDB:LELG_00861; -.
DR   eggNOG; KOG3437; Eukaryota.
DR   HOGENOM; CLU_025279_0_0_1; -.
DR   InParanoid; A5DU25; -.
DR   OrthoDB; 20429at2759; -.
DR   Proteomes; UP000001996; 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; 2.
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:UP000001996}.
FT   DOMAIN          380..585
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..222
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  75888 MW;  9615F76567326477 CRC64;
     MNSSGYWDRS SVGHSNSPNT SSIFISHDAD AGEEAERAQD QNLPPAPTLI LTPAPAPASA
     SASASTSAPI PARAHAPGSA PVALLALLAL LGLLIPLSTT PSADDASLAH VGPYFDITPH
     PNQHEVQMQP QYTPEEIRCS LGSGVLTDEQ ASRIHHHNFM QLIEEDEEEL DDYYVNGTSR
     LGAGLLASRV IGDGGDGDDS GDSENNVVDA DDPIDASDFN EVDDADDRFN GSFSRIGGLA
     TGITTIVPDT QRSTWEGIMT TEDRRQQLRL MQQTLETYPL QNILTIEEGD EHVNESNIID
     GMSSEREVRD NDTDHDMLSH GTTSSVGQEQ LEQQQQQQQQ QHHHHHHNQD HYQQLHHRPL
     EHEVDDDNEI NADESHSQPS LEQVQRVYYT KGLEELESLQ LVDLSALATW KLSSFKPGFG
     LSQLRDDSPE TYWQSDGSNG GNNTIPSNSA FTNNHLSNPH SVTIQFIKRV ALERISIFTN
     YSLDESYTPS KIKIMAGSSE GWDLIDVCTV NFNQPIGWSH IIFNGIRNDG VLKCFMVKIF
     ILANHQEGKD SHIRAIRCFG RKHSVPPVKG LPSIGNPYHD YNHNHNNSIP HRVNPELLRD
     LSIASGSSLN SGILVGNRII SNSSDVRHQT EVDAEVDAEA ESLVLLPLLP QFPKQTLNEE
     TTSAMRNVNA VLGLNSGFKS IELSSVSSIR
//
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