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Database: UniProt
Entry: G2Y390_BOTF4
LinkDB: G2Y390_BOTF4
Original site: G2Y390_BOTF4 
ID   G2Y390_BOTF4            Unreviewed;       903 AA.
AC   G2Y390;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Anaphase-promoting complex subunit 2 {ECO:0000256|ARBA:ARBA00016068};
GN   ORFNames=BofuT4_P002890.1 {ECO:0000313|EMBL:CCD47130.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD47130.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR   EMBL; FQ790286; CCD47130.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2Y390; -.
DR   STRING; 999810.G2Y390; -.
DR   eggNOG; KOG2165; Eukaryota.
DR   HOGENOM; CLU_007149_0_0_1; -.
DR   InParanoid; G2Y390; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR044554; APC2-like.
DR   InterPro; IPR014786; APC2_C.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF08672; ANAPC2; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM01013; APC2; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50069; CULLIN_2; 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:UP000008177};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          564..777
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          13..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   903 AA;  101225 MW;  6B66744AF9EA0F4C CRC64;
     MATFATKRKR VLDSVFKKPE ISEPTPVATP TGSFTTSSQP FGESQSFNHG PKTPSSNTRS
     SQQLRGHDRD SSVAQVRDQI QWDRSWHTVT YRLQLPDVPL DTGSIETLRP LSILSDPSFD
     DALKDVLDPV NRLPFALHTD DLLVWHTQQV RRHLLRQILP VLRLYADEEG PRSLVFGSVK
     ILDFAHRMYL HGLSVILKQV ELFTPGLSRV ILEKFRRDLH AIITNSLTDQ FIAALRTVLE
     NYVSSILGLQ GKKGSGIAPI DARTDKVCNE MLNLVESLHK VGLAGEKFEV IFAEIMNHSM
     TEYVNRGCKG LWSATEINIT PQDGERRNSV LPRTAHHVSP SNCVTDLCGW IGDRYSKLAV
     LVFKVIDNVE VAWSDMERWK EMSIGRLAAL RTDELFDIVV NWPNSNGALH DLRTTITTPQ
     RRLHLTEAFA ATLKERLLHP GASTLLILQT YISMIWSFHS LDHSKVLLDR VAYPLQVYLC
     SREDTVRIII TGLLSDTEDA QGNPIESGGD RLIELAHLLN NDSEHSGQKI DDEELDWHDM
     EWVPDPVDAG PGYKRSKSAD IIGTLIGVFG SQDVFIKEFQ NIISENLLKN DGAYEKEIKV
     LELLKSRFGE APLQSCEVML KDILDSVRLD LAIHKTQDLS IAERKAMPPP PTQPILHTKI
     LSRLFWPPLQ ESTFTLPPQI TNLQSDYSTA FSSLKPSRKL TWLPALGHTT VELELADRTV
     VEECTTWQAT VISCFHSETT HHNPDDEDLP AQKSIEELTS ELEMDSVLIL SALKFWVSKL
     VLQESPPKSQ VYSVLETLNA SDRARSDALA SAPVGADHGD DEGEGETEEK GIAGENAKVY
     WQFVQSMLTN SSSQMGAPQI AMMLKMLIAE GFPYSNEELL EWLGGKVEEG VLECVGGRYR
     LKK
//
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