ID   G1XGF9_ARTOA            Unreviewed;      1030 AA.
AC   G1XGF9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Anaphase-promoting complex subunit 2 {ECO:0000256|ARBA:ARBA00016068};
GN   ORFNames=AOL_s00083g90 {ECO:0000313|EMBL:EGX47582.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX47582.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX47582.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGX47582.1}.
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DR   EMBL; ADOT01000151; EGX47582.1; -; Genomic_DNA.
DR   RefSeq; XP_011123571.1; XM_011125269.1.
DR   AlphaFoldDB; G1XGF9; -.
DR   STRING; 756982.G1XGF9; -.
DR   GeneID; 22894973; -.
DR   eggNOG; KOG2165; Eukaryota.
DR   HOGENOM; CLU_007149_0_0_1; -.
DR   InParanoid; G1XGF9; -.
DR   OMA; VTTWQAT; -.
DR   OrthoDB; 2786196at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
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; 1.20.1310.10; Cullin Repeats; 1.
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   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:UP000008784};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          654..869
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          895..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..926
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..959
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1030 AA;  116138 MW;  28457760D5CE7331 CRC64;
     MLISSFHHPQ EPHRQVKKRR IFHGIFPPAA SASLPTPIAT PAGSFNENTP IAPAVQASPF
     AQGPAFSSPG GEAFVTHSRA WHLATTFLSF PDSPFDVSEE EGTALGVQKD GVYLRRKADL
     FGQDTREAIT YLMTSGVTAE PGENLVEWYT CEVRRHFLEH VRPILEEVER EPVTKTRPEY
     QLNDIISQLR VTCRIYYSVY SAYILPYLAK IDPIASVEPF HRSLASIIAY SLPSKFPSLL
     RKTFYAYFTV ILSLPSSGTA VTDVGLFTSP HIPGADETVH STDVDLELEE DEKAAVNQEE
     ANRRCEEARH AVFKLVESLN AIGLMANGVG EREFALVIDR VAGEWVTYRF SGRYTDSDLE
     TEDAEGDTSM AKLPTSVASA EIMREWLFDS LMPLVVPIMK IIRPGDVDEE LPPVLNRLAQ
     RLSRVRMKEM FDIIVDFPQS MPGIMDLIPT LNTPIARLVL TSTFAYTLNR RLLHQGASTV
     DVLRAYINMI KCFQIIDAKG VLLDKVGARV RRYLSTREDT VVEIVKGILC YEYDEEDENS
     DSMIKSADQS ISIEGAEAFK ESLRRRKAIP GDAEDLDDED VLQEISTELQ ACAQMGADKK
     NEVLGAAAAA SLEDLDYDDM DWQPDPADAG PEFRRDKGTD IISHLFTMLE STKFINEFQN
     QLGKRLLLQP TSEFLREKAT IELLKVRFGE NEMQNAAIML KDLSESRKID THLRDTILTK
     HLSRNTAMAG GPQRMETEVH VKVISRLFWP QHMISEGDFN PPNRIANTLD LFNHEFELLK
     KSRKLNWLKE EGFAVIELEL NDRTLGFKQV PTYAATVIDT FAKGPSPPNP DIPRELNGGE
     VGNAWSIDQL KEKLSMEIEL LQKSLEYWVD RTVLAEYPLN RKIYYVMETL PRSDIPASRR
     TTPHTSPQKR DDSHITPRRR RALSFISEDS NDSGNEEGGT RKEEPTPAKA DAEDDDPLKN
     PRFTMAWNYI AGMLTNQGPL TTDRVFATLS LFLIPMGGLK FDAAELDHFM MKMEENGRVD
     KTPSGWKMRK
//