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Database: UniProt
Entry: A0A1J9SEB6_9PEZI
LinkDB: A0A1J9SEB6_9PEZI
Original site: A0A1J9SEB6_9PEZI 
ID   A0A1J9SEB6_9PEZI        Unreviewed;       993 AA.
AC   A0A1J9SEB6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Anaphase-promoting complex subunit 2 {ECO:0000256|ARBA:ARBA00016068};
GN   ORFNames=BKCO1_5000137 {ECO:0000313|EMBL:OJD37925.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD37925.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD37925.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD37925.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJD37925.1}.
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DR   EMBL; MNUE01000005; OJD37925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9SEB6; -.
DR   STRING; 236234.A0A1J9SEB6; -.
DR   OrthoDB; 2786196at2759; -.
DR   Proteomes; UP000183809; 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   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:UP000183809};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          611..786
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          24..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..72
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   993 AA;  110814 MW;  F82DE1EC01D2CFCA CRC64;
     MAAALQNQRN LIFASVFPFA AQSHGSYHSS SAHPTPLSAA AASPDTTFAA PSHHHNHHHS
     SRSTHHHHDR TAAHNPKLVQ RNVAWNTATR FLKLPEWHPP PSTASDDNNN NSHTTSSTTS
     TSTPSTAAPP RPRKHHHRLN ADVEEALRYL LIGDGRLDAA EYDITPTSGS GSNLFPDLLE
     WYTNEAREHF VACVRPALLA AWRQPVALAG GGAPWRVLER SAATLQAAQA FYSSHLDECV
     LPVVRELDYH QQHQHQHYHH RGGGSGGDEV VVAAPLSRAE KVARKFRRDL HAIVMHALPQ
     QRFAKTLAWV LFDAGCGLFG LEGEGGGWGG GGGEEEEESR VVRERVAGLL RELRDVGLGG
     DQAQRAAAQA MDSLMDAFIG SHHMKVDWYG KKPMTRVLRE WVKDGYSPFI REILSCLTGD
     EEMFEVNEVQ QWTNMAIGRL GRARVENLFD YIVNWDRSLG AILDLKEYIT SPAARNHLTN
     SFLQQVSRRL LHAGATTTHI LDIYIYVIRA FIELDPKGIL LEKVARPIRR YLRDREDTAR
     IIVSSLLADV EDEYGNRVEL SSDISAEIAE EMLNPVAANV QDEDLELNWT DMNWMPDPVD
     ASPEYRKAKS ENVLAYLLSL YDREDFINEL KNILGEHLLK NEGSDFEKEI RLLELFKLRL
     GDSNLQACEV MLKDVLESKR MNKQIHHILK QQSDVYRDTP TELNSQILSS FFWPSLREDD
     FHLPEPIQQL MKEYEAGFEG IKDMRKLHWL PALGRVAVSL DFDDRSLELE VLPWQAAVIY
     AFQEEDDTAD GASDDEPPMT EEEERQHQRR ARLRAVGASD VAPTPEKPKK KKPPVTKTVE
     QLEAALEMDE SLVRSALTFW VGHRALLEQG GGQPDAFAVI DSLAELDSAA DKAARLAAAE
     ARERAEEQDA VGAGAAVKSA DDVLVENMQM YRQFVVGMLT ANGRMGADRV CGMLKMALMG
     GFPFGVEEVG VLLGRMVEEG VLVQAGDGFA VKK
//
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