ID A2QB73_ASPNC Unreviewed; 498 AA.
AC A2QB73;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Contig An01c0450, genomic contig {ECO:0000313|EMBL:CAK37417.1};
DE EC=3.4.25.1 {ECO:0000313|EMBL:CAK37417.1};
GN ORFNames=An01g14120 {ECO:0000313|EMBL:CAK37417.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK37417.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK37417.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SIMILARITY: Belongs to the APC10 family.
CC {ECO:0000256|ARBA:ARBA00006762}.
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DR EMBL; AM269991; CAK37417.1; -; Genomic_DNA.
DR RefSeq; XP_001389812.1; XM_001389775.1.
DR AlphaFoldDB; A2QB73; -.
DR EnsemblFungi; CAK37417; CAK37417; An01g14120.
DR GeneID; 4977529; -.
DR KEGG; ang:An01g14120; -.
DR VEuPathDB; FungiDB:An01g14120; -.
DR HOGENOM; CLU_039415_0_1_1; -.
DR OrthoDB; 20429at2759; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:CAK37417.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 212..462
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..211
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55429 MW; 9776342911FE8A37 CRC64;
MPRHHHLLRR HPAPDTSSPS DNTTPHHAPQ QPPPAPQRAS RSRLGHHAQF QTPPSQGLSI
PTLYPSSGTF DPDHPLQSHP SQHAAPHPAA TAALFSLFGR GVHGRPPNHP ADQMMDDEEV
DEEDEEDDED AIPEEYDGVG FSHETTLSSI AHQRTRHRQR QFQRSISEED GMLPAHDVDV
EGPSDIEEEV EHDEQVEVDE EDEEGVEIEP EAGSESEMLH EREKSPTPLP ANLREISSLA
SWTVSTHKPG CGVTALRHPS PTQYWQSDGP QPHTLTLHFF KLVAIVRIRV YLDFEMDESY
TPTKMTFLAG MGGNDLVEFA NWEGEGPCGW VDVELEGVGG RSGGWVTTDA QKQGGGAGGK
KKKSGRRRKG KGKRRGGFIF EDPDVDVDED EDEDDDEDEE DDPYAGNVLK AMVIQMRIIE
NHQNGKDTHV RGFQVFARDD ERKRVGNAPS ASADGRVRRH SARRSLRAST QEDLERDGVS
KVVTSLEEPD WMGEPVIR
//
