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Database: UniProt
Entry: A0A1R3R902_ASPC5
LinkDB: A0A1R3R902_ASPC5
Original site: A0A1R3R902_ASPC5 
ID   A0A1R3R902_ASPC5        Unreviewed;       486 AA.
AC   A0A1R3R902;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Anaphase-promoting complex subunit 11 {ECO:0000256|ARBA:ARBA00013928};
GN   ORFNames=ASPCADRAFT_518836 {ECO:0000313|EMBL:OOF90963.1};
OS   Aspergillus carbonarius (strain ITEM 5010).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF90963.1, ECO:0000313|Proteomes:UP000188318};
RN   [1] {ECO:0000313|Proteomes:UP000188318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV907513; OOF90963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3R902; -.
DR   STRING; 602072.A0A1R3R902; -.
DR   VEuPathDB; FungiDB:ASPCADRAFT_518836; -.
DR   OMA; YHHPTVH; -.
DR   OrthoDB; 1827251at2759; -.
DR   Proteomes; UP000188318; Unassembled WGS sequence.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR   GO; GO:0097602; F:cullin family protein binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd16456; RING-H2_APC11; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR024991; RING-H2_APC11.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11210:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 11; 1.
DR   PANTHER; PTHR11210; RING BOX; 1.
DR   Pfam; PF12861; zf-ANAPC11; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188318};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          35..78
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          126..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  53707 MW;  2925191A19AF0791 CRC64;
     MKVTIKEWNA VATWRWDMPD DEVCGICRVQ FDGTCPTCKF PGDDCSLLLG KCGHSFHMHC
     LMTWIQQESS KGLCPMCRQS IRFVYLRRSG HLTLSISRQV ICGESGSFPR YGKLAWLPIP
     PDMSLPKHTS PSPLSSSPSR QSIRRTSGSR PQSIIDRPGT AQAVTDIPEE HDRHDAAAAP
     PTASIPIDQE RPHDITPTFQ PFFTLIEDAN FSEYYHPTVH YIFSDDDTDI VTEAALRTLE
     SDHDIFPANG KGKSKSTRDP SQHRHEAAGT EDTYHDDDEY VNHRKEPLLP EPIPGIRDNY
     VILDIDYASP DGAQNETMGP NNDGAASSHE TQGASFPQQQ RTSPQKFTVT SANSLSPAWQ
     VLNTQIEKNN SSGGQPPNGG LVLKIQGTAG LPMAVLGKDK DRERSSQRLE DMMDQFAKRL
     AELRQVIEAG EQTEELVGDT RLPEETNTEN GPALSPEQPI EAQIPVEGGA GNDGQPAERD
     ELLTTE
//
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