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SDS23_ASPNC
ID   SDS23_ASPNC             Reviewed;         508 AA.
AC   A2RB71;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein sds23;
GN   Name=sds23; ORFNames=An18g05720;
OS   Aspergillus niger (strain 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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.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   -!- FUNCTION: Involved in DNA replication and cell separation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SDS23 family. {ECO:0000305}.
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DR   EMBL; AM270409; CAK97491.1; -; Genomic_DNA.
DR   RefSeq; XP_001399023.1; XM_001398986.2.
DR   AlphaFoldDB; A2RB71; -.
DR   SMR; A2RB71; -.
DR   PaxDb; A2RB71; -.
DR   EnsemblFungi; CAK97491; CAK97491; An18g05720.
DR   GeneID; 4990138; -.
DR   KEGG; ang:ANI_1_754164; -.
DR   VEuPathDB; FungiDB:An18g05720; -.
DR   HOGENOM; CLU_024459_0_0_1; -.
DR   Proteomes; UP000006706; Chromosome 8L.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   Gene3D; 3.10.580.10; -; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR016711; Ssd23.
DR   Pfam; PF00571; CBS; 2.
DR   PIRSF; PIRSF018148; UCP018148_CBS_YBR214w; 1.
DR   SMART; SM00116; CBS; 3.
DR   SUPFAM; SSF54631; SSF54631; 2.
DR   PROSITE; PS51371; CBS; 3.
PE   3: Inferred from homology;
KW   CBS domain; Cytoplasm; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..508
FT                   /note="Protein sds23"
FT                   /id="PRO_0000324947"
FT   DOMAIN          108..173
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          199..258
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          276..333
FT                   /note="CBS 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          336..394
FT                   /note="CBS 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  54358 MW;  BE49239B6604A12F CRC64;
     MTDRPMETVA DSNSSGSNLA SPRSSTDSRT PSASVRSLRL SSHAPNHQHR QSISDTLRAT
     PGSPRARRQP SLTQAAIQSL IDNPPAPNNA NPAFVGRDWR EISIGELVSP DDLKFVEINT
     GIEEATNILI DTGAPVLLIR ESPQHKSAVG TFDYADLNAY LLLAAGLTQP NEELLASYEE
     LARKAKEGIP IPLRDVKDLG RKEPLTTLPA SASVMTAVQT FGGGVHRVVV VSERDDNEVL
     GIFSQFRLVK FLWENGRSFP VIDQLYPQSL HDLRIGSRDV ISINGDRPLV DALQIMNEEG
     ISSIAVVDSH FNVVGNISTT DVKLLTRSSS LPLLRNTCTH FISVILSNRG LEEGKDSFPV
     FHVNPGSTLA HTVAKVVATR SHRLWVTDPL SPSSSGPPTP SHSSVHIPLV TNSSPPPSPA
     VNNGTAAPAA YLSAPSIPAS ALPGARLSGR LVGVVSLTDI LNLHARASGL SPADPAESRS
     RRRRSSSSSV GVRRSGEIGR ELFSGRIV
 
 
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