(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7S3_ASPNC

ID   A2Q7S3_ASPNC            Unreviewed;       646 AA.
AC   A2Q7S3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 66.
DE   SubName: Full=Aspergillus niger contig An01c0070, genomic contig {ECO:0000313|EMBL:CAK43546.1};
DE   Flags: Precursor;
GN   ORFNames=An01g01750 {ECO:0000313|EMBL:CAK43546.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43546.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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DR   EMBL; AM269954; CAK43546.1; -; Genomic_DNA.
DR   RefSeq; XP_001388614.1; XM_001388577.2.
DR   MEROPS; S53.007; -.
DR   PaxDb; A2Q7S3; -.
DR   EnsemblFungi; CAK43546; CAK43546; An01g01750.
DR   GeneID; 4978472; -.
DR   KEGG; ang:ANI_1_218014; -.
DR   HOGENOM; HOG000217860; -.
DR   KO; K01279; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
DR   PRODOM; A2Q7S3.
DR   SWISS-2DPAGE; A2Q7S3.
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..646
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002644028"
FT   DOMAIN          212..645
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        288
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        292
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        563
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   METAL           604
FT                   /note="Calcium"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   METAL           605
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   METAL           623
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   METAL           625
FT                   /note="Calcium"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   646 AA;  70071 MW;  E75FF0874B137648 CRC64;
     MKFFSTICSL TLAVSALALP TSDHVIHEKR SATPSRWEKI SRVNGTEHVL VRIGLTQNNL
     DRAYEYLMSV SDSVSPNYGK FWTPEEVHST FAPSNETVNA VRNWLIESGV DESRLVHTKN
     QGWIVFDATT KEAENLLHTK YYHYTDRISG FKTLAAEEYR VPQKIQQHID FIKPGVLLPL
     TSKGPSAKHT KKYKPLKQTS VNATSLTTCD EVITPACVAA LYKIPHASGN VSASNSLGIF
     EEGDYYAQED LDLFFRNFTP YIPKGTHPKP AFIDGASAPV SVADAGAESD LDFQLAYPIV
     YPQTITLYQT DDYDYASGEV ETDGFFNTFL DAVDGSYCTY CAYGECGDSP TLDPTYPDNS
     TGGYKGQLMC GVYKPTNVIS VSYGGQEADL PAYYQQRQCN EFLKLGLQGI SILFASGDDG
     VAGPPGDDST NGCLGNGTIF SPAFPNSCPW VTNVGATKLY PGKTIADGES AVVDPAGHPY
     SVAFSSGGGF SNIYTIPDYQ AEAVAEYFKK HNPPYPYYEG NASFGKNGGV YNRLGRGYPD
     VAANGDNIAE YNAGEFILEG GTSASTPIFS SVINRIIEKR IAAGKGPLGF LNPVLYRNAW
     ALNDITNGSN PGCGTEGFYT APGWDPVTGL GTPNFPKLLD VFLNLP
//

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