(data stored in SCRATCH zone)

SWISSPROT: Q751M3_ASHGO

ID   Q751M3_ASHGO            Unreviewed;       563 AA.
AC   Q751M3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   SubName: Full=AGL326Wp {ECO:0000313|EMBL:AAS54165.1};
GN   ORFNames=AGOS_AGL326W {ECO:0000313|EMBL:AAS54165.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54165.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54165.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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DR   EMBL; AE016820; AAS54165.1; -; Genomic_DNA.
DR   RefSeq; NP_986341.1; NM_211403.1.
DR   STRING; 33169.AAS54165; -.
DR   EnsemblFungi; AAS54165; AAS54165; AGOS_AGL326W.
DR   GeneID; 4622634; -.
DR   KEGG; ago:AGOS_AGL326W; -.
DR   InParanoid; Q751M3; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IBA:GO_Central.
DR   GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR017141; Pept_M20_carboxypep.
DR   InterPro; IPR002933; Peptidase_M20.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
PE   4: Predicted;
DR   PRODOM; Q751M3.
DR   SWISS-2DPAGE; Q751M3.
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037217-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR037217-2}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..563
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004286603"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT   ACT_SITE        229
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT   METAL           194
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT   METAL           194
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ   SEQUENCE   563 AA;  62521 MW;  F0E3A6EF38876318 CRC64;
     MMFAAWPLGQ PISFATALAL LACFSAQTAR SAVVSSEVTG ASLPSCWDVS KPQGGFGDHL
     QQILHNSTLS NLTVEKLQRA VQIPSAWVVD AADCCTAVKS DTETYKQFKR LHEQLSRDFP
     LVWCKLKVET VNELGLLVTW PGSDSGAKPA LISANMDVIV QDQDDLSTSS QFEGKIENEQ
     KQRRTNIHGR GAFDKSHLVG LLEALEYTLE TDPSFQPKRT IVLALGFDEQ LGGELGAAEI
     SKKLESQYGS DSFSVVLGKD VAGVVETYGA YLAPIGVATK QDVRFTFRFN FSDMYRTSPL
     MPTNEFRIFG NISDALNRFP ERYDFTKANP LTSLFQCAAN DFKYMPEEQI KDLLAALEDQ
     DANNRFTDFL RSQPTNYAGF AFTTVQQFSF IHGGSIHAVR PEYLQFEIKE SLTLDTSVEL
     RTELIKAALK EVGPMGLIVN GEVIDAIDSG ITCEVLVDAD TKDEPSPNSD DLELLASTIK
     GLYEDSIFPD LPDKPSKLNV GTSFSAIKTD SSHYKNLSKH VYYFRPGFFQ DFVIPSFNTR
     KEHVGVQTLL YTVAFFYQYV HSL
//

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