(data stored in SCRATCH zone)

SWISSPROT: Q75CG0_ASHGO

ID   Q75CG0_ASHGO            Unreviewed;       765 AA.
AC   Q75CG0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 117.
DE   SubName: Full=ACL041Cp {ECO:0000313|EMBL:AAS51187.2};
GN   ORFNames=AGOS_ACL041C {ECO:0000313|EMBL:AAS51187.2};
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:AAS51187.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51187.2, 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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000256|SAAS:SAAS01128831};
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DR   EMBL; AE016816; AAS51187.2; -; Genomic_DNA.
DR   RefSeq; NP_983363.2; NM_208716.2.
DR   STRING; 33169.AAS51187; -.
DR   EnsemblFungi; AAS51187; AAS51187; AGOS_ACL041C.
DR   GeneID; 4619488; -.
DR   KEGG; ago:AGOS_ACL041C; -.
DR   HOGENOM; HOG000115788; -.
DR   InParanoid; Q75CG0; -.
DR   KO; K19806; -.
DR   OMA; HDFYTCI; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   Gene3D; 3.40.250.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTPase_domain.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   4: Predicted;
DR   PRODOM; Q75CG0.
DR   SWISS-2DPAGE; Q75CG0.
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00160,
KW   ECO:0000256|SAAS:SAAS01031440};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01031415};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          98..228
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          457..727
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          631..718
FT                   /note="TYR_PHOSPHATASE_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          20..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        652
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   765 AA;  85735 MW;  13385CA5B7960D47 CRC64;
     MVLKGGEYYR VGYGPGHKST LSDSVSILSN SSTTAEEGGP GGPAHAKTRS AGMVEGPAVP
     HGSSAYKVGV SAGGGLRFPL HAGCRTMDSR ALGNMLNEDA NTVVVDTRPF VEYSKSHVRG
     ALHVCLPSTL LRRKTFSLAR LLENLPPGDR ESVRERLREH TQGERSLSIV IYDNLPMKGD
     GWSSLACAGL SAKFLENNWE AEGQNVPDVY ILSDGYQQFQ LQFAELSEAL PASADDDLLC
     QPPGLCASAS SLSTPSSFRG SPLEPLPSPL TTSPMSQLFK FQLPTQRPLQ NGSSHAFPRV
     FKMRHFEENS NLESYLGAVD INENRKLSEF DETSDSNGTR FQQSFFKFPL KLSFQLEYAK
     ITELYKQEEI DCVIPKWFQD LMLKPSKMQY VEQFQRLDIL ERTRLDRILN TPFGDKINSV
     STIPCDINDA ELANYFDYDK EYDPEITISS GVELGAKNRY KDVFPYEHTR VVLRRDSELR
     STTVPFEKDS VIDTYINANY LTSPFDSGKK SGSAGRYIAT QAPLPETIHD FYTCIINNNV
     PVVLSLTDEF EHGIEKCCKF WADGEYNGIV VSMLEEHKGE VLFIRRIKIT YNDGKSSYEL
     LQIQIKDWPD LGILDSPKDI IDMIFLKDYV IQQLMSDGIF AEDEMPTVLV HCSAGCGRTG
     TLCTVDSVIS NLTEIAHQSE QWASSKSTAS GVFDPIVTII DRFRKQRISM VQTITQYLFI
     YDCMLRYFKI RLETINEGSD SNRVRSLIGE QDILGNFIRS KITAR
//

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