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Database: UniProt
Entry: I1S1B6_GIBZE
LinkDB: I1S1B6_GIBZE
Original site: I1S1B6_GIBZE 
ID   I1S1B6_GIBZE            Unreviewed;       385 AA.
AC   I1S1B6; A0A098DBY3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=FG10516.1 {ECO:0000313|EnsemblFungi:CEF75955};
GN   ORFNames=FGRAMPH1_01T08303 {ECO:0000313|EMBL:CEF75955.1};
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF75955.1, ECO:0000313|Proteomes:UP000070720};
RN   [1] {ECO:0000313|EnsemblFungi:CEF75955, ECO:0000313|Proteomes:UP000070720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC   {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC   9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF75955};
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2] {ECO:0000313|EnsemblFungi:CEF75955, ECO:0000313|Proteomes:UP000070720}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC   {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC   9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF75955};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3] {ECO:0000313|EMBL:CEF75955.1, ECO:0000313|Proteomes:UP000070720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC   {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC   {ECO:0000313|EMBL:CEF75955.1};
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4] {ECO:0000313|EnsemblFungi:CEF75955}
RP   IDENTIFICATION.
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC   {ECO:0000313|EnsemblFungi:CEF75955};
RG   EnsemblFungi;
RL   Submitted (JAN-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601}.
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DR   EMBL; HG970332; CEF75955.1; -; Genomic_DNA.
DR   RefSeq; XP_011319509.1; XM_011321207.1.
DR   AlphaFoldDB; I1S1B6; -.
DR   STRING; 229533.I1S1B6; -.
DR   EnsemblFungi; CEF75955; CEF75955; FGRRES_10516.
DR   GeneID; 23557419; -.
DR   KEGG; fgr:FGSG_10516; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G08303; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   HOGENOM; CLU_023312_0_0_1; -.
DR   InParanoid; I1S1B6; -.
DR   OrthoDB; 5472710at2759; -.
DR   PHI-base; PHI:5768; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR016278; DUSP12.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45848:SF4; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12; 1.
DR   PANTHER; PTHR45848; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12 FAMILY MEMBER; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PIRSF; PIRSF000941; DUSP12; 3.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070720}.
FT   DOMAIN          104..143
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          153..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        127
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000941-50"
SQ   SEQUENCE   385 AA;  43464 MW;  770030E2EC47B0D8 CRC64;
     MALSRIDGQD ELFVGGLWAL RRSDSLTDRR ITHVLSLVPF DISSLKNFKD EPWIDYGKDF
     RHQLIDIDDV EDSDLLIELP KAVRFIEEGL GANYMEHADD DGGVSLEKDV DVVEKKRKKK
     GGVFVHCAVG KSRSVSAVIA YLLRRYPSRF DPNITPTAIS DPSQSTGSET SAEKRSRKET
     AQEAVHAALT YVRRTRPMAE PNEGFMEQLA LWWEMECPDD VESHPVYQRW AYKREIDENL
     AVGQAPTRLR FEDEETQPHD DSGLSLRCKK CRRTLVTAPF IMEHKPSEKK SSASTCQHYF
     VEPLSWMRGV LEKGELNGRL LCPNDKCGAG VGRYDWKGFR CSCGGWVTPA FSLQKARVDD
     VVKRPTGQSM GIRMPPGQAP RSGNL
//
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