(data stored in SCRATCH zone)

SWISSPROT: Q4W9J4_ASPFU

ID   Q4W9J4_ASPFU            Unreviewed;       578 AA.
AC   Q4W9J4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   SubName: Full=Protein tyrosine phosphatase (Pyp1), putative {ECO:0000313|EMBL:EAL84619.1};
DE            EC=3.1.3.48 {ECO:0000313|EMBL:EAL84619.1};
GN   ORFNames=AFUA_4G04710 {ECO:0000313|EMBL:EAL84619.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84619.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84619.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL84619.1}.
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DR   EMBL; AAHF01000016; EAL84619.1; -; Genomic_DNA.
DR   RefSeq; XP_746657.1; XM_741564.1.
DR   STRING; 746128.CADAFUBP00009550; -.
DR   EnsemblFungi; EAL84619; EAL84619; AFUA_4G04710.
DR   GeneID; 3503955; -.
DR   KEGG; afm:AFUA_4G04710; -.
DR   EuPathDB; FungiDB:Afu4g04710; -.
DR   HOGENOM; HOG000170253; -.
DR   InParanoid; Q4W9J4; -.
DR   KO; K19806; -.
DR   OMA; GNIRQNM; -.
DR   OrthoDB; 411281at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; Q4W9J4.
DR   SWISS-2DPAGE; Q4W9J4.
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00160,
KW   ECO:0000256|SAAS:SAAS01031440, ECO:0000313|EMBL:EAL84619.1};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01031415};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          32..148
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          287..566
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          462..557
FT                   /note="TYR_PHOSPHATASE_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          394..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..415
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        497
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   578 AA;  65109 MW;  24E1D23632950126 CRC64;
     MATYDNTLSG NLAPTTINTM SCEQCAELLE TCGNDVLLLD VRPYAHYARG HIKGSLNLCI
     PTTLLKRTSF DTRKLANTFT SDIDRRSFSR WKQCRYIIVY DAATLDMKDA VPMINMLNKF
     TAEGWNGEGS ILRGGFKVFC NQFNALVQQP ESSNPGISSN KPNSMQISLP PFAPIAGGCA
     LPESSSAAIP FFGNIRQHMD LMGGVGQIPL QLPQNLTDSK RRLLPRWLRD ASDVEDGGQK
     VSEKFLELEK KELDRMKQAL SYEMTGVSTS AQAPSKKYRV AGIEKGNKNR YNNIYPFDHS
     RVRLQDVPSG GCDYVNANYM KAEYSNKRYI ATQAPVPETF DDFWRVIWEQ DVRIVVSLTA
     EIERGQVKCH RYWESGNYGP FRVNNFSERR IPMKASGSRQ NQGQSTTSLS DSSEEPSEPC
     IIVRHFGLSH SAFPFQPLRE VTQLQYPYWP DFGTTSQPSH LLQLVDECNA IIRATSNTCF
     DTRKAMPTEH RPVLVHCSAG CGRTGTFCTV DSTEPREISE RPDTGWIYND NVDLIAKAVA
     DFRTQRPSMI QNLSQFVLCY ESVLEWMVVQ MDEGCENP
//

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