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Database: UniProt
Entry: A0A1L9P3M9_ASPVE
LinkDB: A0A1L9P3M9_ASPVE
Original site: A0A1L9P3M9_ASPVE 
ID   A0A1L9P3M9_ASPVE        Unreviewed;       674 AA.
AC   A0A1L9P3M9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=ASPVEDRAFT_122722 {ECO:0000313|EMBL:OJI96098.1};
OS   Aspergillus versicolor CBS 583.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJI96098.1, ECO:0000313|Proteomes:UP000184073};
RN   [1] {ECO:0000313|Proteomes:UP000184073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV878125; OJI96098.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9P3M9; -.
DR   STRING; 1036611.A0A1L9P3M9; -.
DR   VEuPathDB; FungiDB:ASPVEDRAFT_122722; -.
DR   OrthoDB; 2045814at2759; -.
DR   Proteomes; UP000184073; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:GOC.
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   GO; GO:0033260; P:nuclear DNA replication; IEA:InterPro.
DR   CDD; cd14516; DSP_fungal_PPS1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR047949; PPS1_DSP.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR47550; DUAL SPECIFICITY PROTEIN PHOSPHATASE PPS1; 1.
DR   PANTHER; PTHR47550:SF1; DUAL SPECIFICITY PROTEIN PHOSPHATASE PPS1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184073}.
FT   DOMAIN          497..646
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          565..633
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  75189 MW;  0C61C7D9EBDA67D2 CRC64;
     MATVVVQQQP LRHTTPPPGS VSPALSLNRT SSPVPNKHIP VCPTGPSPIP SRTSSPTPKE
     DAYLPASSPL HPPDAFPKIA ESPPLYSIEI EILEAAVKHC SSQPLPDPNL MFPWLHGLHP
     ENHLQIGFFT NRRRSLRRTP KCWRGLTIVK VGGDLTTSRL KGAVAPDAIL APSGFEFLAV
     DPREGFSVRN FHIQTAKLAP LSDIVVYGQD GVTAKQLLDV AGRITAAQHH WRLSSDHDQT
     LPSYNTFIVS CPFSDIERRA PSLVAVNSSG HLTDQVVDLF QLERLEMCTM SRATELSKNV
     WQGPTPDYLL QAGTSGAPSA ESFDLMIDAN DLAGIPGPRH LANLAKRLAT EPQRLEFPSS
     GSLLLPSGES RDVDDLINTL RWIFYLANPE IPETDAEGDT PMDESPKKSR KILIHCPDGY
     TESSLLVIAY TMFAEGIPAS EAWLRLHREK KRNFFAYPSD VAFLRNVQER ILQESPANPA
     QYRLTDPRWF SFCDGSLPSR ILPYMYLGNL SHANNPEMLW ELGIRRVLSI GEAVTWTDSD
     IAKMGAENVM HITKVQDNGI DPLTEEFDRC LEFIRKGKSD GAATLVHCRV GVSRSATICI
     AEVMASLNLS FPRAYCYVRA RRLNVIIQPH LRFVYELLKW EELQQKKNKQ PLKRELEWAT
     VAREIALMNK PYSR
//
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