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Database: UniProt
Entry: A0A225AK32_9EURO
LinkDB: A0A225AK32_9EURO
Original site: A0A225AK32_9EURO 
ID   A0A225AK32_9EURO        Unreviewed;       618 AA.
AC   A0A225AK32;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=UA08_02280 {ECO:0000313|EMBL:OKL61882.1};
OS   Talaromyces atroroseus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Trachyspermi.
OX   NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61882.1, ECO:0000313|Proteomes:UP000214365};
RN   [1] {ECO:0000313|EMBL:OKL61882.1, ECO:0000313|Proteomes:UP000214365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61882.1,
RC   ECO:0000313|Proteomes:UP000214365};
RA   Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA   Mortensen U.H., Thrane U.;
RT   "Talaromyces atroroseus IBT 11181 draft genome.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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:OKL61882.1}.
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DR   EMBL; LFMY01000003; OKL61882.1; -; Genomic_DNA.
DR   RefSeq; XP_020122003.1; XM_020264305.1.
DR   AlphaFoldDB; A0A225AK32; -.
DR   STRING; 1441469.A0A225AK32; -.
DR   GeneID; 31002035; -.
DR   OrthoDB; 9871at2759; -.
DR   Proteomes; UP000214365; Unassembled WGS sequence.
DR   GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd17657; CDC14_N; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR029260; DSPn.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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; PTHR23339:SF27; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF14671; DSPn; 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   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214365}.
FT   DOMAIN          241..399
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          319..385
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  68746 MW;  A5CF94C58F014582 CRC64;
     MPSHAATAHG QVIEYIQEYA DTHPATFTDR LYLASYSSAP DPYGPPPFPS QQSSSPSKRS
     KASQSPVRAP KRKLPVYFTV DDTLLYNAFH ADFGPLHIGH LYRFAVHFHE ILGDPANTDR
     AVVFYSKPDG RSRANAACLV ACYMVLIQSW PPHLALAPIA QADPPYMPFR DAGYSQADFI
     LNIQDVVYGV WKAKEEALCA LKDFSLEEYE RYERVDMGDF NWVTPHFIAF ASPQHQPVAP
     IPANTPEYAA LPSTLSQVQA SKLPVSFKNV LSHFSSRNVG LIVRLNSELY CPSYFTALGI
     NHIDMIFEDG TCPPLPLVRR FIKMAHDMIT VQKKNIAVHC KAGLGRTGCL IGAYLIYRHG
     FTANEIIAYM RFMRPGMVVG PQQHWLHLNQ GAFREWWFED TMRERLALAA PVTPGRQVTK
     QRSSNGQTVT PPNGGNSRRA ALGEIDNNEA ANYHNDENLP APTPGQPRKS HRKDSRHHPY
     ARNVSGTLAV NSESEKDRSS PKRTQRAGTE QSESEEEIQM RMLAKRASRS PSASPKARSI
     SYSTTVTTSY EVHEDRENWV ESAVVTQKTP TSSRSPIAVG KVRASPRRVT DSKSDAKGVR
     KISGRVGSIG TSSPTRVK
//
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