ID C0NI27_AJECG Unreviewed; 617 AA.
AC C0NI27;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=HCBG_02999 {ECO:0000313|EMBL:EEH09462.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH09462.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG663365; EEH09462.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NI27; -.
DR STRING; 447093.C0NI27; -.
DR VEuPathDB; FungiDB:I7I50_09890; -.
DR HOGENOM; CLU_017787_1_1_1; -.
DR InParanoid; C0NI27; -.
DR OrthoDB; 9871at2759; -.
DR Proteomes; UP000001631; 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:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR044506; CDC14_C.
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:UP000001631}.
FT DOMAIN 241..388
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 309..374
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 32..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 67979 MW; 51355177A6582C2C CRC64;
MPSVMGSYGQ VIEYIQDRLY LASYTHPPSE GAPFSYPVQP KSPSKRSSKA AHGGSAAAGP
RSKPPVYFTV DDTLLYNAFH ADFGPLHIGH LYRFAVHFHE ILGDPANCER PVVFWSKPDS
RSRANAACLV ACYMVLIQSW PPHLALAPIA QADPPYMPFR DAGYSQADFV LTIQDVVYGV
WKAKEEGLCG LKDFSLEEYE KFERVDMGDF NWITPHFLAF ASPQHQQIDP IPPNTPEFAA
LPSTITEVLI SDLPVPFKNV LSHFSSRNIG LVVRLNSELY SPSHFTAMGI SHMDMIFEDG
TCPPLPLVRR FIKIAHEMIH KKKGIAVHCK AGLGRTGCLI GAYLIYRHGF TANEVIAFMR
FMRPGMVVGP QQHWLHLNQT SFREWWFEDC FKEKLAMANP TTPGRAHPKQ QRIISTNGQT
ATPPHPSQKR HALGEIDNNE ASAYADDTLP APTPGQPRKS HRKDSRHHPY ARAVSSGLGS
EAGLETSVSR NGTTKEGNRR RLTEHNSPSE SDEELQLQML ARRASSRTPV SPSQQRSTSH
SATVSLSIHE DVEDYADAVV VSSQPKSTPV AKSGSGILGV GKVRGSARRG IEGKTADKGV
RKHSGRVGSA GAVSRLK
//