ID A0A0D2CFP5_9EURO Unreviewed; 874 AA.
AC A0A0D2CFP5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Protein-tyrosine-phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_01302 {ECO:0000313|EMBL:KIW48737.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW48737.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW48737.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW48737.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR EMBL; KN847332; KIW48737.1; -; Genomic_DNA.
DR RefSeq; XP_016268953.1; XM_016401900.1.
DR AlphaFoldDB; A0A0D2CFP5; -.
DR STRING; 215243.A0A0D2CFP5; -.
DR GeneID; 27353376; -.
DR VEuPathDB; FungiDB:PV06_01302; -.
DR HOGENOM; CLU_001645_11_0_1; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd01446; DSP_MapKP; 1.
DR CDD; cd18533; PTP_fungal; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
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_Pase_dom.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF551; TYROSINE-PROTEIN PHOSPHATASE 3; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT DOMAIN 293..405
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 544..851
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 730..842
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 95718 MW; ACB8FFEEE5DDED41 CRC64;
MTCHHTTTSS PRSSGLATNV NMSAVATTSI KSPSHSHSHS KSHSHSHSHS RSSRPSTTPR
AQPVAASVGQ PLPPLLSPQS RSPHHTKDPK SPSPSYFGFV VGGDDSIPPD SNPGAHARQN
WNFGNAGIQS GVPTPRHVPV EANPEFEAFR RQSEHNHRFA LNTAFSRPSQ SRNNSTSTSH
TEAPSPLTKL PELGRRTNTS EDSTGQGPKT SNASFFDLPR QQSPVSLNLP HSVADYQHAR
LSLPDNGLRT PPMNLVRQTS RSDTLPLSGQ KDMAPLAAPV HIAEILKDES SLVLVLDLRV
YQQYANSRIQ GALNLCIPTT LLKRPAYNVQ KLADTFASGR DQEMFSRWRE CSHIVVYDAN
SSSSKEAVTP LNVLKKFTTE GWHGVGLVVK GGFLAFQKQV PDLVDSGSVQ SGAGNSAQPL
SISAPANDTL AVAGGCAMPT TKSAANPFFG NIRQNMDLLD GVGQMPIKKP TNLSSEAEGS
LPTWLKRASS NSDDGKLVSD RFLNIEKSEQ KRMQDALSVH VSYGTPRSEK PTKIQVAGIE
KGSKNRYNNI FPYDHTRVRL QDVPNDSCDY INASHVKAEY SNRHYIATQA PIPATFNDFW
RVVWEQDVRV IVMLTAEAEG GQVKSHVYWK TGEFGALKLK QLSERRVSLE SKSTAPRTPA
SSRPTLGPRR STTANIPLKD DAKSPTTKSP SAVVRHFSLS HSAHPFQPMR EVTQIQYEDW
PDFGAPASPN ELLGLVEQVN KYVRGSSSPS SVVGPDEATP EGARPIVVHC SAGCGRTGTF
CTIDSVIDML KRQRLSHEGG GDKMDIDDGD WVDRDDVDLV AKTVDDFRHQ RLSMVQNLRQ
FVLCYESILQ WLVQQNDPTH TKRPGVRDPR RSYG
//
