ID A0A0B2WRV7_METAS Unreviewed; 816 AA.
AC A0A0B2WRV7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=MAM_05818 {ECO:0000313|EMBL:KHN96232.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN96232.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHN96232.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN96232.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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:KHN96232.1}.
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DR EMBL; AZHE01000016; KHN96232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WRV7; -.
DR STRING; 1081103.A0A0B2WRV7; -.
DR HOGENOM; CLU_012050_0_0_1; -.
DR OrthoDB; 53899at2759; -.
DR Proteomes; UP000030816; Unassembled WGS sequence.
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; cd14521; DSP_fungal_SDP1-like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF531; DUAL-SPECIFICITY PROTEIN PHOSPHATASE SDP1-RELATED; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816}.
FT DOMAIN 329..518
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 438..489
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 40..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 89007 MW; FCAE9574123F40B7 CRC64;
MPSAAARRLY EDQIPSFMSV FDLEADTIAE GETVTLVDTN MVDTPSKPSC FTDPSQPSSL
GQGGPPSDPT HRHHDSTSTQ MSESTESSPT TTLSTSDSSP LSDPSPSSSP DSPIHLIPLN
DYPSTTFGCR SGASQNNMLC VPESRALDRP MTSPAPRRPR NMKGLSIQPP LTISTSSKYV
ATEPSSPSFI KPKIPATKRK PSQLSLKTGA SDLAKKTSLE VPASSALPPI LQRRALKHST
SSPHIFAAMK SSTFGPPGGM TFPKVLERNE SGLSEMLRPT KQKSLMDLDD AIVEEDSPIK
TQLASLSDYK PFHEAVHNED QKSPGYPDGP IAMYGDRIFL YLEPTAEEAS RFDVVINVAR
EVRNPFEAAE RISEHASTPE NESPIPDTAA TMASFTTAFE YQLTEDSSID TPTTPKANPL
HVPEYIHIPW DHNTDIAPDL MHLCETIENR AQNGKKVLIH CQQGASRSAS LIIAYGLYQS
PDLSVNDAYY AAQAKSRWIS PNMKLMYSLQ DFHKEVAKKK RSPSSSAHRP RTGRSPTKHR
LTLSADAIDI TSKEPHTAPL PGEDISSEAM DSDCPSRPRG NSTPSSQTIS PGPASAPLSY
SWKEHCEDPV PEPSPSIPSR PFEPALPHLQ PLPAVPTGEA FSPRFDAAIL AKPDNLPRRP
KTGLGRPEPI FENLSQTSTI LGLRSFDSHA VFSSFPLRKF QKLSPRNPID GTHLERTVTV
SRSHLDETAL LSPRAEVMTT NPLHDVHEVA GMRFVESPPT PTEGLFSPRE SSFPSDPFSF
FGRMMGFSRP AQAADPRSPP TRGEAPIIRS IDELLQ
//
