ID A0A178AP17_9PLEO Unreviewed; 1029 AA.
AC A0A178AP17;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=IQ06DRAFT_317597 {ECO:0000313|EMBL:OAK99535.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK99535.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK99535.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK99535.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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DR EMBL; KV441714; OAK99535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AP17; -.
DR STRING; 765868.A0A178AP17; -.
DR InParanoid; A0A178AP17; -.
DR OrthoDB; 53899at2759; -.
DR Proteomes; UP000077206; 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:UP000077206}.
FT DOMAIN 218..424
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 344..401
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 112308 MW; F8C3FF2758057A5D CRC64;
MDSSSVTDPS PGASPESPLA KTAASSSFVA DFRSRRPETS PGDSSPSAFF ELQRPTTPAK
KARNLKNLGI NTTTSLTNLR GHTPAPVAVV NKEKNSSAPP SPLFIKPPTP PKRRPSNLSL
TISTPGSTEN KPTRLVIPST PSFNRPTLRH FQSSPSLPLC APSLGPANGM QLPALRPLVT
KASGLSEVPF EMEEEDDQEQ NFDIPQSREE KPAAYPNGPI CIYEAGVYLY FEPTAEQACT
FDVIINVASE VKNPFTSSTS QSQKDIDARR IDGPPAENVD FASLSQRSKP VTSFGMDDNS
PTTPKATPVM MQTTQPGQLV IDGKTYRTPE YIHMPWEHNT DIVPDLHRLV KIMDDRVQQG
KRVLIHCQCG VSRSASLIVA YGLYKDPHMS VQDAYDRAKK RSKWIGPNMN LIMQLQEFRN
SLLRANDSRS QGFGRRSAGL NTTRSTSNNR YSAFERETTS GSRTPRTAPL PPDSDISMQR
ASTGNMMAIS PGPLSAPTGA FPPSFRRSWD ASQSHFDLSS QPTPTTTTTP YVDPAGHVVP
VLSVPADDVS SPAAETQPIP EVQEPQRQST LQLPSVPNFS RQLPLRTAET SGEVTSSHLQ
VGQPAGLQPL SFGALKSPAV ASFNLSSSFA PQGQFESSEI MSPIKTTFDN PWPSGYDVEP
SSFATKSQDR EYEASATLVS PRSEEFHMTG FNPSGIDESY GMLSPRATSF DLSTPSKSPT
FGSSFEPAEL VSPTTTQFPR DIFGKAEEST SEELMSPRAE EFHMSPFKPE VAPDEDPFGL
TSPTRFDVPG NPFDRPTLAI THDDEAEDRR PSFQAILPPS HQTFNGFGSL DASAQAQPSY
PEPLAFRVLG VQPPSDSPAR IDSLSTSPAT QEVPMKTTWD IDSSPLPKAP ATPQTPKEAF
LSTPSKGIRT RFSSPNLRAQ RKLHKLQTEM ESRLPKKAPS PQHAADDIDA LMSPRAEEFT
RNPFRFELQV SAEDNSPVSS NETIKDGRNG HDWSDPLPRQ WTPEKATVDP RSPVQTGSSP
IVRNIWDVL
//
