ID A0A1X2IBU7_9FUNG Unreviewed; 267 AA.
AC A0A1X2IBU7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=BCR42DRAFT_418508 {ECO:0000313|EMBL:ORZ13535.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ13535.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ13535.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ13535.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
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:ORZ13535.1}.
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DR EMBL; MCGE01000016; ORZ13535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IBU7; -.
DR STRING; 90262.A0A1X2IBU7; -.
DR OrthoDB; 53899at2759; -.
DR Proteomes; UP000193560; 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 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:UP000193560}.
FT DOMAIN 81..233
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 157..222
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 45..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 29925 MW; EAC901008A910521 CRC64;
MMTQLSHPSI PNYPALSDPP TATSALALRR KSLKQLRLYP RTIDKIFSPS PSHSTTKRQK
LSSATETYQK TPHQHPSYKK GPIAILPHLY IGNETNAHTW DQLIGIDCIL NVAAEVGQPK
YQSIVPWLDK MKKPATDSSK GYYKLATLQH GEELQIDDAI HLIDQAKKNK KSTLVHCQCG
VARSASVVIA YIMRYLDLPL HEAYAFVQKR APAISPNLTL LYQLQSLEKN HHHLPLVSNQ
SPGVDNNNVS NTPSKNNNKK RKLDLLC
//
