ID A0A075APJ9_ROZAC Unreviewed; 270 AA.
AC A0A075APJ9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE Flags: Fragment;
GN ORFNames=O9G_003513 {ECO:0000313|EMBL:EPZ32049.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ32049.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ32049.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ32049.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
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; KE561190; EPZ32049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075APJ9; -.
DR STRING; 988480.A0A075APJ9; -.
DR EnsemblFungi; EPZ32049; EPZ32049; O9G_003513.
DR HOGENOM; CLU_023312_1_0_1; -.
DR OMA; KIGSFSW; -.
DR OrthoDB; 5472710at2759; -.
DR Proteomes; UP000030755; 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; cd14498; DSP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR016278; DUSP12.
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; PTHR45848:SF4; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12; 1.
DR PANTHER; PTHR45848; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12 FAMILY MEMBER; 1.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000941; DUSP12; 2.
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:UP000030755}.
FT DOMAIN 1..130
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 46..106
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT ACT_SITE 74
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000941-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPZ32049.1"
SQ SEQUENCE 270 AA; 30862 MW; 63CBA6C520333E40 CRC64;
YAAARDLKLL EKNKVTHILN VAHLNQDGLV NGVETINYNI QDIPEFNFLV LFDEITEKMH
SVLANPRNRL VVHCSAGISR SATIVIAYLM RYKTMKFDEA FEVLKRNHVV AHPNSGFTLQ
LKIYDSFSCS FNVNDGKCKG IQSVLDTKNL PLITSFLTER IENTSKENSR FSYLRCGKCR
SMVVESNHVL DHSVKNECRI YFTEPLTFMT ETELQQPSGK IYCKKCKNKL GSFSWSGTTC
SCGEWIVPSF AISKDKVDPQ YEKKIQFDFL
//
