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Database: UniProt
Entry: A0A067JRC7_JATCU
LinkDB: A0A067JRC7_JATCU
Original site: A0A067JRC7_JATCU 
ID   A0A067JRC7_JATCU        Unreviewed;       933 AA.
AC   A0A067JRC7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   RecName: Full=Dual specificity protein phosphatase PHS1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=JCGZ_26381 {ECO:0000313|EMBL:KDP22550.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP22550.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP22550.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP22550.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
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DR   EMBL; KK915447; KDP22550.1; -; Genomic_DNA.
DR   RefSeq; XP_012090601.1; XM_012235211.1.
DR   AlphaFoldDB; A0A067JRC7; -.
DR   STRING; 180498.A0A067JRC7; -.
DR   GeneID; 105648730; -.
DR   KEGG; jcu:105648730; -.
DR   OrthoDB; 325201at2759; -.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0043622; P:cortical microtubule organization; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:InterPro.
DR   CDD; cd14498; DSP; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR015275; Actin-fragmin_kin_cat_dom.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR035010; PHS1.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
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; PTHR47100; DUAL SPECIFICITY PROTEIN PHOSPHATASE PHS1; 1.
DR   PANTHER; PTHR47100:SF5; DUAL SPECIFICITY PROTEIN PHOSPHATASE PHS1; 1.
DR   Pfam; PF09192; Act-Frag_cataly; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT   DOMAIN          701..846
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          766..822
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  103513 MW;  F28BF760A66A5A82 CRC64;
     MAKEQKESSA SIINTTLQAQ DKEEEGELDL GSDEADTPLP LTVTSRVLYM LGDITSGPAY
     RFAQWLELVR KRSVKHHASG FPRRPHGLDT MTSGARELLI DPKSDPPPEQ ASEISLWERL
     GKAAILDIES SSFSWDMLSS LHHTEHSSST EQSEDEMNKA LEVTVNSGGV VFFALFNQPG
     INDALPKEAA AVIKFSSSRM ATQSERLGYE FAKWLGVRTP QARVIHNCSA EWLQIKEAAE
     KARDTAASEG DEVGEVTCSE LLEALELSRC LLLMSYIHGS PLLESSTAFE SRETATALGR
     VLMLDLVIRN EDRLPCRQLR WRGNAANLLL ADQMASANVN ELEDAFDSAI NRYRPRVVRA
     LQKERRATSV DSRLSSHESG LVSQGSDLSD VTESPKSCSK SLRSQASNES IFSELYRSRI
     VAIDSGVPRR PPAGKRANDQ ANYPKLVELL LNCSDYASNL LYDITGGKLG SPLEDPNITD
     IRPTEITAVV QEFRSGFRAA LRDLQSFHIF LLTLHQKLDA LLRAFLNITN RTGDFDKEDI
     VVPESPLHGG VHCPSSPTPS KDRFLNDNNS DFSDSELQRT APRSSSGNKE NSDSRSPMAK
     EGWHGKFKAS GEPLHSLRLT TKLRDIHKFA KVDTESNKEL EQWNEMLRND AIKLCQENNF
     NTGFFEGSDS NCVVDAYELK VRLEHILERI SLISDAANTE KPSSITNSLF IGGALAARSI
     YTLQHLGITH ILCLCANEIG QSDTQYPDLF EYRNYSVYDN EDSNISSIFE EASDFIDHVE
     STGGRVLVHC FEGKSRSATL VLAYLMLRKN FTLLQAWNAL RRVHRRAQPN DGFARILLDL
     DRKLHGKVSM EWQQRKPTIK VCPICGKNAG LSSSSLKLHL QKSHRKLSSG SVDSAMTMEI
     QKALDALKMT SGSGSGSVSP QQSSSVMDDL ELV
//
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