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Database: UniProt
Entry: A0A0R3SQM8_HYMDI
LinkDB: A0A0R3SQM8_HYMDI
Original site: A0A0R3SQM8_HYMDI 
ID   A0A0R3SQM8_HYMDI        Unreviewed;       797 AA.
AC   A0A0R3SQM8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Dual specificity protein phosphatase {ECO:0000313|WBParaSite:HDID_0000738901-mRNA-1};
GN   ORFNames=HDID_LOCUS7387 {ECO:0000313|EMBL:VDL59705.1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000738901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000738901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL59705.1, ECO:0000313|Proteomes:UP000274504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UYSG01010930; VDL59705.1; -; Genomic_DNA.
DR   STRING; 6216.A0A0R3SQM8; -.
DR   WBParaSite; HDID_0000738901-mRNA-1; HDID_0000738901-mRNA-1; HDID_0000738901.
DR   Proteomes; UP000046397; Unplaced.
DR   Proteomes; UP000274504; Unassembled WGS sequence.
DR   GO; GO:0017018; F:myosin 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   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
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:SF540; TYROSINE-PROTEIN PHOSPHATASE VHP-1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 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:UP000274504}.
FT   DOMAIN          18..134
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          338..487
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          407..466
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          174..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..688
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   797 AA;  85792 MW;  12968377480E66AA CRC64;
     MYEIPSVTVH QLAPWLFHKE QVAVLDIRSF REYHTSHICS ALNLGGNRAF KRRLLAHRNA
     LAPFIALLVG VSVENLRKFT KIVLYDQNSA EQPFLYSDNF TQFVISGTAE LFPNAVLLQG
     GFVGFCAAYP QLCWQHPDKL PDEEFVGVKG DSGLENLLQE CLYKLYHEIP PSNPLSPGER
     SNISTRQPSS CSSCGSSSSQ QSCDSGVVLS AADSASSTLM LNRKAISRVT SAPIKRPTTV
     VASLSVDDAI MAGSSSRRPS RLRPNTLSLC SPSFSTSATS AAVNTLTNNI MDRPSRCTFA
     SSFRFLSTPP PSTSSLQSSR PASTVSAALS AEAFESPLPT AVLPHLLIGC QADAMSAEVC
     SDFGVTHVIN VSADGEMSPH VSPCRFLRIP IHDNGKADIV QYFDKAFAFL GKAALYLYSA
     KRSGGRVLIH CFAGISRSPT LAIAYLMHNQ RITFDEAYNR VKSLRPKISP NFNFIGQLTD
     FEHRLNLSSL PSATSAVEVN RVPPVIIVPT VSPTQAATPP ENNVPENTPR IMRQASTCCA
     SVVTVSTMTI PASATTSGPV RPVSLSLRRP SLKPLAVVAS KKRDRTQYLS PNSVFFSSSD
     NSSPGDDETS ATYHVSNTTP TLLDAKTSTS QSTFVAHRKR SRFGPLLPSP STAIASLDLS
     SPTEDQNLQS LNNFPSTPPP PPSPRPRRLR RPSPLRVDET RRFSLSTFSD FSRAALAACA
     AAVTSSADAP SSDIDSEIDM AASNPTIISS GLHSPSAAHR WILGDSCRHQ QATAESSCHS
     SLSSSSNSQH TPSFPIS
//
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