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Database: UniProt
Entry: A0A0M3I2Z2_ASCLU
LinkDB: A0A0M3I2Z2_ASCLU
Original site: A0A0M3I2Z2_ASCLU 
ID   A0A0M3I2Z2_ASCLU        Unreviewed;       722 AA.
AC   A0A0M3I2Z2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 2.
DT   08-NOV-2023, entry version 34.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001094001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0001094001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (MAY-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00009580}.
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DR   AlphaFoldDB; A0A0M3I2Z2; -.
DR   WBParaSite; ALUE_0001094001-mRNA-1; ALUE_0001094001-mRNA-1; ALUE_0001094001.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
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   GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR   CDD; cd14513; DSP_slingshot; 1.
DR   CDD; cd11652; SSH-N; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR043587; Phosphatase_SSH-like.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR043588; SSH-N.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45864:SF2; PROTEIN PHOSPHATASE SLINGSHOT; 1.
DR   PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR   PROSITE; PS51998; DEK_C; 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}.
FT   DOMAIN          306..361
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          446..587
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          508..565
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          595..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  82070 MW;  62D3EB39B91BF4F8 CRC64;
     MSLVTVQRSP TPSENANFDH SDADVCECGL SPRKSKSVAS SECFFYVKGT AVILLNHDRT
     NVAHNSANGE IEEHLQAMLR MLPPEDTLTM AVRLQPNSDQ DCLQDHARYL AVVASSSRQD
     IDDSRDAREC VLLGLDCLPG DKATIGVVIP IFASTHVRLD GDGGIAVDCD SSYHLFRPVS
     VQAMWTMFQC LHKELREVQG AKNSPSQTAR PGERLVDYYL RHISSQDAIR AEWERSSSEY
     GIGTSSDLGA TTADAERFSI EGRGNDNSVE AQIHDRLKEV MQTVDLDDVT SKDIRMKVHI
     FVDFFERLEA QIHDRLKEVM QTVDLDDVTS KDIRMKVEES MGINLDDYKD FISRQMMVIM
     GQMDKASQIF PYLYLGTEWN ACDWQWLENN GAHSKCFAIY ESHLNHKDWH RILLRVEVEE
     SMGINLDDYK DFISRQMMVI MGQMDKASQI FPYLYLGTEW NACDWQWLEN NGVQYIVNVT
     NEVENFFPAR LKYLKIRVCD EASTELLKHW NQTNQFIKEA KEKGSAVLVH CKKGISRSSS
     TVIAYAMKEY GWGLSQAMEH VKKKRDCITP NKGFVEQLKT FEGMLDAFKK REQFDAPPST
     STILPESPMR SERRQPRRKH LMSYHISHNI VDVASPICSC NRLSEHGSTV RSLVGSFEAK
     GRGDDSARLT SRTSDTHLER PPVTFRLEKL TDWKTRHSLA VSMPPSCTNT SISQIRALTI
     SQ
//
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