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Database: UniProt
Entry: A0A0B2W1K3_TOXCA
LinkDB: A0A0B2W1K3_TOXCA
Original site: A0A0B2W1K3_TOXCA 
ID   A0A0B2W1K3_TOXCA        Unreviewed;       328 AA.
AC   A0A0B2W1K3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=Ppp1cc {ECO:0000313|EMBL:KHN87497.1};
GN   ORFNames=Tcan_11074 {ECO:0000313|EMBL:KHN87497.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN87497.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN87497.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN87497.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J.,
RA   Yang Y., Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W.,
RA   Jex A.R., Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01116782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KHN87497.1}.
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DR   EMBL; JPKZ01000423; KHN87497.1; -; Genomic_DNA.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031036};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT   DOMAIN      125    130       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   328 AA;  37526 MW;  3F3B117EE43E4FA2 CRC64;
     MVSRRRPEQY NEFDVNDVLR RLLAVKTYQK SLDVTEHELK MICNLSRSIF MSQPMLLELE
     SPLKIAGDIH GQYSDLIRLF DLCGYPPESN YLFLGDYVDR GPKSIETIAL LLCYKIKYPK
     NFFVLRGNHE VANLNRIYGF YDECKRRCNV KIWKCFQDVF NCMPIAALIE HKILCCHGGL
     SPSLRSLEQI RRITRPVDVQ ETGLVCDILW SDPDPNVIGW APNERGVSYV FGPEVLAQFL
     RRMDLDIVVR GHQVVEDGYE FFGRRGLVTI FSAPNYCGEF DNAGAIMSVD ENLLCSFQKD
     IESASKFGHS ATRLKVALEA CVCVVQDI
//
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