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Database: UniProt
Entry: A0A1I7S9I4_BURXY
LinkDB: A0A1I7S9I4_BURXY
Original site: A0A1I7S9I4_BURXY 
ID   A0A1I7S9I4_BURXY        Unreviewed;       319 AA.
AC   A0A1I7S9I4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   10-APR-2019, entry version 9.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0968000.1};
RN   [1] {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0968000.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21909270; DOI=10.1371/journal.ppat.1002219;
RA   Kikuchi T., Cotton J.A., Dalzell J.J., Hasegawa K., Kanzaki N.,
RA   McVeigh P., Takanashi T., Tsai I.J., Assefa S.A., Cock P.J.,
RA   Otto T.D., Hunt M., Reid A.J., Sanchez-Flores A., Tsuchihara K.,
RA   Yokoi T., Larsson M.C., Miwa J., Maule A.G., Sahashi N., Jones J.T.,
RA   Berriman M.;
RT   "Genomic insights into the origin of parasitism in the emerging plant
RT   pathogen Bursaphelenchus xylophilus.";
RL   PLoS Pathog. 7:e1002219-e1002219(2011).
RN   [2] {ECO:0000313|WBParaSite:BXY_0968000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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}.
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DR   STRING; 6326.BUX.s00649.36; -.
DR   WBParaSite; BXY_0968000.1; BXY_0968000.1; BXY_0968000.
DR   Proteomes; UP000095284; Whole Genome Shotgun Assembly.
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:UP000095284};
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}.
FT   DOMAIN      122    127       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   319 AA;  35492 MW;  1B3AA9EAEB47C7E0 CRC64;
     MAGTASNLNL TDLLIRLLSV GNPEKGLTKT VKDEEILTVC AKAHDVFLSQ SVFVEIDPPV
     RICGDTHGQY GDLLRLFNRG GFPPTSNYLF LGDYVDRGRQ NLETILILFI YKLKYPNNFF
     LLRGNHECAN INKVYGFAEE CARRYQQSGQ RIWQAFQDVF QVMPLSGLVG DRILCMHGGI
     SPQLKSLKQL RDIKRPNDAT GPTLEMDLLW ADPVVGLTGF QENMRGASFG FGPDVLAKLC
     AELNIDMVAR AHQVVQDGYE FFGNRKLVTI FSAPHYCGQF DNAAAMMIVD SNLVCSFQIL
     RPTLGRGVTK TVPTSQGKC
//
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