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}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
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
//
