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Database: UniProt
Entry: A0A0N4T265_BRUPA
LinkDB: A0A0N4T265_BRUPA
Original site: A0A0N4T265_BRUPA 
ID   A0A0N4T265_BRUPA        Unreviewed;       310 AA.
AC   A0A0N4T265;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   10-APR-2019, entry version 18.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=BPAG_LOCUS2255 {ECO:0000313|EMBL:VDN83441.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000228501-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000228501-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:BPAG_0000228501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDN83441.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UZAD01000294; VDN83441.1; -; Genomic_DNA.
DR   WBParaSite; BPAG_0000228501-mRNA-1; BPAG_0000228501-mRNA-1; BPAG_0000228501.
DR   Proteomes; UP000038020; Genome Assembly.
DR   Proteomes; UP000278627; 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:UP000038020,
KW   ECO:0000313|Proteomes:UP000278627};
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:UP000038020}.
FT   DOMAIN      123    128       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   310 AA;  35210 MW;  DB39D0EBEDEB7927 CRC64;
     MSFDVDNLID RLLSVGLSGG VALTKCVPEQ EISALLLVSL LGTARQIFLS QPPLIEIEPP
     VKVCGDLHGQ YADLLRLYNR CGFPPDANYI FLGDYVDRGK QSLETICLQF CYKTKYPENF
     FLLRGNHECA AINRAYGFYD ECNRRYSIRL WQMFQDVFNC LPFCGLIAGK IFCMHGGLSP
     KLNNWDQLLH IERPIDPPNP SIHIDLLWAD PDKWVRGWQQ NTRGVSYVFG ADVVNAFCQD
     MNIDLVARAH QVVQDGYEFF ANRKLVTIFS APHYCGEFDN AAAIMTVDDQ LLCSFDVLRS
     TSNPIRVSQF
//
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