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Database: UniProt
Entry: L7JUA1_TRAHO
LinkDB: L7JUA1_TRAHO
Original site: L7JUA1_TRAHO 
ID   L7JUA1_TRAHO            Unreviewed;       323 AA.
AC   L7JUA1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=THOM_2041 {ECO:0000313|EMBL:ELQ74999.1};
OS   Trachipleistophora hominis (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC   Trachipleistophora.
OX   NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ74999.1, ECO:0000313|Proteomes:UP000011185};
RN   [1] {ECO:0000313|EMBL:ELQ74999.1, ECO:0000313|Proteomes:UP000011185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA   Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA   Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA   Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA   Embley T.M.;
RT   "The genome of the obligate intracellular parasite Trachipleistophora
RT   hominis: new insights into microsporidian genome dynamics and reductive
RT   evolution.";
RL   PLoS Pathog. 8:E1002979-E1002979(2012).
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, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
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         ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273}.
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DR   EMBL; JH993998; ELQ74999.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7JUA1; -.
DR   STRING; 72359.L7JUA1; -.
DR   VEuPathDB; MicrosporidiaDB:THOM_2041; -.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   InParanoid; L7JUA1; -.
DR   OMA; EEHEIRY; -.
DR   Proteomes; UP000011185; Unassembled WGS sequence.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
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   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004273, ECO:0000313|EMBL:ELQ74999.1};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011185}.
FT   DOMAIN          120..125
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   323 AA;  36423 MW;  0C90C80F720678F8 CRC64;
     MEYNEVSVDK IISKLLSVKN SRLGKNVHLS ESEILFLCEK TKEIHLSQPM LLHIKAPIKI
     CGDIHGQYRD LLKLFDFGGF PPDNNYLFLG DYVDRGKQSL ETICLLFAYK IKYPQNIFLL
     RGNHECASIN KIYGFFDECK RRHSIRIWKN FTDSFNCLPI SAIVGERILC MHGGISPELK
     NLDQIRKIKR PTDVPDDGLL CDILWGDPEP SISGWGENDR GVSVTFGADV VKEFLDSNDL
     DLICRAHQVV EEGYEFFADR RLVTVFSAPN YCGEFDNAGA IMNVDEDLTC SFQILKPTDK
     LSPVSDGFIG MADSVSNSTT SDS
//
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