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Database: UniProt
Entry: A0A0V0RJI6_9BILA
LinkDB: A0A0V0RJI6_9BILA
Original site: A0A0V0RJI6_9BILA 
ID   A0A0V0RJI6_9BILA        Unreviewed;       306 AA.
AC   A0A0V0RJI6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=Ppx1 {ECO:0000313|EMBL:KRX14389.1};
GN   ORFNames=T07_8835 {ECO:0000313|EMBL:KRX14389.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14389.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX14389.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX14389.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|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. PP-6 (PP-V)
CC       subfamily. {ECO:0000256|ARBA:ARBA00038400}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX14389.1}.
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DR   EMBL; JYDL01000161; KRX14389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0RJI6; -.
DR   STRING; 6336.A0A0V0RJI6; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF10; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 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};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT   DOMAIN          113..118
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   306 AA;  34875 MW;  A105724A68237A4B CRC64;
     MVICDKYNPE ELVEAAKSGK YFSEAVVRTL FNRVREIFIN EPNVLRVSSP IVVCGDIHGQ
     FFDLKSLFNC YGEVPTNRYL FLGDYVDRGR NSLEVLLWLF SLKVRFPEHI FLLRGNHECR
     TITQTYGFYD ECLSKYGHSG IWNFCCEVFD SIPLAAVIDD RVLCVHGGLS PKIHTISEIH
     SINRVREIPL TGPFADLLWS DPEEEIGSFQ LNSSRGAGVL FGRTAVETFL QENQLQLICR
     SHQLCLEGYK YLWDQKLLTI WSAPNYTYSC KNKAAVVRFI PDGTCAFSVF EAADNPHVQA
     EALYTV
//
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