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Database: UniProt
Entry: A0A085NE66_9BILA
LinkDB: A0A085NE66_9BILA
Original site: A0A085NE66_9BILA 
ID   A0A085NE66_9BILA        Unreviewed;       334 AA.
AC   A0A085NE66;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=M514_07502 {ECO:0000313|EMBL:KFD67762.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD67762.1};
RN   [1] {ECO:0000313|EMBL:KFD67762.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD67762.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
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; KL367511; KFD67762.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085NE66; -.
DR   Proteomes; UP000030758; 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; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE-RELATED; 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}.
FT   DOMAIN          140..145
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          314..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  37997 MW;  2A2DFBEFA447D784 CRC64;
     MAAMETALQD FRSPADGTHS NRIPQEKIEE FTQMIDQLIK VRVAGDSPLT ESFVLELLDY
     AEASLLDDCT LIDLKPPIIV CGDIHGDYAT LLRIFSTQGW PPTRRYLFLG DYVDRGILSL
     EVITLLLLFK TLYPKDFYIL RGNHEAMSVN RIYGFKREVS TLRFTKVLWY RFQSTFNCLP
     LAALIENKIF CVHGGISFRL VSLQQIRVLK RPINLPNDGF LLDLLWADPS QEGRGFEPNE
     MRNASFTFSE STLRQWLDCM GLQMLVRAHE VVPEGFEVSW DGKLITVFSC PNYTSGNKAA
     VMSISRQLQV SFTKYQGKKP ARGRATGRPR GGHK
//
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