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Database: UniProt
Entry: G4VC21_SCHMA
LinkDB: G4VC21_SCHMA
Original site: G4VC21_SCHMA 
ID   G4VC21_SCHMA            Unreviewed;       378 AA.
AC   G4VC21;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_148510.2};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_148510.2}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_148510.2};
RG   WormBaseParasite;
RL   Submitted (NOV-2019) 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, 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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DR   RefSeq; XP_018650069.1; XM_018795792.1.
DR   AlphaFoldDB; G4VC21; -.
DR   STRING; 6183.G4VC21; -.
DR   EnsemblMetazoa; Smp_148510.2; Smp_148510.2; Smp_148510.
DR   GeneID; 8341847; -.
DR   KEGG; smm:Smp_148510; -.
DR   WBParaSite; Smp_148510.2; Smp_148510.2; Smp_148510.
DR   CTD; 8341847; -.
DR   eggNOG; KOG0697; Eukaryota.
DR   HOGENOM; CLU_013173_4_0_1; -.
DR   InParanoid; G4VC21; -.
DR   OMA; SICENMM; -.
DR   OrthoDB; 11028at2759; -.
DR   PhylomeDB; G4VC21; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   ExpressionAtlas; G4VC21; baseline.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992:SF233; ALPHABET, ISOFORM E; 1.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008854}.
FT   DOMAIN          23..293
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   378 AA;  41775 MW;  EEF0A74E01F6E0DD CRC64;
     MGGLLSSPKT DKYNETGCGN GLRYGISSMQ GWRLSMEDSH CAITQLPGNL KDWSFFAVFD
     GHAGALVSEL CATELLKCIV DTEEFKKINP DLAPSLQEVE RGIRDGFLSL DDRLRHLPQL
     ASGEDRSGST AVCVLITPKH IFFANCGDSR AILIRKGKVA FATVDHKPVN PNEKQRIQNA
     GGSVIIQRVN GSLAVSRSLG DYAFKAAKDL GPTEQLISPE PEITVVDRDK DLDEIIVLAC
     DGIWDVLTNE EICSLLQNRM RCVDDLSMIC NETIDMCLYK GSSDNMSMVL VAFDPAPRVD
     PTCKTEDENL ESVLLQRTKE FLEKHSKTEV TTEMVVEDLQ TSVGSLSSSE NWLCKIGKIQ
     ELIDSHRLAY SNRGIQNR
//
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