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Database: UniProt
Entry: Q5CYW0_CRYPI
LinkDB: Q5CYW0_CRYPI
Original site: Q5CYW0_CRYPI 
ID   Q5CYW0_CRYPI            Unreviewed;       322 AA.
AC   Q5CYW0;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
DE   Flags: Fragment;
GN   ORFNames=cgd7_810 {ECO:0000313|EMBL:EAK90676.1};
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK90676.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK90676.1, ECO:0000313|Proteomes:UP000006726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
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|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}.
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:EAK90676.1}.
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DR   EMBL; AAEE01000001; EAK90676.1; -; Genomic_DNA.
DR   RefSeq; XP_628270.1; XM_628268.1.
DR   AlphaFoldDB; Q5CYW0; -.
DR   STRING; 353152.Q5CYW0; -.
DR   EnsemblProtists; EAK90676; EAK90676; cgd7_810.
DR   GeneID; 3371773; -.
DR   KEGG; cpv:cgd7_810; -.
DR   InParanoid; Q5CYW0; -.
DR   OMA; YRCENQA; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000006726; Chromosome 7.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
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:SF12; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A; 1.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006726}.
FT   DOMAIN          125..130
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EAK90676.1"
SQ   SEQUENCE   322 AA;  37245 MW;  9EDB5818F32F5149 CRC64;
     ERQLFSRMPK GLDVYLDSLK LDREISTLLE CKTLSENEVK QLCELAKDIL EEEQNVQQIG
     LPLTVVGDIH GQFFDLKEIF RIGGVPPETN FLFLGDYVDR GYYSVESVTL IVALKVRYRN
     RVFLIRGNHE SRQITQVYGF YDECLRKYGT PNVWRYFTDL FDYLPLSALI DNKIFCPHAG
     LSPSLPSLDS IKSLDRIQEV PHEGPMCDLL WSDPDERYGW GVSHRGAGYT FGEDVSEMFN
     HTNNLQLICR AHQLILDGYQ WSHNKNVVTV FSAPNYCYRC ENQAAILRID DLGNFTFLQF
     DHAPEKVLPR QENQLPVPDY FV
//
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