ID Q5CW69_CRYPI Unreviewed; 752 AA.
AC Q5CW69;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=cgd8_1430 {ECO:0000313|EMBL:EAK89357.1};
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:EAK89357.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK89357.1, 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|RuleBase:RU366020};
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:RU366020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU366020}.
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:EAK89357.1}.
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DR EMBL; AAEE01000003; EAK89357.1; -; Genomic_DNA.
DR RefSeq; XP_627050.1; XM_627050.1.
DR AlphaFoldDB; Q5CW69; -.
DR STRING; 353152.Q5CW69; -.
DR EnsemblProtists; EAK89357; EAK89357; cgd8_1430.
DR GeneID; 3374581; -.
DR KEGG; cpv:cgd8_1430; -.
DR VEuPathDB; CryptoDB:cgd8_1430; -.
DR InParanoid; Q5CW69; -.
DR OMA; NNCINAM; -.
DR OrthoDB; 276880at2759; -.
DR Proteomes; UP000006726; Chromosome 8.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366020};
KW Magnesium {ECO:0000256|RuleBase:RU366020};
KW Manganese {ECO:0000256|RuleBase:RU366020};
KW Metal-binding {ECO:0000256|RuleBase:RU366020};
KW Protein phosphatase {ECO:0000256|RuleBase:RU366020};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726}.
FT DOMAIN 412..729
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 752 AA; 86965 MW; 8EC67E8CDD22C766 CRC64;
MLMNGYERRV FVESKECEAG IRFLKRLSKE LERQNGNNKN NKEGIILAMA GILERNRQRL
IRETRDQLLN LKTRIICEDE IEEIQRKDIE KSRKKMNVEE GNRKIKKSIL KEEKKKEIKE
GINKSKLVFG ELDEEKNRED RFIIKIENGR NETGSWEDPI PSNNGVPYDH FERRIYDKYV
DYWRNSKLSV PFSTWISGEK MDRKRSSSIM SFELIEENSS ISCKSIQEAI YRIRRFEQDF
QAIPKEIIFP LIEKGILINN SKNTLDNFSG NTWKDNNYNH LEFNRAKIKN QDIIEKNQLN
LQSSFKVPQS LFFSMVISDH ENMIHSKLSK TGIITNEQIK GNDKKMTNLV INNNDSLLEK
DNINKKQCNC DFYKLRQKFI EEYNLYELIG SNSNLEKLDQ SMESNLRLWM GAYYLPRNDK
RARGGEDGWF LSEDLQSMGV ADGVGEWEDL SGKSARVFSN SIMKNSLQYI KSNRDRSLEK
PSILAKDSLK VGLDHCEKSG VHGASTALVA CFDHYSGNIG FANMGDSGAL VLRRLQFDTG
KLEIVRRVKE MQHEFNCPYQ FANLPPEHEW DELIEKGFHD IVRLAKIEKK NKEDSNIMDD
KYSMQLACDD PELSQLLEVP LKEGDMVILG TDGLFDNLFD FEITSISGLS FSPIESKLFY
NCLDYTTTPM VIAKSIALSA YYKSLDPFSK TPFANQAKRF YSGGKNSLFE SQSFSGGKED
DISVLVAWVV HKDDFETLTK NSPHYCDISK KL
//
