ID U6KTF4_EIMTE Unreviewed; 797 AA.
AC U6KTF4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=ETH_00010250 {ECO:0000313|EMBL:CDJ40208.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ40208.1};
RN [1] {ECO:0000313|EMBL:CDJ40208.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ40208.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ40208.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ40208.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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.
CC {ECO:0000256|ARBA:ARBA00008294, ECO:0000256|RuleBase:RU004273}.
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DR EMBL; HG674990; CDJ40208.1; -; Genomic_DNA.
DR RefSeq; XP_013230961.1; XM_013375507.1.
DR AlphaFoldDB; U6KTF4; -.
DR EnsemblProtists; CDJ40208; CDJ40208; ETH_00010250.
DR GeneID; 25251245; -.
DR VEuPathDB; ToxoDB:ETH2_1529200; -.
DR VEuPathDB; ToxoDB:ETH_00010250; -.
DR OMA; HRETCAA; -.
DR OrthoDB; 46665at2759; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 44..87
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 624..659
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 716..751
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 584..611
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 89156 MW; 01A1AE336F868D43 CRC64;
MTFKVGDKVA VYGYPATVKF VGTFPPPRGP GGAPGGPPGG PPGGPHGQLS GPVVGVEFLK
RGPGDCDGSY HSRRYFHCAP GKGRFVRAFS VKPFSEETCA ATRIQTSFRR YRAAETFQEL
AAFRFWNELD HFEEKDALVN NRRVLFCCSS AAAAQKQRSS SSAAESCKSL DVGTPTLNTI
KKQIHDEDFL DVGEVPTERP RASSSTLQVP GAAAAAATPG GRMARRRSST RQRQSIDANT
IAEEGLPPGY KGPHLRWPIT REFALDLIDH FRDHSDVPLP RKYALELVMA VEEHYKQTMK
GAVAEVEIPK KPGGRLVLVG DTHGQLNDVL WILYKFGPPS ATNVYLFNGD IADRGRSSVE
IFLLLFAFKL QCASSVIINR GNHESADMNE VYGFAQEVRQ KYGGLLYQKF QDIFHLLPLC
VVLEKRVFIV HGGLCRKDNI TLHHIDKLHR QRPCPASPHT FEDTLMFDLL WSDPQPDRGR
GWSTRGADCI AFGPDVTDAF LTKNNLEVCI RSHQVPTNLR GFEPVHDGRC VTLFSASNYC
GTTGNYGGVI IFEANLSFEI QEYMAPSLQE IQQLHRETCA ATQKVLLQKK MKELETQAKR
ANRRSAAARM SQEIVQKMCK MVCEKKQDLW WCFFNMDSDG SGKITPAQWR EACSIVLGQE
LPWVNIMKCL KAVSKDGLVH YNDFLYRYKV DFRPPICKHL NWRQECVARV FESIMSADLS
LKETLMLFDR NCDGTVSFRE FNELLSDLDI GLSEPQVRIL MRLITASPAF NAAAGSIDVA
EFLGRFKVVY SNSIKEE
//
