ID U6GRR8_EIMAC Unreviewed; 319 AA.
AC U6GRR8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=EAH_00060250 {ECO:0000313|EMBL:CDI81289.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI81289.1};
RN [1] {ECO:0000313|EMBL:CDI81289.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI81289.1};
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:CDI81289.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI81289.1};
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 -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; HG671583; CDI81289.1; -; Genomic_DNA.
DR RefSeq; XP_013248946.1; XM_013393492.1.
DR AlphaFoldDB; U6GRR8; -.
DR EnsemblProtists; CDI81289; CDI81289; EAH_00060250.
DR GeneID; 25274095; -.
DR VEuPathDB; ToxoDB:EAH_00060250; -.
DR OMA; CAFLQAN; -.
DR OrthoDB; 1488111at2759; -.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-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 144..149
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDI81289.1"
SQ SEQUENCE 319 AA; 36388 MW; D6EB218C160637C2 CRC64;
MEPLPDPKHD RVVSSVQPPP AKPLALNVLY PQGQDSPPDW KELRSHLQRE GRVFKEDCLE
IIRKVNDITS NEPNLLRLSD PITVVGDIHG QYYDLLKLLD VGGDPDTTQY LFLGDYVDRG
SFSVEVLLLL FALKLNYPSR VWLLRGNHEC RQMTSFFNFR DECESKYDMA VYYAFMELSQ
IGGINRFQEP PRGGLFCDLL WADPLDEARE DAEAQLAQST DGGQDNARKH RAGTPISRER
AEALRRKVQS VGRLMRVFKT IREENELIVQ LKGCTPGDRI PVGLLIQGRQ GLKNELEKFQ
NAKQIDAMNE RRPDGAPKR
//
