ID Q95097_PARTE Unreviewed; 320 AA.
AC Q95097;
DT 01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=GSPATT00016140001 {ECO:0000313|EMBL:CAK81298.1},
GN GSPATT00034294001 {ECO:0000313|EMBL:CAK64817.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:AAA19173.1};
RN [1] {ECO:0000313|EMBL:AAA19173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=51S {ECO:0000313|EMBL:AAA19173.1}, and Wildtype 51 S
RC {ECO:0000313|EMBL:CAA47831.1};
RX PubMed=1327778; DOI=10.1111/j.1432-1033.1992.tb17259.x;
RA Friderich G., Klumpp S., Russell C.B., Hinrichsen R.D., Kellner R.,
RA Schultz J.E.;
RT "Purification, characterization and structure of protein phosphatase 1 from
RT the cilia of Paramecium tetraurelia.";
RL Eur. J. Biochem. 209:43-49(1992).
RN [2] {ECO:0000313|EMBL:AAA19173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=51S {ECO:0000313|EMBL:AAA19173.1};
RA Schultz J.E., Russell C.B., Pohner J., Hinrichsen R.D., Klumpp S.;
RT "Protein phosphatases in the protozoan Paramecium.";
RL Adv. Protein Phosphatases 7:315-333(1993).
RN [3] {ECO:0000313|EMBL:AAA19173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=51S {ECO:0000313|EMBL:AAA19173.1};
RX PubMed=8165136; DOI=10.1093/nar/22.7.1221;
RA Russell C.B., Fraga D., Hinrichsen R.D.;
RT "Extremely short 20-33 nucleotide introns are the standard length in
RT Paramecium tetraurelia.";
RL Nucleic Acids Res. 22:1221-1225(1994).
RN [4] {ECO:0000313|EMBL:CAK64817.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK64817.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [5] {ECO:0000313|EMBL:CAK64817.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK64817.1};
RG Genoscope;
RL Submitted (MAR-2006) 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; L26481; AAA19173.1; -; Genomic_DNA.
DR EMBL; X67492; CAA47831.1; -; mRNA.
DR EMBL; CT868034; CAK64817.1; -; Genomic_DNA.
DR EMBL; CT868396; CAK81298.1; -; Genomic_DNA.
DR PIR; S29310; S29310.
DR RefSeq; XP_001432214.1; XM_001432177.1.
DR RefSeq; XP_001448695.1; XM_001448658.1.
DR AlphaFoldDB; Q95097; -.
DR STRING; 5888.Q95097; -.
DR EnsemblProtists; CAK64817; CAK64817; GSPATT00034294001.
DR EnsemblProtists; CAK81298; CAK81298; GSPATT00016140001.
DR GeneID; 5017999; -.
DR GeneID; 5034480; -.
DR KEGG; ptm:GSPATT00016140001; -.
DR KEGG; ptm:GSPATT00034294001; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; Q95097; -.
DR OMA; YLVMESR; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR CDD; cd07414; MPP_PP1_PPKL; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF385; SERINE_THREONINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|RuleBase:RU004273, ECO:0000313|EMBL:AAA19173.1};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 123..128
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 320 AA; 36393 MW; C21AF3CCD800A308 CRC64;
MSKDNKGEID VDSIIERLLS VRGSKPGKNV NLTEAEVRGL CIKARDIFIS QPILLELEAP
LKICGDVHGQ YFDLLRLFEY GGYPPESNYL FLGDYVDRGK QSLETICLLL AYKIKYPENF
FLLRGNHECA SINRIYGFYD ECKRRYTIKL WKTFTDCFNC LPVAALIDEK ILCMHGGLSP
ELSNLEQIRR IMRPTDVPDT GLLCDLLWSD PDKDVQGWAD NERGVSYVFS QEIVQVFLKK
HELDLICRAH QVVEDGYEFF SKRQLVTLFS APNYCGEFDN AGSMMTVDES LMCSFQILKP
AEQGQGASQQ NKAGSAKFVN
//
