ID A0E4V6_PARTE Unreviewed; 659 AA.
AC A0E4V6;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=GSPATT00023499001 {ECO:0000313|EMBL:CAK90323.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK90323.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK90323.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK90323.1,
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).
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|ARBA:ARBA00001482};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CT868659; CAK90323.1; -; Genomic_DNA.
DR RefSeq; XP_001457720.1; XM_001457683.1.
DR AlphaFoldDB; A0E4V6; -.
DR STRING; 5888.A0E4V6; -.
DR EnsemblProtists; CAK90323; CAK90323; GSPATT00023499001.
DR GeneID; 5043505; -.
DR KEGG; ptm:GSPATT00023499001; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_416504_0_0_1; -.
DR InParanoid; A0E4V6; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR CDD; cd00027; BRCT; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 243..445
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 532..619
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 659 AA; 76831 MW; FB0C8859AB187101 CRC64;
MRPKYQQTQN DTNSQVRINI KHVSPIQIEV LKQSGEKVEE NEKIGVYIFE NQNKSILASS
QGFIVWAQNQ KVFEIPVTEQ YFTIGIIYKN KGDIPNQEEL ENNTTSTSSL AQQNYVKLNF
AQLAIKNCQG NIQILKWKVN VGDYISPTMI LGICSDETQE DVIDLKSKIN GRVIELAKTK
IILPRNYALM VIDSSQTCNH LKIENNYCLI CNEKVIRNVE SLDLNYSDDI SKKISKEIVL
DILKKRKLIM VLDLDQTILH AIKVSTTFNK YEFCEKQNKM IQADSEAQFN GFQQLGFNIK
EHLLDMTCDQ QSKFIIKLRP YFEQFFLTLI PLFDIFIYTK ASKSYADFIL SFITHRLNEF
IPEHKPFFPP QRVLSREDTI CSNSKSLNRL FYPGIATNLL VILDDNAGMW NQFKENLIHT
KPFVYFNEHG STKDGQGIVT DIEKEVQIFN KNDFWLYTIT QKLKEISDKF WSQIKQAQDD
PNFIVEIEQQ VCKAKKVKTE IIEDTSLRLE ERNLLDIIIN RKISVPTIYL EMRRSILSGV
TLFFAISEAH EETIKRGLEQ AKDKAVILGA KVYREFKEDN FVGQENSYVI TVGRRKIRSI
MIAQEKNIPI IHYKWIEDCD NYLFRADYKL YVEREDGNNK SLTEEDQRDY VLKCQLLKI
//
