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Database: UniProt
Entry: A0A096P7L4_OSTTA
LinkDB: A0A096P7L4_OSTTA
Original site: A0A096P7L4_OSTTA 
ID   A0A096P7L4_OSTTA        Unreviewed;       821 AA.
AC   A0A096P7L4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=OT_ostta03g00790 {ECO:0000313|EMBL:CEF96999.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF96999.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(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}.
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:CEF96999.1}.
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DR   EMBL; CAID01000003; CEF96999.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A096P7L4; -.
DR   STRING; 70448.A0A096P7L4; -.
DR   InParanoid; A0A096P7L4; -.
DR   OrthoDB; 298319at2759; -.
DR   Proteomes; UP000009170; Chromosome 3.
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; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR23081:SF0; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1; 1.
DR   PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT   DOMAIN          227..494
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..765
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  91323 MW;  6BDEE7C1744CE196 CRC64;
     MNRERVPTRR ARPLERETRR RVRARAREML DRDGTVDLRL RVAGREAQRE LWVTCEPFET
     SDETSRRNDD DSVENDDDDD DDDGRGASGR EGTRHASMLR ELGRGEDGVT IVGFWETRGT
     PDPLAALHFL SRRSAGAPAF RCSPKSGLND DLKKAIEDLH EEMVRENKSA VMPPTSGGRM
     GELHLVAVPD AETVAAGDGD RGARNPKTMF VAFQTDEMAP AYAQGLLKHN RLVVVLDLDE
     TLVQATTLHA LDRRIETARS KMLSLMKFDF NNPRLTTVMI DEVKKEKQAC ETALRRSQLD
     RQMLMQFVTE GAVTVNNRRS VTIPEIEPLS NGMQRLRNVI RIPSPHTKGA MLAFTLIDPS
     SPATAMLVHI RPGWGELRSY LSGSDRGSKR AETFVCTMAN IDYAREMCRL LDPHGTVFDP
     AQLDKRIKSV KPDELKSLSD TCGLHFPSEL AVIVDDRTAV WEPSAQSHIL AVTPFMPYGT
     DVEFGTGIEQ NEASGSGGVL GKVQSMLETV RLRWHMDYGK FAAKARMHVH DTASFGAIRA
     RKVGEGEDQP TSTGTSVDTL RAEHNRKKSE RLFYPPNTGD LLQPLMEIEA KDAALNIAER
     GGATRAAAGS GSRLAAALGV LSRPKNNAKS QQKVCEQEVE ELKVDIKSEP EDMFPASLFR
     EQRKSAPEEV KPMHSTMDDT PTAKAPAKQA KSSPQKPLSG TKHGRDTDVS DSNSGTEPES
     ESEPEVVEDE EEEEEEEEEE EYEEEYEEEE EEEEEEEEEV DGDKNDDDEQ PRSKEPSGKN
     IARSKQVKPA IAKKPAAKKT ARPTKVFRVG SRASNRLSQS Q
//
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