ID D7FLE7_ECTSI Unreviewed; 831 AA.
AC D7FLE7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBJ29715.1};
GN ORFNames=Esi_0159_0051 {ECO:0000313|EMBL:CBJ29715.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ29715.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ29715.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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DR EMBL; FN648136; CBJ29715.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FLE7; -.
DR STRING; 2880.D7FLE7; -.
DR EnsemblProtists; CBJ29715; CBJ29715; Esi_0159_0051.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; D7FLE7; -.
DR OrthoDB; 51109at2759; -.
DR Proteomes; UP000002630; Unplaced LGUn.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14498; DSP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR46377; DUAL SPECIFICITY PROTEIN PHOSPHATASE 19; 1.
DR PANTHER; PTHR46377:SF1; DUAL SPECIFICITY PROTEIN PHOSPHATASE 19; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 19..158
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 79..137
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 189..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 85192 MW; E3625A18B42E03A8 CRC64;
MTKRANPPPL SRSLVQDNVP AKVTDRLWIG SIHAAFNQDS MQDRGITHVL NASGLPATFP
RQFTYFTVDI RDKESSNILT AIGAVNIFVE AGIEKGGVLV HCAGGRSRSA AFVVAFIMST
QGCSYDAAYA QVRRARPVAS VNRGFEQQLR AYGAAQCDVF AAHQMMLRIR AAALLDRRNL
LLLRRSSGVT PSETVGDGAA GGEAAEHTRT SPTRPSAQHQ LGATGAAAAA GSVSTAGIPP
TPRSPRGRGR SPAGINPPNI DLPSLQAVLA RSSPRNQADQ YAPDAGASPL SLVTSNSTAT
ITSSMAASQQ QSPPCSGSAS ASGGSSSCSG GTDTVVTRGR GDRRSPSPLS ERRGQSRVAV
ATTTTVSVSS GSPTTRRSAA ARRPPPPLRV ITTELGPDRP PMHNRWVPEG FLAGVQATTA
GAGPPLQGAT VTVGGGGAGG GGGTAVAEAI RLQSPLGFTP SPSRLRPWAA GRCSSGTATG
GGGGGGCAGD SRCGDGQRNS PVFAFESEDD SSNVDPFERE GEGTLAEAYP VAVDAIYTAS
GSGGSGVISV GSGGGGMSYP GWEGAVGSGG GSAGCRRLRR ATGTPTNATL QSGEFNLMLS
SKVPLSAGSG MESVSPLMTP RSPRTPASCG STSPCASDGS FSNSLSRPQS AEKRQFLMRM
NQMESRTLAT TGPPSFPDTE SQNERPTSRP GGRWLHVDLL DWMGDIMVAP TGHICCPSSG
CGVELGNWSW EKPEAAGLKS PTGPPLIRLD KALIKNTSYM RSQLDSSRSS LSRDNTPKSS
PCASANSPSK GSPGSALPES DLRRSSGILE SRLAGLSASP QLTQPARGSP G
//
