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Database: UniProt
Entry: D8LLL8_ECTSI
LinkDB: D8LLL8_ECTSI
Original site: D8LLL8_ECTSI 
ID   D8LLL8_ECTSI            Unreviewed;       485 AA.
AC   D8LLL8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Sulfotransferase {ECO:0000313|EMBL:CBN74649.1};
DE            EC=2.8.2.- {ECO:0000313|EMBL:CBN74649.1};
GN   ORFNames=Esi_0037_0054 {ECO:0000313|EMBL:CBN74649.1};
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:CBN74649.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBN74649.1, 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; FN648564; CBN74649.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8LLL8; -.
DR   SMR; D8LLL8; -.
DR   EnsemblProtists; CBN74649; CBN74649; Esi_0037_0054.
DR   eggNOG; KOG3704; Eukaryota.
DR   InParanoid; D8LLL8; -.
DR   OrthoDB; 37019at2759; -.
DR   Proteomes; UP000002630; Unplaced LGUn.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10605:SF56; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:CBN74649.1}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..485
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003117264"
FT   DOMAIN          173..420
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   REGION          22..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         286
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         294
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
SQ   SEQUENCE   485 AA;  52453 MW;  A56AD70C3B1906E2 CRC64;
     MVAAVVSLVL ALAFLPIILT GPSDPATPMP PMPATPPDDL DSGGGVADPG REKPAPPAAS
     ASGVARRVEL AAAAVAGRGS SSSSSSSASY SDNHESRQGF DGQQSWRREQ EEGGGGGWAG
     GGDSGVPEDL SAGRAAGGGA TGVVAEGEGG KLRDGRNRCF VGAEGDHRCY PTVFFFGTSK
     CGTTSLARWL DHHPATHWVA NPRRPHQIEE TGVKEAHVFD DPPKGDPAFE EGMHHEKLFI
     TTPKSGAEDV VIDYTPHYIA VAETPHRIAD IYGGRESGLK FIVTLREPAG RAISSWEFKN
     EYNPKKGRRE ESRSLAKTIE DGGRRAMKLH ACLALAKSKA VSPRDRDLKL CNPRKFLEVP
     LYVSHVGKSM YALQLERWFD LFGRENFKVV FTDDMAVDPV GVLEDVLHFL GLELTSEDES
     KGLPDMKGWK KITGMAYNKT KSKKKDELGD QVTDEVKEGL RKFFEPHNEA LEEILGQPLP
     EAWGS
//
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