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Database: UniProt
Entry: D8LJQ2_ECTSI
LinkDB: D8LJQ2_ECTSI
Original site: D8LJQ2_ECTSI 
ID   D8LJQ2_ECTSI            Unreviewed;       547 AA.
AC   D8LJQ2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Sulfotransferase {ECO:0000313|EMBL:CBN77079.1};
DE            EC=2.8.2.- {ECO:0000313|EMBL:CBN77079.1};
GN   ORFNames=Esi_0026_0167 {ECO:0000313|EMBL:CBN77079.1};
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:CBN77079.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBN77079.1, 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).
CC   -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC       family. {ECO:0000256|ARBA:ARBA00007730}.
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DR   EMBL; FN648442; CBN77079.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8LJQ2; -.
DR   EnsemblProtists; CBN77079; CBN77079; Esi_0026_0167.
DR   eggNOG; ENOG502QU6N; Eukaryota.
DR   InParanoid; D8LJQ2; -.
DR   OMA; FEQINIP; -.
DR   OrthoDB; 89741at2759; -.
DR   Proteomes; UP000002630; Chromosome LG12.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR   InterPro; IPR027443; IPNS-like_sf.
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; PF05118; Asp_Arg_Hydrox; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Transferase {ECO:0000313|EMBL:CBN77079.1}.
FT   DOMAIN          138..229
FT                   /note="Aspartyl/asparaginy/proline hydroxylase"
FT                   /evidence="ECO:0000259|Pfam:PF05118"
FT   DOMAIN          265..480
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   REGION          498..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        274
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         370
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         378
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
SQ   SEQUENCE   547 AA;  61918 MW;  B604C6F929D34A10 CRC64;
     MMAAMVSAAP RNVGGEILVP PSGQVKLKDK TTPVIEQVAK EQLDPEARPL VFTRGRADLS
     LLKLLLSSRG ASIWTDEEHD RTNVKMTRPA HDKWGISKIV LVFCDDFLKR VYTFPWYHEP
     EWKEALQPVL DVLGIPEEKM VRCLLASMPP GCVIPVHHDT GHWVQHTHRV HVAVVTDVSE
     VDFLVGPDPK HMRKVMFDEG RVVEFNNQAK HAVTNRWSRN RVHLILDYVD EYPLDFVRLA
     PGSKLVQTRR SIDVEGLVTR QGPDPAFVVL GGQKCGTTLL YECLNQHPLV ARGRRRETHF
     FDWAWPAKGE SLTVDQLRES YMAFFYAEEL KSHPSIVTGE STPSYLLRGD LVIPRLKNVA
     GKTRLLVMLR DPVKRAYSHY HMAVDPEGTP AQLRSRGGGG WTSKTFEQVV EEERAVLEKA
     GVGPATSPGD FARDYLSTRP NGYGGHSLLG RGLYALQLQP WLEAFGRDQI KVLFLEEVVK
     SEDSLQEAMD GVFEHVGLPP SPVEDKAPKN HRDYPPMDEG VRRRLRDFYA PYDAALRQLL
     RRDSLPW
//
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