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Database: UniProt
Entry: C3YFU1_BRAFL
LinkDB: C3YFU1_BRAFL
Original site: C3YFU1_BRAFL 
ID   C3YFU1_BRAFL            Unreviewed;       510 AA.
AC   C3YFU1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN   ORFNames=BRAFLDRAFT_80288 {ECO:0000313|EMBL:EEN60746.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN60746.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60746.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN60746.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005093}.
CC   -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004841}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC       {ECO:0000256|ARBA:ARBA00010420}.
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DR   EMBL; GG666510; EEN60746.1; -; Genomic_DNA.
DR   RefSeq; XP_002604736.1; XM_002604690.1.
DR   AlphaFoldDB; C3YFU1; -.
DR   STRING; 7739.C3YFU1; -.
DR   eggNOG; KOG3703; Eukaryota.
DR   InParanoid; C3YFU1; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR   GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR   GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR021930; Heparan_SO4_deacetylase.
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; PF12062; HSNSD; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU361155}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..510
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002933696"
FT   DOMAIN          43..222
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          312..492
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        321
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         419
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
SQ   SEQUENCE   510 AA;  59482 MW;  36E22F8E361AF1A1 CRC64;
     MAPVLSELVH WLVCLANECL KIWSRAGGQE AIFATFGYMD CDNALISAQS RLGSLVPGFR
     FNLGFSGYFY HSGDDIEDIG DDALLANAHE FWWFPHMWAH TQPHTFTNET SLREQMILNK
     RFAKEHGIPT DGGYAVAPHH SGVYPVHVPL YEAWRKVWGI KVTSTEEYPH LRPPRHRRGF
     IYKNIVVLPR QTCGLFTHTI FIDKYPGGRS RLEESIHGGE LFQTFINSRV NIFMTHLSNY
     GNDRLALYTF ESVIKFVQCW TNLQLKTVPP MELGRKYFDL YPEEANPVWQ NPCDDKRHLA
     IWSKYKTCDR LPRFLVIGPQ KTGTTALYAF LSMHPNILSN FPSSKTFEEV QFFNGANYYR
     GIDWYMEFFP TPSNSSLQYL FEKSATYFDN ELVPKRAHAL LPRAKIVTIL INPARRAYSW
     YQLLILDGDQ LRTDPVSTMW KTQKFLKVKP HFDYDSHLRY ILEIHLLILD GDQLRTDPVS
     TMWKTQKFLK VKPHFDYDSH LRYILEIHVC
//
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