ID   A0A0K0F9S9_STRVS        Unreviewed;       883 AA.
AC   A0A0K0F9S9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE            EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
OS   Strongyloides venezuelensis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0558100.1};
RN   [1] {ECO:0000313|Proteomes:UP000035680}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A, De Silva N.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SVE_0558100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
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   AlphaFoldDB; A0A0K0F9S9; -.
DR   STRING; 75913.A0A0K0F9S9; -.
DR   WBParaSite; SVE_0558100.1; SVE_0558100.1; SVE_0558100.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000035680; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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   Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          117..521
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          613..859
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        622
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         721
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         837..841
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        823..832
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   883 AA;  103181 MW;  C1CA8947563649EC CRC64;
     MQSNGAILLN CMHILNSPSK YLPRKKLFGV FNKISIVPFI ICFLITFWIG NSYLKVFWEI
     EDVRVVRYKA FQPPDFSCPI QCEDNLSPEV NVYQNVSTKT EEGILILSAN PSKLCTSSSG
     KKILQQLDAF RIMYKVISLK EPVINLNFGD IGLYSIILIE DFYEYLKSSS NLRGNINGYC
     KKYKVGMLFM VPNVDPGNTF LENNEFMLKN IQPRQYAGNF FINTTSAIPF ITKKCLKLEI
     IQPSTNSWTF FNTSPYFSSI LSVNSTDYLS VVIKDDGLYD DVEKVFFGGS IDYWVIQLLF
     HDTILYFEPR LKIKFSRERY LQIDVDDIFV GQQGTRIVAE DVDYLIKSQQ ILRKSISNFS
     YTLGFSGYFF RKGNILEKKG DEYLIEKKDN FLWFPHMWRH NHAQDHDEPY LKAVMTQNRL
     FAENFKLPLV KGYAVSPQHI GVYPILDYLY DAWKEIWDIT ITSTEEYPHF KPMGARRGFK
     YNNISILPRQ TCGLYTHTLY YHAYPGGYQT FLDNIFGGNL FFSILLNPYN VFMTHQQNYA
     HDRLAEYTFR NIVNFFKCYT NINFKWVETD LLRNKYFETF PEEQKIIWTN PCDDTRHIKM
     LSPKHNCIDI SLPNLLIIGP QKTGTTALAS FLKLHPDVGA NDILEDSFEE VQFFSSDYKY
     EKGIYWYSSF FRNARNQTKK IIFDKTANYF DHPTAPLTTS SLLGNPFVVI VLKDPVFRAY
     SWYQHMRFHD DPVANKYTFE EVMLSNNTDT VKLKSRCFTP GRYAYHLLKW LRYYPPSKII
     TIDADSLLGE PSKTLSLLVK RIGLPEFNFT SVIKYNDNKG FHCAVIEGHS RCLGRSKGRK
     YSQLSEETIK KIDELYKEEN KILYNILHTN KFSIPVWLKK KLL
//