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Database: UniProt
Entry: A0A016SV64_9BILA
LinkDB: A0A016SV64_9BILA
Original site: A0A016SV64_9BILA 
ID   A0A016SV64_9BILA        Unreviewed;       874 AA.
AC   A0A016SV64;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-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};
GN   Name=Acey_s0172.g378 {ECO:0000313|EMBL:EYB94410.1};
GN   Synonyms=Acey-hst-1 {ECO:0000313|EMBL:EYB94410.1};
GN   ORFNames=Y032_0172g378 {ECO:0000313|EMBL:EYB94410.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB94410.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYB94410.1}.
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DR   EMBL; JARK01001508; EYB94410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SV64; -.
DR   STRING; 53326.A0A016SV64; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..516
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          609..815
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        617
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         710
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         827..831
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        813..822
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   874 AA;  101244 MW;  1799F8563E55F78E CRC64;
     MIYTSLISSF SECVWYVIWL VPGEAADFIM LPYCSRRLLK SFKFVIALTM LISVTLIYKV
     SFRPDIAVKR YPPQRLPHYE CPCNTSSVSN RVSPYANQNL TEHRALILLE SAYSRHGRLL
     QQILTASKYP FKAETFSKNL PLLTTATRGR YAIIIIENYY KYLNMAKWNR QLLDKYCVEY
     NVPLISFLST RPNTTYQKVK IKGSKLHFWQ NQEVLSLKVA ESDIHRISRI GNERTDVNTH
     EWILFEESPA FSTVIFARDA FGRPRAAVIH DKGEEDNVKR ILFGHNVTDW TIKMTFLDTL
     WYTTGGRVGW SLDRYVQIDV DDIFVGARGT RMVESDVRAL LESQKNLRQY ISNFTYMLGF
     SGSYFRNGDD NEDKGDELLV ELAENFVWFP HMWRHNHAHE HNLTYMEATM TQNLMFAQNM
     RLPVKYPYAI APQHDGVYPV HSELYKAWKK IWKVEVTATE EYPHFKPATD RKGFIHMNIS
     VLPRQTCGLY THTQFFHNYP GGFSKLTSLV YGGELFFTIL MNPVSIFMTH QQNFAHDRLA
     LYTFENLVRF IQCWTNIRLL WQSPVESAKM YFSLMPQERL PVWSNPCNDP RHKAILPPSL
     NCSNLTLSNT LIVGPQKTGS TALATFLSLH PNVSTNAPIP DSFEELQFFG GANYHNGIEW
     YTRQFTRAHV VYDKSATYFD NANAARDAFA LVPDAKIVVI LYDPARRAYS WYQHILAHND
     SVAVAAGSMD VILNAETPQL RKIKQRCISG GRYTHHLDRW LEHYPMSNLI LIDGERLREE
     PAIVMTELTE KLGLPYFDYS KAVRYSSSKR FFCQVIDGKT KCLGRGKGRV YPPMPPELWA
     RLNNIFLQDN TALHKFLVKN HLPVPRWLRA LLEG
//
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