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
//