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Database: UniProt
Entry: A0A0V0WDI8_9BILA
LinkDB: A0A0V0WDI8_9BILA
Original site: A0A0V0WDI8_9BILA 
ID   A0A0V0WDI8_9BILA        Unreviewed;       915 AA.
AC   A0A0V0WDI8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE            EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN   Name=sfl {ECO:0000313|EMBL:KRX73760.1};
GN   ORFNames=T06_7907 {ECO:0000313|EMBL:KRX73760.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73760.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX73760.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX73760.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX73760.1}.
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DR   EMBL; JYDK01000165; KRX73759.1; -; Genomic_DNA.
DR   EMBL; JYDK01000165; KRX73760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WDI8; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000054673; 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; 2.
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:UP000054673};
KW   Transferase {ECO:0000313|EMBL:KRX73760.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          93..418
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          418..550
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          640..852
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        649
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         745
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         865..869
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        850..860
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   915 AA;  107240 MW;  B48A11F5EA1E1F42 CRC64;
     MNRRRRSNWR LLCYLLFART LKYCTVRRQV WFLFFAALIT CYFGYQWHGR FDVAYSPVTL
     PFYNCPANAL VDQTLMSGGV FSVPREQFNS KCDSKILLLV ENQYSALGQQ IKTVLNYLKV
     PYKVQAVRKT LPSLTNLARG RYMIIIFENF YRYINMNHWN RQLLDKYCKE FGASIVAFMP
     NKSDDQDEFD PVKLLGFPLY VQKQRRFANA SLSDISQLLY IAKRGSHFPG PVGNSSNWVG
     FKPNHSTYKP VMFARDVSNA NDVQSLVLLD NGEFDGIRRL LFGNDLNSFW PLKLLFLDGL
     RFLSFGKVQL PLVRYLQIDI DDIFVGQENG KITKADVEEL LRSQERMKKY VANFVYNLGF
     CGRFYGRGND LDRSGDEMLI EKAADFRWFP HQWRHAKAHQ LNSTVFLSQM LQNLQFAELH
     WFPHSWGHMQ AHWKTNVTEL LEDMNYNEGF AKQHDIPVQW SYAVSPHHSG VYPVHDPLYD
     AWKSIWKIRV TSTEQYPHLK PASLRRGFVY KDIMVMPRQT CGLYTHTIFI EQFPGGKERL
     DESIFGGELF YTFVFNPFLI FMTHQANYAK DRLAVYTFEN AVRFIRCWTN LKLQTIATLE
     MAEKYFQMYP QEVNPVWGNP CSDQRHAELL STKNLCKQFP DAIIVGPQKT GSTALYTFLK
     LHPLVNSSLS HPKTFEEVQF FCGRNYLHGI NAYSEYFPPR QEKTLLFEKS ATYFDCDLAP
     LRVHSLLPRA KIIMIVISPI KRAYSWFQHM KAHNDPTALK NDFIDVLQSK ENGPPEMWKF
     RQRCLTPGHY AHHIEHWLAH FPAKQIHIVD GEALQQRPAV VMTHLLDFLE LPDMDYNEKL
     VYNTKKGFFC IREEFNRTRC LGKSKGRSYS PPSEDVRRYL INYYKTHNIA FHRLLLRLGY
     EAPTWLQQEL QESST
//
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