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
//