ID A0A0V0XT61_TRIPS Unreviewed; 917 AA.
AC A0A0V0XT61;
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};
DE Flags: Fragment;
GN Name=sfl {ECO:0000313|EMBL:KRX91131.1};
GN ORFNames=T4E_7547 {ECO:0000313|EMBL:KRX91131.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX91131.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX91131.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX91131.1};
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:KRX91131.1}.
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DR EMBL; JYDU01000145; KRX91130.1; -; Genomic_DNA.
DR EMBL; JYDU01000145; KRX91131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XT61; -.
DR STRING; 6337.A0A0V0XT61; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000054815; 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:UP000054815};
KW Transferase {ECO:0000313|EMBL:KRX91131.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..421
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 421..553
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 643..854
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 652
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 748
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 868..872
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 853..863
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX91131.1"
SQ SEQUENCE 917 AA; 107320 MW; 475D3BAF844F89E1 CRC64;
LSEQNSMIRR RNWQVLCYLL FARTLKYCIV RRQVWFLFVA VLITCYFGYQ WHGRFGVAYS
PVTLPFYDCP ANALFDQPPM SGAMFAASRE QLNSKCDSKI LLLVENQYSA LGQQIKTVLN
YLKVPYKVQA VRKTLPSLTN LARGRYMIII FENFNRYINM NHWNRQLLDK YCKEFGASIV
AFMTSKSDQD EFDPVKLLGF PLYVQKQRRF ANASLSDISQ LLYIAKRGSH FPGPVGNGSN
WVGFRPNHST YKPVMFARDV LNANDVQSLV LLDNGEFDGI RRLLFGNDLN SFWPLKLLFL
DGLRFLSFGK IELPLVRYLQ IDIDDIFVGQ ENGKITKADV EELLKSQERM KKHVTNFVYN
LGFCGRFYGR GNDLDRSGDE MLIEKAANFR WFPHQWRHAK AHQLNSTVFS SQMLQNLQFA
KLHWFPHSWA HMQAHWKVNV TELLEDMNHN EGFAEQHDIP VQWSYAVSPH HSGVYPVHDP
LYDAWKSIWK IKVTSTEQYP HLKPASLRRG FVYKDIMVMP RQTCGLYTHT IFIEQFPGGK
ERLDESIFGG ELFYTFVFNP FLIFMTHQAN YAKDRLAVYT FENAVRFIRC WTNLKLETIS
TLEMAEKYFQ MYPQEVNPIW GNPCSDQRHL ELLNTKNLCK QFPDALIVGP QKTGSTALYT
FLKLHPLVNS SLPHPKTFEE VQFFCGRNYL HGINAYSEYF PPRQEKTLLF EKSATYFDCD
LAPLRVYNLL PHAKIIIIAI SPIKRAYSWF QHMKAHDDPT ALKNDFIDVL QSKENGPPEM
WKFRQRCLTP GHYAHHIEHW LAHFPAKQIH IVDGEALQQR PAVVMSHLLD FLELPDMNYN
EKLVYNTKKG FFCIREEFNR TRCLGKSKGR SYSPPSEDVR RYLINYYKTH NIAFHRLLLR
LGYETPTWLQ KELQEST
//
