ID A0A0V1N599_9BILA Unreviewed; 933 AA.
AC A0A0V1N599;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:KRZ78910.1};
GN ORFNames=T10_5261 {ECO:0000313|EMBL:KRZ78910.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ78910.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ78910.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ78910.1};
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:KRZ78910.1}.
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DR EMBL; JYDO01000009; KRZ78910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1N599; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000054843; 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:UP000054843};
KW Transferase {ECO:0000313|EMBL:KRZ78910.1};
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..422
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 442..560
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 650..862
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 659
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 755
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 875..879
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 860..870
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ78910.1"
SQ SEQUENCE 933 AA; 109147 MW; 17178263CD2FC227 CRC64;
LSEQNSMIRR RNWQVLCYLL FARTLKYCIV RRQVWFLFFA VLITCYFGYQ WHGRFGVAYS
PVTLPFYDCP ANALFDQPPM SGGIFSASRE QLNSKCDSKI LLLVENQYSA LGQQIKTVLN
YLKVPYKVQA VRKTLPSLTN LARGRYMIII FENFYRYINM NHWNRQLLDK YCKEFGASIV
AFMANKSDQD EFDPVKLLGF PLYVQKQRRF ANASLSDISQ LLYIAKRGSH FPGPVGNSSN
WVGFRPNHST YKPVMFARDV SNANDVQSLV LLDNGEFDGI RRLLFGNDLN SFWPLKLLFL
DGLRFLFFGK VELPLVRYLQ IDIDDIFVGQ ENGKITKADV EELLRSQERM RKHVTNFIYN
LGFCGRFYGR GNDLDRSGDE MLIEKAANFR WFPHQWRHAK AHQLNITVFS SQMLQNLQFA
KVCFLLNLIV VFFVGLLWSA RAAQLHWFPH SWAHMQAHWK VNQHDIPVQW SYAVSPHHSG
VYPVHDPLYD AWKSIWKIKV TSTEQYPHLK PASLRRGFVY KDIMVMPRQT CGLYTHTIFI
EQFPGGKERL DESIFGGELF YTFVFNPFLI FMTHQANYAK DRLAVYTFEN VVRFIRCWTN
LKLETISTLE MAEKYFQMYP QEVNPIWGNP CSDQRHVELL SSKNLCKQFP DALIVGPQKT
GSTALYTFLK LHPLVNSSLS HPKTFEEVQF FCGRNYLHGI NAYSEYFPPR QEKTLLFEKS
ATYFDCDLAP LRVHSLLPHA KIIIIAISPI KRAYSWFQHM KAHDDPTALK NDFIDVLQSK
ENGPPEMWKF RQRCLTPGHY AHHIEHWLAH FPAKQIHIVD GEALQQRPAV VMTHLLDFLE
LPDMDYNEKL VYNTKKGFFC IREEFNRTRC LGKSKGRSYS PPSEDVHRYL INYYKTHNIA
FHRLLLRLGY ETPTWLQQEL QEINVTFHAL LGS
//
