ID A0A0V1L0L5_9BILA Unreviewed; 914 AA.
AC A0A0V1L0L5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:KRZ52770.1};
GN ORFNames=T02_10988 {ECO:0000313|EMBL:KRZ52770.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ52770.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ52770.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ52770.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ52770.1}.
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DR EMBL; JYDW01000183; KRZ52770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L0L5; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000054721; 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:UP000054721};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..417
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 417..549
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 639..851
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 648
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 744
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 864..868
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 849..859
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 914 AA; 107129 MW; D984407768967999 CRC64;
MNRRRSNWRL LCYLLFARTL KYCTVRRQVW FLFFAALITC YFGYQWHGRF DVAYSPVTLP
FYNCPANALV DHTLMSGGVF SVPREQFNSK CDSKILLLVE NQYSALGQQI KTVLNYLKVP
YKVQAVRKTL PSLTNLARGR YMIIIFENFY RYINMNHWNR QLLDKYCKEF GASIVAFMPN
KSDDQDEFDP VKLLGFPLYV QKQRRFANAS LSDISQLLYI AKRGSHFPGP VGNNSNWVGF
KPNHSTYKPV MFARDVSNAN DVQSLVLLDN GEFDGIRRLL FGNDLNSFWP LKLLFLDGLR
FLSFGKVQLP LVRYLQIDID DIFVGQENGK ITKADVEELL RSQERMKKYV ANFVYNLGFC
GRFYGRGNDL DRSGDEMLIE KAADFRWFPH QWRHAKAHQL NSTVFLSQML QNLQFAELHW
FPHSWGHMQA HWKTNVTELL EDMNYNEGFA KQHDIPVQWS YAVSPHHSGV YPVHDPLYDA
WKSIWKIRVT STEQYPHLKP ASLRRGFVYK DIMVMPRQTC GLYTHTIFIE QFPGGKERLD
ESIFGGELFY TFVFNPFLIF MTHQANYAKD RLAVYTFENA VRFIRCWTNL KLQTIATLEM
AEKYFQMYPH EVNPVWGNPC SDQRHAELLS TKNLCKQFPD AIIVGPQKTG STALYTFLKL
HPLVNSSLSH PKTFEEVQFF CGRNYLHGIN AYSEYFPPRQ EKTLLFEKSA TYFDCDLAPL
RVHSLLPRAK IIMIVISPIK RAYSWFQHMK AHNDPTALKN DFIDVLQSKE NGPPEMWKFR
QRCLTPGHYA HHIEHWLAHF PAKQIHIVDG EALQQRPAVV MTHLLDFLEL PDMDYNEKLV
YNTKKGFFCI REEFNRTRCL GKSKGRSYSP PSEDVRRYLI NYYKTHNIAF HRLLLRLGYE
APTWLQQELQ ESST
//
