ID A0A090LEU1_STRRB Unreviewed; 1262 AA.
AC A0A090LEU1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN ORFNames=SRAE_2000291500 {ECO:0000313|EMBL:CEF68257.1,
GN ECO:0000313|WBParaSite:SRAE_2000291500.1,
GN ECO:0000313|WormBase:SRAE_2000291500};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF68257.1};
RN [1] {ECO:0000313|EMBL:CEF68257.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000291500.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF68257.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000291500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004841}.
CC -!- SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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DR EMBL; LN609529; CEF68257.1; -; Genomic_DNA.
DR STRING; 34506.A0A090LEU1; -.
DR EnsemblMetazoa; SRAE_2000291500.1; SRAE_2000291500.1; WBGene00263134.
DR WBParaSite; SRAE_2000291500.1; SRAE_2000291500.1; WBGene00263134.
DR WormBase; SRAE_2000291500; SRP03281; WBGene00263134; -.
DR eggNOG; KOG3703; Eukaryota.
DR OrthoDB; 2913264at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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 CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR021930; Heparan_SO4_deacetylase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF126; SEPTIN; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00735; Septin; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Transferase {ECO:0000313|EMBL:CEF68257.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 879..1142
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1230..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1154..1228
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1239..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 146938 MW; D04A8197E5B12327 CRC64;
MQSVGEGLLN YIRILSISSK FFPKKKIFGM CNRISIVSSI CFIIFFWFGS RYLKIFWEIE
DIKVIRYKAF QPSDFVCPNQ CTNDILLDVN TFQNVTLRTE EGILVLSANP SKLYVSSNGK
KILQQLNAFR ILYKVVSLKE PTINLNFGDT GLYSLILVED FYEYLKSSSN LRGSISGYCK
KYKVGMIFMV PNVDSKNVFL ENNEFMLKNI QPKQYVSNLF INTSSTIPFI TKRCLKIDSI
RPHIDSWTLF NSSVYFSSIL SVNLTESLSA VVKDNGFYDD IEKVFFGGSM NYWIIQLLFH
DTILYFEPRL KSRFSYKRYL QIDIDDIFVG QQGTRIVAED VDYLIKTQQN LRENIDNFTY
TLGYSGYFFR KGNILEEKGD EYLMEKKDNF LWFPHMWKHN HAQDHDEYYL KAVMTQNRLF
AENFKLPLVK GYAVSPQHIG VYPVLNHLYT AWKEIWNVTI TSTEEYPHFK PMGGRRGFRY
RNISILPRQT CGLYTHTLYY HAYPGGYQTF LDNIFGGNLF FSILLNPYNV FMTHQQNYAH
DRLAEYTFKN AINFFKCYTN IEFKWVESSI LEKMYFETFP EEQKIIWTNP CDDTRHIKLL
SSTKNCKDIP LPNLLIIGPQ KTGTTALANF LKLHPDVGTN DLLKDSFEEV QFFSNEYKYE
KSIYWYSDLF KNARNQSKKY IFEKTANYFD HPTAPVTTSS LLGNPFIVIV LKDPVLRAYS
WYQHMKSHND PVANKYTFEE VMLSNKNETI KLKSRCYTPG RYAFHLLKWL RYYSPSKIIT
IDADALLTDP STTLTRLGKR IGLSDFDFTS VIKYNENKGF HCPVIEGHPK CLGKSKGRKY
NQLMMANLKR SVSQHIPETN DYIGVVNYTN QVFRRAVKNG FEFTLMVVGE SGLGKSTFLN
TLFSTELEKY EGNVIPSTQK VVAKSFYLTE NKVKVKLTLV DTPGFGDSID NTNCWKPIVE
YIDSKYSQYL NEETKIERKN KIPDERVHLC LYFIAPTGHS LREIDIKFMK NLHDKVNIIP
LIAKADTLTL GEMNRFKENI LRDVEKNGIK IYQFEPSGGD EASQNYSRVP YGIVCSNHII
ETKTGRKVRV REYPWGVVEV DNLKHNDFVA MKEVLLKKHL IDLICDTANV HYENFRFNQL
SGPFKGGNVD CDPMSQMEAE NRMLEEQFEA TKKNMEKVYS EKVIDWELRL KERENKLASV
EKEQRQLLQS KREKLDQLTK EVQEIKISVG QNENASSKCS PGEKKKKSAT LGIFHRNTKH
EI
//
