ID   A0A0V1L9P6_9BILA        Unreviewed;      1105 AA.
AC   A0A0V1L9P6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 {ECO:0000313|EMBL:KRZ55954.1};
GN   Name=Hs3st3b1 {ECO:0000313|EMBL:KRZ55954.1};
GN   ORFNames=T02_8342 {ECO:0000313|EMBL:KRZ55954.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ55954.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ55954.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ55954.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SYF2 family.
CC       {ECO:0000256|ARBA:ARBA00010028}.
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:KRZ55954.1}.
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DR   EMBL; JYDW01000104; KRZ55954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1L9P6; -.
DR   STRING; 6335.A0A0V1L9P6; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR013260; mRNA_splic_SYF2.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10605:SF73; HEPARAN SULFATE 3-O SULFOTRANSFERASE-B, ISOFORM A; 1.
DR   PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   Pfam; PF08231; SYF2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT   DOMAIN          857..1038
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   REGION          490..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          408..461
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          563..590
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        493..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        866
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         866..870
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         947
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         955
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         1069..1073
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        1053..1064
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   1105 AA;  129000 MW;  0067EC5227BDBED7 CRC64;
     MILKLFTSAG IIIFNYMQRY LLINTCKSYL LYCFDCYVFL RLVSVFSHFR IWILNLYHYF
     KILKDYISIS ELYLIMDRLQ KFKELKMRNN EARKLNHREV VEEDRRNKLP ANYEAKRKRA
     EWEISEFEKR KEAEERGEDY DRLKLLQMPA DIAWKLQQNP KALKKQRNKE FKRVDFCTAA
     IRNYERLSEQ IKPDFQEYNG MKELLAEDFY PDSNTLIQNA HYPSDSKIDR LIEDLNMQKA
     RREKARRRKE FDPDAPIDYI NERNKQYNMK LDRYYDHSYV KMARAAVSPY IRRNSRLRPL
     TSCIQRRNHK GGNLSMEGFE EEVLQLKKKI QYLNEDNMLL KIKLNKYDVE LKKKVLIKSR
     AVRLFSDDID KIFIAFHDNI MEKEIKDLLS SQKHSFMSIA QGERGILLNS LKQRVIRLEH
     LLREKDELIR KLKCDIRSTR LNEAAIEIDT LYGEINRLKA MCGLKSKSVY STGECSSYDT
     LSNVASWTSE ISGSRHEQRE KYHGEKKRTA QASMSEEENN TDGNFQKESS SSSVDNDDVE
     AEKVDCSDDC TRNKLEKATS FNAVEDVSEL ENLKERMKHL EDSLADRETR LVEITNMLTD
     CQEQLTIQQK FASNKVDKCS SEQPITEGEN RFLKTEKSEG PENDSITSQA VEVAECENSS
     SEFNNGKSDR ELKMASRLIV NVVKAHLFRL KQIEALKSSN FELSKQFQSG SVDQNFNENG
     EAERKQAVGP SIINTNQQAE DESESGDDDD DHIVVVESEK SNELYNFDID SDADIIMVPD
     SPEKSNACWQ CNGAAGFIIV SHMWHVVKAI EVKNNNLLSK KAFWTKYSDN FKQEKLKNIL
     NKQLEDVKQN LLLKRLPDAI IIGVKKAGTR ATLEYLRLHD QIKAPGPEIH FFDRNYKYGL
     DWYREQMPPA APEDVIIEKT PRYFISPEAP TKIRSMNQKM KLIVVFRDPV TRLLSEYAQI
     ASKRPGLPSF EQMAFLDANR TRVNRSWGAV HTGLYEKHLR HWLKLFPKSQ ILFISGEQLI
     TNPVNVTANM EQFLNLPKKI TDQHFAFGGK FPCLKKLPLS EPHCLGKTKG RLHPVVSEKD
     LQTLRRFYKP YNDVLYKLIG QSFDW
//