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
//