ID A0A3B4YSY0_SERLL Unreviewed; 305 AA.
AC A0A3B4YSY0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN Name=HS3ST1 {ECO:0000313|Ensembl:ENSSLDP00000031423.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000031423.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000031423.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC {ECO:0000256|RuleBase:RU361155}.
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DR AlphaFoldDB; A0A3B4YSY0; -.
DR STRING; 1841481.ENSSLDP00000031423; -.
DR Ensembl; ENSSLDT00000032319.1; ENSSLDP00000031423.1; ENSSLDG00000024142.1.
DR GeneTree; ENSGT00940000160449; -.
DR OrthoDB; 10019at2759; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605:SF16; HEPARAN SULFATE GLUCOSAMINE 3-O-SULFOTRANSFERASE 1; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU361155}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..305
FT /note="Sulfotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017401674"
FT DOMAIN 53..291
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT REGION 19..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 62
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 62..66
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 145
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 153
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 253
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 268..272
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 254..263
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 305 AA; 35250 MW; EE2BC5F37A203189 CRC64;
MAALLLGLLL FAIQSPPVPS RPMADGGPPS PPTSSPTDNG TTSHPNGTLQ QLPQIIIIGV
RKGGTRALIE MLSLHSAVAA AQNEVHFFDW ESHFQKGFPW YLSQMPYAYP DQLTVEKTPA
YFTSSKVPKR IHQMNPDIKL LLILRDPTER VLSDYTQVFY NRLQKHKRYQ PIESILVKDG
EINLGYKALN RSLYYVHMQN WLQYFPLESI HVVDGDELIR DPFPEMKKVE RFLKLEPQIN
ASNFYFNKTK GFYCLRDHGR ERCLHDSKGR AHPHVAPAIL QKLYQFFHEP NKKFFELVGR
TFNWK
//
