GenomeNet

Database: UniProt
Entry: J3S121_CROAD
LinkDB: J3S121_CROAD
Original site: J3S121_CROAD 
ID   J3S121_CROAD            Unreviewed;       296 AA.
AC   J3S121;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
OS   Crotalus adamanteus (Eastern diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8729 {ECO:0000313|EMBL:AFJ51549.1};
RN   [1] {ECO:0000313|EMBL:AFJ51549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Venom gland {ECO:0000313|EMBL:AFJ51549.1};
RX   PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA   Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT   "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT   (Crotalus adamanteus).";
RL   BMC Genomics 13:312-312(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 3,3',5'-triiodo-L-thyronine =
CC         3,3',5'-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC         H(+); Xref=Rhea:RHEA:67888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57261,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176513;
CC         Evidence={ECO:0000256|ARBA:ARBA00024561};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889;
CC         Evidence={ECO:0000256|ARBA:ARBA00024561};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 3,3',5-triiodo-L-thyronine =
CC         3,3',5-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC         H(+); Xref=Rhea:RHEA:67876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:176511, ChEBI:CHEBI:533015;
CC         Evidence={ECO:0000256|ARBA:ARBA00024579};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC         Evidence={ECO:0000256|ARBA:ARBA00024579};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 3,3'-diiodo-L-thyronine = 3,3'-
CC         diiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:67892, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:176514, ChEBI:CHEBI:176515;
CC         Evidence={ECO:0000256|ARBA:ARBA00024508};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC         Evidence={ECO:0000256|ARBA:ARBA00024508};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC         bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00024527};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC         Evidence={ECO:0000256|ARBA:ARBA00024527};
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC       {ECO:0000256|ARBA:ARBA00005771, ECO:0000256|RuleBase:RU361155}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JU176025; AFJ51549.1; -; mRNA.
DR   AlphaFoldDB; J3S121; -.
DR   GO; GO:0004062; F:aryl sulfotransferase activity; IEA:UniProt.
DR   GO; GO:0051923; P:sulfation; IEA:UniProt.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR11783:SF14; SULFOTRANSFERASE 1B1; 1.
DR   PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361155}.
FT   DOMAIN          37..288
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
SQ   SEQUENCE   296 AA;  34661 MW;  CF2F7CE027BC6D08 CRC64;
     MATEDYLRQD CQMVHGIPMV YAFSFDWDRI ENFQSRPDDI VIATYPKSGT TWLSEIVDMI
     LNNGDPDKCK RDAIFNKVPM LEFVVPGKMP AGTEQLTHMS SPRVVKTHLP VSLLPKSFWD
     KGCKMIYMAR NAKDVAVSFY HFDLMNKLHP DPGSWGDYLE KFMTGRTMIF GSWYDHVKNW
     WNKRNDHSIL YLFYEDMKED PKHEIKKLIH FLGKNFDESV VDKIVYHTSF DMMKDNPMTN
     YRMAPAAVMD HSISPFMRKG IAGDWKNHFT VAQNEAFDEN YKKTMADTTL QFRTEI
//
DBGET integrated database retrieval system