GenomeNet

Database: UniProt
Entry: G1NQY4_MELGA
LinkDB: G1NQY4_MELGA
Original site: G1NQY4_MELGA 
ID   G1NQY4_MELGA            Unreviewed;       351 AA.
AC   G1NQY4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000016275.2, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000016275.2, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000016275.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC       {ECO:0000256|RuleBase:RU361155}.
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DR   RefSeq; XP_019473247.1; XM_019617702.1.
DR   RefSeq; XP_019473248.1; XM_019617703.1.
DR   AlphaFoldDB; G1NQY4; -.
DR   Ensembl; ENSMGAT00000017249.2; ENSMGAP00000016275.2; ENSMGAG00000015334.2.
DR   GeneTree; ENSGT00940000164759; -.
DR   HOGENOM; CLU_017703_0_0_1; -.
DR   InParanoid; G1NQY4; -.
DR   OrthoDB; 10019at2759; -.
DR   TreeFam; TF350755; -.
DR   Proteomes; UP000001645; Chromosome 8.
DR   Bgee; ENSMGAG00000015334; Expressed in ovary and 4 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR10605:SF18; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   Transferase {ECO:0000256|RuleBase:RU361155};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          99..337
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        108
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         108..112
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         191
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         199
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         299
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         314..318
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        300..309
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   351 AA;  40757 MW;  1EF2A300B4EE36A3 CRC64;
     MINASENCCL FTAGSANQLK KGPIYSFINQ TQYYLELIIL LHMAFLLVSA YFLLTHTQGA
     PVENGALLET LKSQVGLFSN KSEHYSAQVR PPGTSRRIPQ TIIIGVRKGG TRALLEMLDI
     HPNIVVAATE VHFFDWDENY VKGIDWYRSL MPFSYGNQIT IEKTPGYFTS PQAPERIHDM
     NSSIKLLLIL RDPTERVISD YTQVYYNRVE SHKPVQLFED IVIKNGALNT KYKAIQRSLY
     DVHMEKWLKH FSLDQIHIVD GNTLIKDPLP ELQKVERFLN LPSRIMSSNF YFNQTKGFYC
     IRSDGRERCL HESKGRPHPL VNNTVLEQLY SYFREHNAKF YRMVNHSFDW H
//
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