TYW3_DANRE
ID TYW3_DANRE Reviewed; 251 AA.
AC Q6DHJ1; A5PN41;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=tRNA wybutosine-synthesizing protein 3 homolog;
DE Short=tRNA-yW-synthesizing protein 3;
DE EC=2.1.1.282;
DE AltName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase;
GN Name=tyw3; ORFNames=si:ch211-215b16.3, zgc:92277;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC that acts as a component of the wybutosine biosynthesis pathway.
CC Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC tRNA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000305}.
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; BX927315; CAN88068.1; -; Genomic_DNA.
DR EMBL; BC075981; AAH75981.1; -; mRNA.
DR RefSeq; NP_001002611.1; NM_001002611.1.
DR AlphaFoldDB; Q6DHJ1; -.
DR SMR; Q6DHJ1; -.
DR STRING; 7955.ENSDARP00000055736; -.
DR PaxDb; Q6DHJ1; -.
DR PRIDE; Q6DHJ1; -.
DR Ensembl; ENSDART00000055737; ENSDARP00000055736; ENSDARG00000038222.
DR GeneID; 436884; -.
DR KEGG; dre:436884; -.
DR CTD; 127253; -.
DR ZFIN; ZDB-GENE-040718-355; tyw3.
DR eggNOG; KOG1228; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_047426_1_1_1; -.
DR InParanoid; Q6DHJ1; -.
DR OMA; GKWHHYA; -.
DR OrthoDB; 1313208at2759; -.
DR PhylomeDB; Q6DHJ1; -.
DR TreeFam; TF329327; -.
DR UniPathway; UPA00375; -.
DR PRO; PR:Q6DHJ1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000038222; Expressed in somite and 27 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 3.30.1960.10; -; 1.
DR InterPro; IPR003827; tRNA_yW-synthesising.
DR InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR Pfam; PF02676; TYW3; 1.
DR SUPFAM; SSF111278; SSF111278; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..251
FT /note="tRNA wybutosine-synthesizing protein 3 homolog"
FT /id="PRO_0000281846"
FT REGION 213..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 28798 MW; C16C9F504732752E CRC64;
MDGDSFQQWK NQCLNKCDFS KKGSVDEDIS HVVSFINSQD RYFTTSSCSG RIILFDAVSD
CPDVQKQNCS WLFVTHQKCQ MEDVVRGLEK SVGDATFKFE PFVLHVQCKQ LEDAQLLHTV
AINSGFRNSG ITVGKKGKII MAVRSTHCLE VPLSHRSHVL VTHQYLDFLV GVANQKMEEN
LKRIQRFSEC LQAALQPQEE KCSFKEADNK TVYRRRRKRT QDVSVTDSSQ NTQEHHENTE
EEIDCDLLFL L
