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Database: UniProt
Entry: Q20240_CAEEL
LinkDB: Q20240_CAEEL
Original site: Q20240_CAEEL 
ID   Q20240_CAEEL            Unreviewed;       460 AA.
AC   Q20240;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 2 homolog {ECO:0000256|ARBA:ARBA00017179};
DE            EC=2.5.1.114 {ECO:0000256|ARBA:ARBA00012265};
DE   AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|ARBA:ARBA00031315};
GN   ORFNames=CELE_F40F9.10 {ECO:0000313|EMBL:CAA94765.2}, F40F9.10
GN   {ECO:0000313|EMBL:CAA94765.2, ECO:0000313|WormBase:F40F9.10};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA94765.2, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAA94765.2, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA94765.2,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC       component of the wybutosine biosynthesis pathway. Wybutosine is a hyper
CC       modified guanosine with a tricyclic base found at the 3'-position
CC       adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes
CC       the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC       adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14)
CC       to produce wybutosine-86. {ECO:0000256|ARBA:ARBA00037786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC         4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC         H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC         COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC         ChEBI:CHEBI:73550; EC=2.5.1.114;
CC         Evidence={ECO:0000256|ARBA:ARBA00036405};
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DR   EMBL; BX284605; CAA94765.2; -; Genomic_DNA.
DR   RefSeq; NP_505502.2; NM_073101.4.
DR   AlphaFoldDB; Q20240; -.
DR   SMR; Q20240; -.
DR   STRING; 6239.F40F9.10.1; -.
DR   EPD; Q20240; -.
DR   PaxDb; 6239-F40F9-10; -.
DR   EnsemblMetazoa; F40F9.10.1; F40F9.10.1; WBGene00009586.
DR   GeneID; 179363; -.
DR   KEGG; cel:CELE_F40F9.10; -.
DR   UCSC; F40F9.10; c. elegans.
DR   AGR; WB:WBGene00009586; -.
DR   WormBase; F40F9.10; CE42760; WBGene00009586; -.
DR   eggNOG; KOG1227; Eukaryota.
DR   GeneTree; ENSGT00940000153304; -.
DR   HOGENOM; CLU_022610_1_0_1; -.
DR   InParanoid; Q20240; -.
DR   OMA; ELLCCQQ; -.
DR   OrthoDB; 122704at2759; -.
DR   PhylomeDB; Q20240; -.
DR   PRO; PR:Q20240; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00009586; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0031591; P:wybutosine biosynthetic process; IBA:GO_Central.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:Q20240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          51..307
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
FT   REGION          260..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  52532 MW;  78DBCCFA0594BAC3 CRC64;
     MERTSSLRRK TSDGVLAKAS NFGQMLEDVR KLALSKSLWD DEMQRDLPKK WEKHGDMIVF
     PQNTFTHINW RYIGRELWAV VAQSLNVARV GRKRLIDEER TPHVDLLLGA DAWVDYVDER
     GIKFCYDATK RVFENSKKAE MKRISKWSCQ GQTIVDMYAS LGYYTLTFLV SCEAKQVVAI
     DWNDEILESL IRSAQVNNVD DRLLVIHGDC RRVCPDQTAD RVYLGLLPSC RAHWLAACKA
     LKPEGGIVHI NEILDMTEKK KTPQKTEKVE KKVVAEKKKK PADGKEKTDK DAAPKKKKVL
     RQKTLPVLSA VHEDSKPEVE STSIPTAPES DEPSENNSET NGTEGGQKKK KFSRSASIVE
     EMENRVLPEV KIWKEYENEG WARLTDRHRE FAKDCADSCT RFLNNIHLSD LMYSVTVVNM
     IRYGEVSKGK EHIVLELLCC QQDASAEHLI SKFTSENLKS
//
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