TYW4_CANGA
ID TYW4_CANGA Reviewed; 674 AA.
AC Q6FXA5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=tRNA wybutosine-synthesizing protein 4;
DE Short=tRNA-yW synthesizing protein 4;
DE EC=2.1.1.290;
DE EC=2.3.1.231;
DE AltName: Full=Leucine carboxyl methyltransferase 2;
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase;
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase;
GN Name=PPM2; Synonyms=TYW4; OrderedLocusNames=CAGL0B01485g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. May methylate the carboxyl group of leucine residues to form
CC alpha-leucine ester residues (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-
CC adenosyl-L-methionine = 7-[(3S)-(3-amino-3-
CC methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-
CC COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543,
CC ChEBI:CHEBI:74275; EC=2.1.1.290;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in
CC tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-
CC homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119,
CC Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231;
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
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DR EMBL; CR380948; CAG57934.1; -; Genomic_DNA.
DR RefSeq; XP_445034.1; XM_445034.1.
DR AlphaFoldDB; Q6FXA5; -.
DR SMR; Q6FXA5; -.
DR STRING; 5478.XP_445034.1; -.
DR EnsemblFungi; CAG57934; CAG57934; CAGL0B01485g.
DR GeneID; 2886671; -.
DR KEGG; cgr:CAGL0B01485g; -.
DR CGD; CAL0127682; CAGL0B01485g.
DR VEuPathDB; FungiDB:CAGL0B01485g; -.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_002761_0_0_1; -.
DR InParanoid; Q6FXA5; -.
DR OMA; WEVDFPD; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000002428; Chromosome B.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0031591; P:wybutosine biosynthetic process; IEA:EnsemblFungi.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF04072; LCM; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..674
FT /note="tRNA wybutosine-synthesizing protein 4"
FT /id="PRO_0000226140"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 184..185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 674 AA; 76295 MW; D00A86FA06C5369A CRC64;
MSTQIKREKP IKKQFQKKKF ADLAVQGTNN SSIASKRSVE LTYLPKLGVG SNAEKLQPGK
PYFRYFVPKK IKRSPCINRG YWLRLHAVRS HIESILDSCQ ENITIINLGC GYDPLPFEML
DPQNPQYSRY SNRLNFIDID YPDLLNIKSG VIKETPELLS IIGGIDPTET NMIISERYKT
IPCDLYDMPA FEALLKSENL GHPNTIKIFI AEVSLAYMKH EKADDIIASC SKFPNSHFIM
LEQIIPVGEY EPFSGRMLKH FSKNESPLQT VTKYQTIESQ IERFRRYNFT NVNAGDMFQL
WNSLSSNVHS KIENIEPFDE LEEFHLFCHH YMICHATNNE QFKFNESIKF REPEVLPSLP
ISGLRIDSID KIGFSKRFGS SVISKDSIIY TGGASPYRSD EADVINLEEC TIETLSNMKL
PDARVCHSYD SLMDGKLDIL IGGRKAPHQP FNDVFIFEKQ TASWEKVATL DYPIYRHATS
SLSNDKLLLF GGNFCLKEPF LTITVKSETQ IVVRSINCPD SIKSSIGAAM CYNEASNDVI
ILGGSSNGTE VSDKLIIMSY DDKSETLTVK KEVTNDLFKR YGSKIIHLTD DEYLVVGGTS
PDRLFDASNS IITYNSRSDE IKSVRIPDHI WQGDELMLVG FELQKLNGKI IIFGGGATCY
GFGSVNNSIY SIEK
