TYW4_RAT
ID TYW4_RAT Reviewed; 686 AA.
AC Q5XIA3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Lcmt2; Synonyms=Tyw4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(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 (By similarity). May methylate the carboxyl group of leucine
CC residues to form alpha-leucine ester residues. {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 -!- SUBUNIT: Interacts with RNF144B/IBRDC2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
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DR EMBL; BC083783; AAH83783.1; -; mRNA.
DR RefSeq; NP_001011956.1; NM_001011956.1.
DR AlphaFoldDB; Q5XIA3; -.
DR SMR; Q5XIA3; -.
DR STRING; 10116.ENSRNOP00000060993; -.
DR jPOST; Q5XIA3; -.
DR PaxDb; Q5XIA3; -.
DR PRIDE; Q5XIA3; -.
DR Ensembl; ENSRNOT00000068132; ENSRNOP00000060993; ENSRNOG00000043002.
DR GeneID; 296098; -.
DR KEGG; rno:296098; -.
DR UCSC; RGD:1305829; rat.
DR CTD; 9836; -.
DR RGD; 1305829; Lcmt2.
DR eggNOG; KOG2918; Eukaryota.
DR GeneTree; ENSGT00940000162599; -.
DR HOGENOM; CLU_002761_2_0_1; -.
DR InParanoid; Q5XIA3; -.
DR OMA; WEVDFPD; -.
DR OrthoDB; 1094856at2759; -.
DR PhylomeDB; Q5XIA3; -.
DR TreeFam; TF315087; -.
DR UniPathway; UPA00375; -.
DR PRO; PR:Q5XIA3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000043002; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5XIA3; RN.
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 Gene3D; 2.120.10.80; -; 2.
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; SSF117281; SSF117281; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..686
FT /note="tRNA wybutosine-synthesizing protein 4"
FT /id="PRO_0000204425"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 161..162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 686 AA; 75533 MW; 50443D777C3F9587 CRC64;
MGPRSRQRRT GTVQSTNDSS SLSKRSLAAQ GYVSDAFAPL LVPGIVRRTP LIHRGYYVRA
RAVRHCVRAF LDLTGAIRSP TRAQILSLGS GSDSLYFRLK AAGLLTRTAV WEVDFPDVSR
LKAKRIEETP ELCAQTGPFK IGDSASTLCF ESSDYRILGA DLRELQRLGE ALDSAGLDAT
SPTLILAEAV LTYLEPSRAA ALIAWVAQRF PNALFVIYEQ MKPGDAFGQI MLQHFRRLNS
PLHGLELFPD VEAQRQRFLQ AGWTTCSALD LNEFYRRLIP ADERRRVETL EPFDEFEEWH
LKCSHYFILA ASRGDILSET PVFLPSEASF QIDPALPSGF LSASVVTSDH QHSSLQRYGH
TSVLLSPGII FSAGGFGEQE GRHCRVSRFH LLSRSCDSEW KGCQISTLGT EGQWDGRLYH
TMTRLSDTRV LVLGGRLSPV NPASGALQLD IYKSEDNCPE GQNVVVTKAA LEEGSMLSCW
RHSTTEVYYQ NQRYLFVYGG RSVTDPVLSD CRFLHVETMA WVRIPVQGSS PEGRHSHSAC
SWQGGALIAG GLGASEEPLS SVFFLRPVSS GFLWESIHIQ PSITPRYSHT AHVFNGKLLL
VGGVWIHSSS VPGVTVISLT TGLSSEYQID TASVPWPLML HNHSSALLPE EQQLLLIGGG
GNCFSFGTYF NPHTVGLDLS SLGLGQ
