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TRM5_DROME
ID   TRM5_DROME              Reviewed;         457 AA.
AC   Q8IRE4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE            EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000255|HAMAP-Rule:MF_03152};
GN   ORFNames=CG32281;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.E.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC       various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC       dependent on the nature of the nucleoside 5' of the target nucleoside.
CC       This is the first step in the biosynthesis of wybutosine (yW), a
CC       modified base adjacent to the anticodon of tRNAs and required for
CC       accurate decoding. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC       mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR   EMBL; AE014296; AAN11538.2; -; Genomic_DNA.
DR   EMBL; BT082011; ACO57630.1; -; mRNA.
DR   RefSeq; NP_728821.2; NM_167995.2.
DR   AlphaFoldDB; Q8IRE4; -.
DR   SMR; Q8IRE4; -.
DR   STRING; 7227.FBpp0072898; -.
DR   PaxDb; Q8IRE4; -.
DR   PRIDE; Q8IRE4; -.
DR   DNASU; 317953; -.
DR   EnsemblMetazoa; FBtr0073034; FBpp0072898; FBgn0052281.
DR   GeneID; 317953; -.
DR   KEGG; dme:Dmel_CG32281; -.
DR   UCSC; CG32281-RA; d. melanogaster.
DR   FlyBase; FBgn0052281; CG32281.
DR   VEuPathDB; VectorBase:FBgn0052281; -.
DR   eggNOG; KOG2078; Eukaryota.
DR   GeneTree; ENSGT00940000153304; -.
DR   HOGENOM; CLU_022610_2_3_1; -.
DR   InParanoid; Q8IRE4; -.
DR   OMA; PKKQMFC; -.
DR   OrthoDB; 788980at2759; -.
DR   PhylomeDB; Q8IRE4; -.
DR   BioGRID-ORCS; 317953; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 317953; -.
DR   PRO; PR:Q8IRE4; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0052281; Expressed in eye disc (Drosophila) and 23 other tissues.
DR   Genevisible; Q8IRE4; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070901; P:mitochondrial tRNA methylation; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03152; TRM5; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..457
FT                   /note="tRNA (guanine(37)-N1)-methyltransferase"
FT                   /id="PRO_0000414129"
FT   BINDING         240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         278..279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         306..307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ   SEQUENCE   457 AA;  53074 MW;  2BD7AAA9FA17336E CRC64;
     MFIVSRLKDL TIITNRLRHY FRNMDVKELQ PPSSVRGMQE LQREQFRKIV QVPRLRVPES
     QVQRVMPLVK KFLLKMEHLH PVRAVDQSRE ILLHPTPVKN WDSLPTEDLQ RQKVNAENFS
     FADLELRYEN WSANEILKSV LPTEEEGLTS YSRIGHIAHL NLRDHLLPYK QLIGQVLRDK
     LPNCRTVVNK ASSIDNTYRN FQLELICGDP DYQVETKENG VPFEFDFSKV YWNPRLSTEH
     ERIVKMLKSD DVLYDVFAGV GPFSIPAAKK RCHVLANDLN PESFRWLQHN AKRNKCLPNI
     KMSNKDGRQF IVEELREDLL KRLCTTDTTT YGIHITMNLP AMAVEFLDAF RGLYSADELA
     QLPTNVCYPT VHVYSFAKGE NTKELVRQLV ESNLGASLDE NLLQGINFVR NVAPNKDMYR
     VSFKLSLNML TTLKEVEVTR KRYAEEELEV ATKVKCV
 
 
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