ID   TRMB_DANRE              Reviewed;         241 AA.
AC   Q5XJ57; A7MCF3; F1QU80;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE            EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_03055};
DE   AltName: Full=Methyltransferase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03055};
DE   AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03055};
DE   AltName: Full=miRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03055};
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE   AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
GN   Name=mettl1; ORFNames=zgc:103636;
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].
RC   TISSUE=Larva, and Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic component of METTL1-WDR4 methyltransferase complex
CC       that mediates the formation of N(7)-methylguanine in a subset of RNA
CC       species, such as tRNAs, mRNAs and microRNAs (miRNAs). Catalyzes the
CC       formation of N(7)-methylguanine at position 46 (m7G46) in a large
CC       subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable
CC       loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA
CC       tertiary structure and protect tRNAs from decay. Also acts as a
CC       methyltransferase for a subset of internal N(7)-methylguanine in mRNAs.
CC       Internal N(7)-methylguanine methylation of mRNAs in response to stress
CC       promotes their relocalization to stress granules, thereby suppressing
CC       their translation. Also methylates a specific subset of miRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_03055}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC         methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03055};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a guanosine in mRNA + S-adenosyl-L-methionine = an N(7)-
CC         methylguanosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60508, Rhea:RHEA-COMP:15584, Rhea:RHEA-COMP:15585,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74480; Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60509;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a guanosine in miRNA + S-adenosyl-L-methionine = an N(7)-
CC         methylguanosine in miRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60512, Rhea:RHEA-COMP:15587, Rhea:RHEA-COMP:15588,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74480; Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60513;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03055}.
CC   -!- SUBUNIT: Catalytic component of the METTL1-WDR4 complex, composed of
CC       mettl1 and wdr4. {ECO:0000255|HAMAP-Rule:MF_03055}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_03055}.
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DR   EMBL; CABZ01008506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01061933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01061934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU929297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC083450; AAH83450.1; -; mRNA.
DR   EMBL; BC152158; AAI52159.1; -; mRNA.
DR   RefSeq; NP_001005952.1; NM_001005952.1.
DR   RefSeq; XP_005155729.1; XM_005155672.3.
DR   RefSeq; XP_005155730.1; XM_005155673.3.
DR   RefSeq; XP_009303993.1; XM_009305718.2.
DR   AlphaFoldDB; Q5XJ57; -.
DR   SMR; Q5XJ57; -.
DR   STRING; 7955.ENSDARP00000128994; -.
DR   PaxDb; 7955-ENSDARP00000101871; -.
DR   GeneID; 449779; -.
DR   KEGG; dre:449779; -.
DR   AGR; ZFIN:ZDB-GENE-041010-24; -.
DR   CTD; 4234; -.
DR   ZFIN; ZDB-GENE-041010-24; mettl1.
DR   eggNOG; KOG3115; Eukaryota.
DR   InParanoid; Q5XJ57; -.
DR   OMA; LPNYFAK; -.
DR   OrthoDB; 116813at2759; -.
DR   PhylomeDB; Q5XJ57; -.
DR   TreeFam; TF314083; -.
DR   UniPathway; UPA00989; -.
DR   PRO; PR:Q5XJ57; -.
DR   Proteomes; UP000000437; Chromosome 11.
DR   Bgee; ENSDARG00000076518; Expressed in gastrula and 22 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR   GO; GO:0106004; P:tRNA (guanine-N7)-methylation; ISS:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025763; Trm8_euk.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR   PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..241
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000370558"
FT   REGION          141..149
FT                   /note="AlphaC helix"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   REGION          215..223
FT                   /note="Alpha6 helix"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         61
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   CONFLICT        73
FT                   /note="Q -> L (in Ref. 2; AAI52159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="S -> G (in Ref. 2; AAH83450)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   241 AA;  27966 MW;  69B0FE8B16F64E8A CRC64;
     MSVCMPQKRY YRQRAHSNPM ADHTFQYPVC PEQMDWSPLY PQYFPQQEEA GGAQVEFADI
     GCGYGGLLVQ LSQLFPQQLI LGLEIRVKVS DYVQDRIRSL RVAEPGRYQN IACLRSNAMK
     YLPNFFRKGQ LSKMFFLFPD PHFKKTKHKW RIISPTLLAE YAYTLRIGGL VYTNTDVEEV
     HEWIVQHFSD HPLFSRVTEE QLADDIIVGH LGTCTEEGKK VQRNGGKNFL AVFRRVEDPQ
     T
//