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Database: UniProt
Entry: A0A0F6TBV3_9CORY
LinkDB: A0A0F6TBV3_9CORY
Original site: A0A0F6TBV3_9CORY 
ID   A0A0F6TBV3_9CORY        Unreviewed;       280 AA.
AC   A0A0F6TBV3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000256|ARBA:ARBA00014679, ECO:0000256|HAMAP-Rule:MF_00605};
DE            EC=2.1.1.228 {ECO:0000256|ARBA:ARBA00012807, ECO:0000256|HAMAP-Rule:MF_00605};
DE   AltName: Full=M1G-methyltransferase {ECO:0000256|ARBA:ARBA00029736, ECO:0000256|HAMAP-Rule:MF_00605};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|ARBA:ARBA00033392, ECO:0000256|HAMAP-Rule:MF_00605};
GN   Name=trmD {ECO:0000256|HAMAP-Rule:MF_00605,
GN   ECO:0000313|EMBL:AKE39436.1};
GN   ORFNames=NG00_01353 {ECO:0000313|EMBL:AVH88599.1}, UL81_07405
GN   {ECO:0000313|EMBL:AKE39436.1};
OS   Corynebacterium camporealensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39436.1, ECO:0000313|Proteomes:UP000033566};
RN   [1] {ECO:0000313|Proteomes:UP000029996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105508 {ECO:0000313|Proteomes:UP000029996};
RA   Hassan S.S., Tiwari S., Jamal S.B., Oliveira L.D.C., Souza F.,
RA   Mariano D.C., Almeida S., Dorella F., Pereira F., Carvalho A., Leal C.A.,
RA   Soares S.D.C., Figueiredo H.C., Silva A., Azevedo V.A.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AVH88599.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105508 {ECO:0000313|EMBL:AVH88599.1};
RA   Seo M.-J., Seok Y.J., Cha I.-T.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AKE39436.1, ECO:0000313|Proteomes:UP000033566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39436.1,
RC   ECO:0000313|Proteomes:UP000033566};
RX   PubMed=26021938;
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT   Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL   Genome Announc. 3:e00572-15(2015).
RN   [4] {ECO:0000313|EMBL:AVH88599.1, ECO:0000313|Proteomes:UP000029996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105508 {ECO:0000313|EMBL:AVH88599.1,
RC   ECO:0000313|Proteomes:UP000029996};
RA   Coimbra N., Jamal S.B., Jaiswal A., Silva A.L., Azevedo V.;
RT   "Genome sequencing of Corynebacterium camporealensis CIP 105508.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000256|ARBA:ARBA00002634, ECO:0000256|HAMAP-Rule:MF_00605}.
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:0000256|ARBA:ARBA00001189, ECO:0000256|HAMAP-
CC         Rule:MF_00605};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00605}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00605}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000256|ARBA:ARBA00007630, ECO:0000256|HAMAP-Rule:MF_00605}.
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DR   EMBL; CP011311; AKE39436.1; -; Genomic_DNA.
DR   EMBL; CP027001; AVH88599.1; -; Genomic_DNA.
DR   RefSeq; WP_035105087.1; NZ_CP027001.1.
DR   AlphaFoldDB; A0A0F6TBV3; -.
DR   STRING; 161896.UL81_07405; -.
DR   KEGG; ccj:UL81_07405; -.
DR   PATRIC; fig|161896.4.peg.1448; -.
DR   HOGENOM; CLU_047363_0_0_11; -.
DR   OrthoDB; 9807416at2; -.
DR   Proteomes; UP000029996; Chromosome.
DR   Proteomes; UP000033566; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   Gene3D; 1.10.1270.20; tRNA(m1g37)methyltransferase, domain 2; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_TrmD.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR46417; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46417:SF1; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 2.
DR   PIRSF; PIRSF000386; tRNA_mtase; 2.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00605};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00605}; Reference proteome {ECO:0000313|Proteomes:UP000033566};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00605};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00605}.
FT   DOMAIN          22..77
FT                   /note="tRNA methyltransferase TRMD/TRM10-type"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   DOMAIN          113..259
FT                   /note="tRNA methyltransferase TRMD/TRM10-type"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   REGION          71..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00605,
FT                   ECO:0000256|PIRSR:PIRSR000386-1"
FT   BINDING         171..176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00605,
FT                   ECO:0000256|PIRSR:PIRSR000386-1"
SQ   SEQUENCE   280 AA;  30968 MW;  A63A008EAD28E27E CRC64;
     MRLDVITIFP EYLDPLRHAL LGKAIEQGKL AVGVHDLRQW ATDRHKSVDD TPFGGGPGMV
     MKPEVWGPAL DDVATGSTST PDLESSLPHL NKPRRDDVAG VTPQGYGGGE EGIDKPLLIV
     PTPAGKPFTQ ADAQAWSAEQ HIVFACGRYE GIDQRVVEDA EKRYRVREVS IGDYVLIGGE
     VATLVIAEAV VRLVPGVLGN QRSHEEDSFS DGLLEGPSYT KPRQWRGLEV PEVLTSGNHA
     KVDRWRREQS LLRTWQHRPE LLDDVELSKA DRAFLDSLRD
//
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