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Database: UniProt
Entry: B2KCP9_ELUMP
LinkDB: B2KCP9_ELUMP
Original site: B2KCP9_ELUMP 
ID   B2KCP9_ELUMP            Unreviewed;       237 AA.
AC   B2KCP9;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 95.
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|HAMAP-Rule:MF_00605};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605};
GN   Name=trmD {ECO:0000256|HAMAP-Rule:MF_00605};
GN   OrderedLocusNames=Emin_0740 {ECO:0000313|EMBL:ACC98295.1};
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98295.1, ECO:0000313|Proteomes:UP000001029};
RN   [1] {ECO:0000313|EMBL:ACC98295.1, ECO:0000313|Proteomes:UP000001029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191 {ECO:0000313|EMBL:ACC98295.1,
RC   ECO:0000313|Proteomes:UP000001029};
RX   PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000256|ARBA:ARBA00002634, ECO:0000256|HAMAP-Rule:MF_00605,
CC       ECO:0000256|RuleBase:RU003464}.
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, ECO:0000256|RuleBase:RU003464};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00605, ECO:0000256|RuleBase:RU003464}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000256|ARBA:ARBA00007630, ECO:0000256|HAMAP-Rule:MF_00605,
CC       ECO:0000256|RuleBase:RU003464}.
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DR   EMBL; CP001055; ACC98295.1; -; Genomic_DNA.
DR   RefSeq; WP_012414910.1; NC_010644.1.
DR   AlphaFoldDB; B2KCP9; -.
DR   STRING; 445932.Emin_0740; -.
DR   KEGG; emi:Emin_0740; -.
DR   HOGENOM; CLU_047363_0_1_0; -.
DR   OrthoDB; 9807416at2; -.
DR   Proteomes; UP000001029; 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   NCBIfam; TIGR00088; trmD; 1.
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; 1.
DR   PIRSF; PIRSF000386; tRNA_mtase; 1.
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:UP000001029};
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          25..219
FT                   /note="tRNA methyltransferase TRMD/TRM10-type"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   BINDING         112
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         131..136
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   237 AA;  26631 MW;  C01E884A0B27C265 CRC64;
     MSIKIDVVTP FPDIVDGPLG QSIPGRARKE KILNLGFCNP RDFVKDKHKS IDDRVYGGGA
     GMLMKAEPLY QAIKKLRKKG SVVIYTSPRG KVFNQTLAKK LSLKKHLIFV CGHYEGVDAR
     IYPEFDLEVS LGDFILTGGE SAAVVMIDAI TRLLPGVFKK SGVTELESFE NNLLEPPQYT
     RPEVWRRKRV PAVLLSGNHK EIETWKQKEA VKITKKFRPD LLPTSEKRTS LKAKKAK
//
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