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Database: UniProt
Entry: A0A0G1TLZ4_9BACT
LinkDB: A0A0G1TLZ4_9BACT
Original site: A0A0G1TLZ4_9BACT 
ID   A0A0G1TLZ4_9BACT        Unreviewed;       148 AA.
AC   A0A0G1TLZ4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000256|RuleBase:RU003464};
DE            EC=2.1.1.228 {ECO:0000256|RuleBase:RU003464};
DE   Flags: Fragment;
GN   ORFNames=UY10_C0022G0010 {ECO:0000313|EMBL:KKU82831.1};
OS   Microgenomates group bacterium GW2011_GWA2_47_8.
OC   Bacteria.
OX   NCBI_TaxID=1618503 {ECO:0000313|EMBL:KKU82831.1, ECO:0000313|Proteomes:UP000034016};
RN   [1] {ECO:0000313|EMBL:KKU82831.1, ECO:0000313|Proteomes:UP000034016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
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|RuleBase:RU003464};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003464}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003464}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000256|RuleBase:RU003464}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKU82831.1}.
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DR   EMBL; LCOS01000022; KKU82831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1TLZ4; -.
DR   PATRIC; fig|1618503.3.peg.489; -.
DR   Proteomes; UP000034016; Unassembled WGS sequence.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
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   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU003464};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU003464};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU003464};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003464};
KW   tRNA processing {ECO:0000256|RuleBase:RU003464}.
FT   DOMAIN          23..148
FT                   /note="tRNA methyltransferase TRMD/TRM10-type"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   NON_TER         148
FT                   /evidence="ECO:0000313|EMBL:KKU82831.1"
SQ   SEQUENCE   148 AA;  16581 MW;  E87FFBF5BF7EEFF8 CRC64;
     MHITILTLFP EMFVGPFDHS IVKRAKQKGL LTINIVNIRD YATDKHKSVD DRPYGGGTGM
     IMRVDVIDRA IKEQKHVLKE KTIFLDPKGT PYTQAKAREL SRFDHLILIC GHYEGVDERV
     SALVDESISV GDYILTGGEI PAMVLVDS
//
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