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Database: UniProt
Entry: A0A099PCP6_9GAMM
LinkDB: A0A099PCP6_9GAMM
Original site: A0A099PCP6_9GAMM 
ID   A0A099PCP6_9GAMM        Unreviewed;       245 AA.
AC   A0A099PCP6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ECO:0000313|EMBL:KGK42650.1};
GN   ORFNames=LH51_05505 {ECO:0000313|EMBL:KGK42650.1};
OS   Nitrincola sp. A-D6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK42650.1, ECO:0000313|Proteomes:UP000029924};
RN   [1] {ECO:0000313|EMBL:KGK42650.1, ECO:0000313|Proteomes:UP000029924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-D6 {ECO:0000313|EMBL:KGK42650.1,
RC   ECO:0000313|Proteomes:UP000029924};
RA   Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA   Fernandez S., Ferrer A., Chavez R., Levican G.;
RT   "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT   Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL   Submitted (SEP-2014) 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       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}.
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:KGK42650.1}.
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DR   EMBL; JRLB01000027; KGK42650.1; -; Genomic_DNA.
DR   RefSeq; WP_036520526.1; NZ_JRLB01000027.1.
DR   AlphaFoldDB; A0A099PCP6; -.
DR   STRING; 1545442.LH51_05505; -.
DR   OrthoDB; 9807416at2; -.
DR   Proteomes; UP000029924; 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: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:UP000029924};
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          23..221
FT                   /note="tRNA methyltransferase TRMD/TRM10-type"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   BINDING         113
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         133..138
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   245 AA;  27273 MW;  F16AAC48B548D32F CRC64;
     MWFGIVSLFP EMFDAVTGYG ITGRAVRSGL LEVECWNPRD FTLDKHRTVD DRPYGGGPGM
     LMKVQPLRDA IQAARLKAPG QPRVIYLSPQ GRRLDQAGVS ELAVADSLIL VAGRYEGIDE
     RLLDADIDEE WSLGDFVLSG GELPAMVMVD AVSRMLPGVL GHEDSAAEDS FAAGLLDCPH
     YTRPETLDDK QVPSVLLGGN HADIKRWRLK QQLGRTWQRR PDLLEKIEFS PEQQALLSEY
     IREAE
//
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