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Database: UniProt
Entry: K9P618_CYAGP
LinkDB: K9P618_CYAGP
Original site: K9P618_CYAGP 
ID   K9P618_CYAGP            Unreviewed;       231 AA.
AC   K9P618;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=Cyagr_1230 {ECO:0000313|EMBL:AFY28408.1};
OS   Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Cyanobium.
OX   NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY28408.1, ECO:0000313|Proteomes:UP000010388};
RN   [1] {ECO:0000313|Proteomes:UP000010388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003495; AFY28408.1; -; Genomic_DNA.
DR   RefSeq; WP_015108861.1; NC_019675.1.
DR   AlphaFoldDB; K9P618; -.
DR   STRING; 292564.Cyagr_1230; -.
DR   KEGG; cgc:Cyagr_1230; -.
DR   PATRIC; fig|292564.3.peg.1179; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_1_3; -.
DR   OrthoDB; 9807416at2; -.
DR   Proteomes; UP000010388; 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};
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          24..218
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   231 AA;  25607 MW;  8079E0C41EFF1EE3 CRC64;
     MRFDVVSLVP DAFTPLLGLG VIGRAFAAGI AEVHTHNPRD HATDRYRKVD DVPYGGGAGM
     VLKPEPVYAA FEAIPVLPRR RVLLMSPQGQ PLHQRDLRRW ATEHDQLVLL CGHYEGFDER
     IRPLANEEVS LGDFVLTGGE LPALVVISGV VRLLPGTVGS PDCLEAESHS GLLLEHPHYT
     RPAEFRGMAV PEVLRSGDHG AIARWRLEQQ VARTRERRAD LLALWQAQQE T
//
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