TRMD_ANAPZ
ID TRMD_ANAPZ Reviewed; 232 AA.
AC Q2GIL5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_00605};
DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
GN Name=trmD {ECO:0000255|HAMAP-Rule:MF_00605}; OrderedLocusNames=APH_1267;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00605};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00605}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00605}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC {ECO:0000255|HAMAP-Rule:MF_00605}.
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DR EMBL; CP000235; ABD43497.1; -; Genomic_DNA.
DR RefSeq; WP_011451293.1; NC_007797.1.
DR PDB; 3KNU; X-ray; 2.25 A; A/B/C/D=1-232.
DR PDB; 4IG6; X-ray; 2.40 A; A=1-232.
DR PDBsum; 3KNU; -.
DR PDBsum; 4IG6; -.
DR AlphaFoldDB; Q2GIL5; -.
DR SMR; Q2GIL5; -.
DR STRING; 212042.APH_1267; -.
DR EnsemblBacteria; ABD43497; ABD43497; APH_1267.
DR GeneID; 56369113; -.
DR KEGG; aph:APH_1267; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_5; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR EvolutionaryTrace; Q2GIL5; -.
DR Proteomes; UP000001943; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd18080; TrmD-like; 1.
DR Gene3D; 1.10.1270.20; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00605; TrmD; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR46417; PTHR46417; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF000386; tRNA_mtase; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00088; trmD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..232
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000257389"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 132..137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:3KNU"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:3KNU"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3KNU"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:3KNU"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3KNU"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3KNU"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:3KNU"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:4IG6"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:3KNU"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4IG6"
SQ SEQUENCE 232 AA; 25761 MW; 413D471EE118F339 CRC64;
MIFNVLTIFP QMFPGPLGVS NLGSALKKGL WTLNVFDIRA FANNKHNTVD DTPYGGGPGM
LLRADVLGRC IDEVLSLHPN TKLMFTSPRG VSFTQDIARQ TMNFDNITLL CGRFEGIDER
VVDFYKLQEV SIGDYVLSGG ELAAMVIIDT CVRMVPGVIG NAESLKQESM EGSLEYPQYT
RPASWKGMEV PEVLLTGNHG EIEKWRRNAS LSITAARRPD LLKDRYGEND VE
