TRMD_PARP8
ID TRMD_PARP8 Reviewed; 255 AA.
AC B2JF31;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Bphy_0771;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69960.1; -; Genomic_DNA.
DR RefSeq; WP_012400180.1; NZ_CADFGH010000007.1.
DR PDB; 4H3Y; X-ray; 2.50 A; A/B=1-255.
DR PDB; 4H3Z; X-ray; 2.15 A; A/B=1-255.
DR PDBsum; 4H3Y; -.
DR PDBsum; 4H3Z; -.
DR AlphaFoldDB; B2JF31; -.
DR SMR; B2JF31; -.
DR STRING; 391038.Bphy_0771; -.
DR EnsemblBacteria; ACC69960; ACC69960; Bphy_0771.
DR KEGG; bph:Bphy_0771; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_2_4; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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..255
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_1000130145"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 137..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:4H3Z"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:4H3Z"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 205..223
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:4H3Z"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:4H3Z"
SQ SEQUENCE 255 AA; 28462 MW; 99315D28355C3172 CRC64;
MQFDIVTLFP DMFRALTDWG ITSRAAKQER YGLRTWNPRD FTTDNYRTID DRPYGGGPGM
VMLARPLEDA INAAKAAQAE QGIGGARVVM MSPQGATLNH DKVMRFAAEP GLILLCGRYE
AIDQRLIDRV VDEEVSLGDF VLSGGELPAM ALIDAVVRHL PGVLNDAQSA VQDSFVDGLL
DCPHYTRPEE YDGVRVPDVL LGGHHAEIEQ WRRREALRNT WLKRPDLIVQ ARKNKLLSRA
DEAWLASLAK DASKH
