TRM1_AQUAE
ID TRM1_AQUAE Reviewed; 392 AA.
AC O67010;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE EC=2.1.1.215 {ECO:0000255|HAMAP-Rule:MF_00290};
GN Name=trm1 {ECO:0000255|HAMAP-Rule:MF_00290}; OrderedLocusNames=aq_841;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19491098; DOI=10.1074/jbc.m109.020024;
RA Awai T., Kimura S., Tomikawa C., Ochi A., Ihsanawati X., Bessho Y.,
RA Yokoyama S., Ohno S., Nishikawa K., Yokogawa T., Suzuki T., Hori H.;
RT "Aquifex aeolicus tRNA (N2,N2-guanine)-dimethyltransferase (Trm1) catalyzes
RT transfer of methyl groups not only to guanine 26 but also to guanine 27 in
RT tRNA.";
RL J. Biol. Chem. 284:20467-20478(2009).
CC -!- FUNCTION: Dimethylates the guanine residues at position 26 and 27 of
CC one or more tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC groups. {ECO:0000255|HAMAP-Rule:MF_00290, ECO:0000269|PubMed:19491098}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26)/guanosine(27) in tRNA + 4 S-adenosyl-L-
CC methionine = 4 H(+) + N(2)-dimethylguanosine(26)/N(2)-
CC dimethylguanosine(27) in tRNA + 4 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43136, Rhea:RHEA-COMP:10353, Rhea:RHEA-COMP:10354,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.215;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00290,
CC ECO:0000269|PubMed:19491098};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|HAMAP-Rule:MF_00290}.
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DR EMBL; AE000657; AAC06976.1; -; Genomic_DNA.
DR PIR; G70372; G70372.
DR RefSeq; NP_213571.1; NC_000918.1.
DR RefSeq; WP_010880509.1; NC_000918.1.
DR PDB; 3AXS; X-ray; 2.16 A; A=1-392.
DR PDB; 3AXT; X-ray; 2.49 A; A=1-392.
DR PDBsum; 3AXS; -.
DR PDBsum; 3AXT; -.
DR AlphaFoldDB; O67010; -.
DR SMR; O67010; -.
DR STRING; 224324.aq_841; -.
DR PRIDE; O67010; -.
DR EnsemblBacteria; AAC06976; AAC06976; aq_841.
DR KEGG; aae:aq_841; -.
DR eggNOG; COG1867; Bacteria.
DR HOGENOM; CLU_010862_5_1_0; -.
DR InParanoid; O67010; -.
DR OMA; VFYNPVM; -.
DR OrthoDB; 996713at2; -.
DR BioCyc; MetaCyc:MON-16631; -.
DR BRENDA; 2.1.1.215; 396.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.30.56.70; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00290; tRNA_dimethyltr_TRM1; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR022923; TRM1_arc_bac.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR PANTHER; PTHR10631; PTHR10631; 1.
DR Pfam; PF02005; TRM; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00308; TRM1; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..392
FT /note="tRNA (guanine(26)-N(2)/guanine(27)-N(2))-
FT dimethyltransferase"
FT /id="PRO_0000147678"
FT DOMAIN 2..375
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:3AXS"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3AXS"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3AXS"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:3AXS"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3AXT"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3AXS"
FT HELIX 368..384
FT /evidence="ECO:0007829|PDB:3AXS"
SQ SEQUENCE 392 AA; 45479 MW; D2441A3754566043 CRC64;
MEIVQEGIAK IIVPEIPKTV SSDMPVFYNP RMRVNRDLAV LGLEYLCKKL GRPVKVADPL
SASGIRAIRF LLETSCVEKA YANDISSKAI EIMKENFKLN NIPEDRYEIH GMEANFFLRK
EWGFGFDYVD LDPFGTPVPF IESVALSMKR GGILSLTATD TAPLSGTYPK TCMRRYMARP
LRNEFKHEVG IRILIKKVIE LAAQYDIAMI PIFAYSHLHY FKLFFVKERG VEKVDKLIEQ
FGYIQYCFNC MNREVVTDLY KFKEKCPHCG SKFHIGGPLW IGKLWDEEFT NFLYEEAQKR
EEIEKETKRI LKLIKEESQL QTVGFYVLSK LAEKVKLPAQ PPIRIAVKFF NGVRTHFVGD
GFRTNLSFEE VMKKMEELKE KQKEFLEKKK QG
