TRM1_SULAC
ID TRM1_SULAC Reviewed; 382 AA.
AC Q4J947;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE EC=2.1.1.216 {ECO:0000255|HAMAP-Rule:MF_00290};
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
GN Name=trm1 {ECO:0000255|HAMAP-Rule:MF_00290}; OrderedLocusNames=Saci_1343;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of a
CC number of tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC groups. {ECO:0000255|HAMAP-Rule:MF_00290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00290};
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; CP000077; AAY80678.1; -; Genomic_DNA.
DR RefSeq; WP_011278180.1; NC_007181.1.
DR AlphaFoldDB; Q4J947; -.
DR SMR; Q4J947; -.
DR STRING; 330779.Saci_1343; -.
DR PRIDE; Q4J947; -.
DR EnsemblBacteria; AAY80678; AAY80678; Saci_1343.
DR GeneID; 3473456; -.
DR KEGG; sai:Saci_1343; -.
DR PATRIC; fig|330779.12.peg.1296; -.
DR eggNOG; arCOG01219; Archaea.
DR HOGENOM; CLU_010862_5_1_2; -.
DR OMA; VFYNPVM; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..382
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_1000197039"
FT DOMAIN 4..373
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ SEQUENCE 382 AA; 43464 MW; DEF5CEC3B19259C6 CRC64;
MSLVEIIEGK ARILIPNYKD YMKDGKFDPS WAPVFYNPKM ILNRDLSVLA ANVVKPKSLI
DGLSATGVRG IRYGLEINGV EEIILNDIDS DAVELIKKNV KINDLESRAK IYNNNINSLL
HEIKVDYVDI DPFGSPAPFL LSSFSAAKSK QYVAITATDL AALMCSSKTS ARRKYGLICN
KMSFSRELGL RGLISKAITE AAVVEKAVTP VFSFYNDYYY RVIFKVERGA KKVDRQLSKL
VYYYECPKCG YRIESEYLQQ MKCTNCNLVM QTYGPAYKES LVDYEFLNNM ISELDKFSYF
QTFSKLKSIL LTIKDESKYS ENYYRIDFLA SLARVNVPRR DNVINCLVDA SRTHLDPLGV
KTSKNLDEIK ECIKKLSSRN TS