TRM56_HALMA
ID TRM56_HALMA Reviewed; 180 AA.
AC Q5V3R4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=tRNA (cytidine(56)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00077};
DE EC=2.1.1.206 {ECO:0000255|HAMAP-Rule:MF_00077};
DE AltName: Full=tRNA ribose 2'-O-methyltransferase aTrm56 {ECO:0000255|HAMAP-Rule:MF_00077};
GN OrderedLocusNames=rrnAC0857;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
CC -!- FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose
CC methylation of cytidine at position 56 in tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_00077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42968, Rhea:RHEA-COMP:10308, Rhea:RHEA-COMP:10309,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.206;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00077};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00077}.
CC -!- SIMILARITY: Belongs to the aTrm56 family. {ECO:0000255|HAMAP-
CC Rule:MF_00077}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY596297; AAV45838.1; -; Genomic_DNA.
DR RefSeq; WP_011223279.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V3R4; -.
DR SMR; Q5V3R4; -.
DR STRING; 272569.rrnAC0857; -.
DR EnsemblBacteria; AAV45838; AAV45838; rrnAC0857.
DR GeneID; 40151882; -.
DR KEGG; hma:rrnAC0857; -.
DR PATRIC; fig|272569.17.peg.1596; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_123709_0_0_2; -.
DR OMA; VVHLTMY; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00077; tRNA_methyltr_aTrm56; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR InterPro; IPR002845; tRNA_mtfrase_aTrm56.
DR PANTHER; PTHR42197; PTHR42197; 1.
DR Pfam; PF01994; Trm56; 1.
DR PIRSF; PIRSF016123; UCP016123; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..180
FT /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT /id="PRO_0000365298"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT BINDING 112..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ SEQUENCE 180 AA; 20120 MW; 4F5342912E0C410A CRC64;
MKDSPQVTVL RLGHRPGRDE RMTTHVGLTA RALGADKVVL ANAARNQADT VIDITDRFGG
PFDVASTEEP KRLIRDFEGR VVHLTMYGEP VQEVEADVRE ANTAEPLLVV VGAEKVPFEV
YEHADWNVGV TNQPHSEVAS LAVFLDRLFE GRELDREWEN PDRVVVPQET GKRVVDPDEE
