TRM56_IGNH4
ID TRM56_IGNH4 Reviewed; 218 AA.
AC A8ABJ8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Igni_1123;
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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}.
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DR EMBL; CP000816; ABU82300.1; -; Genomic_DNA.
DR RefSeq; WP_012123264.1; NC_009776.1.
DR AlphaFoldDB; A8ABJ8; -.
DR SMR; A8ABJ8; -.
DR STRING; 453591.Igni_1123; -.
DR EnsemblBacteria; ABU82300; ABU82300; Igni_1123.
DR GeneID; 5561777; -.
DR KEGG; iho:Igni_1123; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_123709_0_0_2; -.
DR OMA; VVHLTMY; -.
DR OrthoDB; 83050at2157; -.
DR PhylomeDB; A8ABJ8; -.
DR Proteomes; UP000000262; Chromosome.
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 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..218
FT /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT /id="PRO_0000365302"
FT REGION 170..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT BINDING 106..110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT BINDING 124..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ SEQUENCE 218 AA; 24058 MW; DEE98454F004F92A CRC64;
MKVYVLRIGH RPDRDKRITT HVGLVARAFG AHGFVLSPCD EKVLEKLRDV EERWGRLLEE
IACTNSPLKY VKTWDGTVVH LTMYGLPVDS VIDEIRQKDK ILVIVGAEKV PREYYELAHY
NVAIGNQPHS EVAALAIFLD RLYGGAELYR QPVGGKLRII PTEKGKKVVK VGEEGPSGGA
PGVRAERGRG GRGEGVQGAD EVRGHKRGAT DRDLGDET
