ID A0A173DZ22_9CHLA Unreviewed; 161 AA.
AC A0A173DZ22;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Putative tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885};
DE EC=2.1.1.207 {ECO:0000256|HAMAP-Rule:MF_01885};
DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885};
GN ORFNames=M787_002325 {ECO:0000313|EMBL:ANG66153.1};
OS Chlamydia gallinacea 08-1274/3.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=1143323 {ECO:0000313|EMBL:ANG66153.1, ECO:0000313|Proteomes:UP000019147};
RN [1] {ECO:0000313|EMBL:ANG66153.1, ECO:0000313|Proteomes:UP000019147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08-1274/3 {ECO:0000313|EMBL:ANG66153.1,
RC ECO:0000313|Proteomes:UP000019147};
RX PubMed=24461712; DOI=10.1016/j.syapm.2013.12.004;
RA Sachse K., Laroucau K., Riege K., Wehner S., Dilcher M., Creasy H.H.,
RA Weidmann M., Myers G., Vorimore F., Vicari N., Magnino S.,
RA Liebler-Tenorio E., Ruettger A., Bavoil P.M., Hufert F.T.,
RA Rossello-Mora R., Marz M.;
RT "Evidence for the existence of two new members of the family Chlamydiaceae
RT and proposal of Chlamydia avium sp. nov. and Chlamydia gallinacea sp.
RT nov.";
RL Syst. Appl. Microbiol. 37:79-88(2014).
CC -!- FUNCTION: Could methylate the ribose at the nucleotide 34 wobble
CC position in tRNA. {ECO:0000256|HAMAP-Rule:MF_01885}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-
CC adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-
CC methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333, Rhea:RHEA-COMP:10334,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74508, ChEBI:CHEBI:74511; EC=2.1.1.207;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43084, Rhea:RHEA-COMP:10331, Rhea:RHEA-COMP:10332,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.207;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01885};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01885}.
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DR EMBL; CP015840; ANG66153.1; -; Genomic_DNA.
DR RefSeq; WP_021828853.1; NZ_CP015840.1.
DR AlphaFoldDB; A0A173DZ22; -.
DR STRING; 1143323.M787_002325; -.
DR GeneID; 81478139; -.
DR KEGG; cgz:M787_002325; -.
DR eggNOG; COG0219; Bacteria.
DR OrthoDB; 9789043at2; -.
DR Proteomes; UP000019147; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0141102; F:tRNA (5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0141098; F:tRNA (cytidine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd18094; SpoU-like_TrmL; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR016914; TrmL.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42971; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR42971:SF1; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW ECO:0000313|EMBL:ANG66153.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885,
KW ECO:0000256|PIRSR:PIRSR029256-1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01885, ECO:0000313|EMBL:ANG66153.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT DOMAIN 2..140
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
SQ SEQUENCE 161 AA; 17950 MW; E692F0B83A5A00F8 CRC64;
MRVVLYNPDI PQNTGNIGRT CLALGASLIL VRPLGFSLLD KFVKRAGMDY WDQVNVSVVD
SLEEALAGVS LDKMFFLSTK GSKYYGEASL PIDGTYIFGS ESKGLPEEML KQYYNHCYYL
PMRPGIRSLN LATTVGVVLF EVVRQNNYSS YIRKGLSVLS N
//
