ID A5Z7S8_9FIRM Unreviewed; 164 AA.
AC A5Z7S8;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=EUBVEN_01766 {ECO:0000313|EMBL:EDM50985.1};
OS Eubacterium ventriosum ATCC 27560.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=411463 {ECO:0000313|EMBL:EDM50985.1, ECO:0000313|Proteomes:UP000006000};
RN [1] {ECO:0000313|EMBL:EDM50985.1, ECO:0000313|Proteomes:UP000006000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM50985.1,
RC ECO:0000313|Proteomes:UP000006000};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM50985.1, ECO:0000313|Proteomes:UP000006000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM50985.1,
RC ECO:0000313|Proteomes:UP000006000};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium ventriosum (ATCC 27560).";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01885}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDM50985.1}.
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DR EMBL; AAVL02000035; EDM50985.1; -; Genomic_DNA.
DR RefSeq; WP_005363265.1; NZ_DS264285.1.
DR AlphaFoldDB; A5Z7S8; -.
DR STRING; 411463.EUBVEN_01766; -.
DR GeneID; 66465717; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_0_0_9; -.
DR OrthoDB; 9789043at2; -.
DR Proteomes; UP000006000; Unassembled WGS sequence.
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:EDM50985.1};
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:EDM50985.1};
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 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 164 AA; 18912 MW; 5404DE0307B31471 CRC64;
MNVILLEPEI PQNTGNIGRT CCATGTKLHL IEPMGFRINE KNLKRAGMDY WDDLDVTIYD
SFKDFMDQHP GIKIWMATTK APHRYTDVEF GPDDYIMFGK ESAGIPEEIL VDNEDTCIRI
PMNPEIRSLN LANSVAIVLY EALRQNDFHG MQMEGHLHRL QWKE
//
