GenomeNet

Database: UniProt
Entry: A0A0B5AQ00_9BACL
LinkDB: A0A0B5AQ00_9BACL
Original site: A0A0B5AQ00_9BACL 
ID   A0A0B5AQ00_9BACL        Unreviewed;       205 AA.
AC   A0A0B5AQ00;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=JMA_12760 {ECO:0000313|EMBL:AJD90593.1};
OS   Jeotgalibacillus malaysiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=1508404 {ECO:0000313|EMBL:AJD90593.1, ECO:0000313|Proteomes:UP000031449};
RN   [1] {ECO:0000313|EMBL:AJD90593.1, ECO:0000313|Proteomes:UP000031449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D5 {ECO:0000313|EMBL:AJD90593.1,
RC   ECO:0000313|Proteomes:UP000031449};
RA   Yaakop A.S., Chan K.-G., Goh K.M.;
RT   "Complete genome of a marine bacteria Jeotgalibacillus malaysiensis.";
RL   Submitted (AUG-2014) 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   ---------------------------------------------------------------------------
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; CP009416; AJD90593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5AQ00; -.
DR   STRING; 1508404.JMA_12760; -.
DR   KEGG; jeo:JMA_12760; -.
DR   HOGENOM; CLU_110125_0_0_9; -.
DR   BioCyc; JESP1508404:G14D9-10530-MONOMER; -.
DR   Proteomes; UP000031449; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule.
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   NCBIfam; TIGR00185; tRNA_yibK_trmL; 1.
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   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:AJD90593.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01885, ECO:0000313|EMBL:AJD90593.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN          51..193
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885"
SQ   SEQUENCE   205 AA;  23289 MW;  B706E67E3456D564 CRC64;
     MHIQTIAGED CGHIVIQPLI LHRSGIIFFT FHDKIENGSA EIHDEVKTLG LHVVLFQPEI
     PANTGNIART CAATGTSLHL IKPLGFSTDD KMLKRAGLDY WQHVDIHYHE SLEDFYQASE
     GGEYFYLTKY GTKPHSTFDY SDMEKDFYFI FGRETSGLPD DVIENNKDRA LRIPMNEHVR
     SLNLSNTAAI LVYEALRQQN YPSLG
//
DBGET integrated database retrieval system