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Database: UniProt
Entry: B1VF40_CORU7
LinkDB: B1VF40_CORU7
Original site: B1VF40_CORU7 
ID   B1VF40_CORU7            Unreviewed;       195 AA.
AC   B1VF40;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   OrderedLocusNames=cu0419 {ECO:0000313|EMBL:CAQ04379.1};
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ04379.1, ECO:0000313|Proteomes:UP000001727};
RN   [1] {ECO:0000313|EMBL:CAQ04379.1, ECO:0000313|Proteomes:UP000001727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
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}.
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DR   EMBL; AM942444; CAQ04379.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1VF40; -.
DR   STRING; 504474.cu0419; -.
DR   KEGG; cur:cu0419; -.
DR   eggNOG; COG0219; Bacteria.
DR   HOGENOM; CLU_110125_1_0_11; -.
DR   OMA; AGLDYWH; -.
DR   Proteomes; UP000001727; 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   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:CAQ04379.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001727};
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};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN          30..183
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141
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         163
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         171
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   195 AA;  20984 MW;  FE6060CA874F3642 CRC64;
     MSSQPSTPAS AAGRSSSLTT SPRPAAEPPF HILFDQPQIP PNTGNAIRMC AGTGATLHLA
     GPLGFNFEEK HVRRAGLDYH DLANVQLHED FEAAAAHLTG LSRQQAAAGA QPQTRIFAFT
     THAKTWFTDV DFRRGDVLLF GPEPTGLDEE TLADPRITAQ LRIPMLPARR SMNLSNAAAV
     AAYEAWRQLG FPGGQ
//
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