ID   A0A2A3S4L5_9GAMM        Unreviewed;       181 AA.
AC   A0A2A3S4L5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   11-DEC-2019, entry version 10.
DE   RecName: Full=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 TrmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN   Name=trmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN   ORFNames=A6J60_000105 {ECO:0000313|EMBL:PNK59446.1}, A6J60_013255
GN   {ECO:0000313|EMBL:PNK61733.1};
OS   Psychrobacter sp. FDAARGOS_221.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK59446.1, ECO:0000313|Proteomes:UP000217719};
RN   [1] {ECO:0000313|EMBL:PNK59446.1, ECO:0000313|Proteomes:UP000217719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_221 {ECO:0000313|EMBL:PNK59446.1,
RC   ECO:0000313|Proteomes:UP000217719};
RA   Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA   Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA   Aluvathingal J., Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in
CC       the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA).
CC       Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH
CC       of the wobble nucleotide. {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   -!- SUBUNIT: Homodimer. {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: 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:PNK59446.1}.
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DR   EMBL; NWFK02000001; PNK59446.1; -; Genomic_DNA.
DR   EMBL; NWFK02000001; PNK61733.1; -; Genomic_DNA.
DR   Proteomes; UP000217719; Unassembled WGS sequence.
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   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; tRNA_cyt/urid_MeTfrase.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR42971; PTHR42971; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:PNK59446.1};
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,
KW   ECO:0000256|SAAS:SAAS00477754, ECO:0000313|EMBL:PNK59446.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN          3..154
FT                   /note="SpoU_methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   BINDING         82
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT                   ECO:0000256|PIRSR:PIRSR029256-1"
FT   BINDING         112
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT                   ECO:0000256|PIRSR:PIRSR029256-1"
FT   BINDING         134
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT                   ECO:0000256|PIRSR:PIRSR029256-1"
FT   BINDING         142
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT                   ECO:0000256|PIRSR:PIRSR029256-1"
SQ   SEQUENCE   181 AA;  20350 MW;  1DFBB86F8781934E CRC64;
     MTIHIVLVHP RIPNNTGSAI RLCANTGAQL HLVEPLGFDL EDKKLRRAGL DYHEYANMQV
     HKDWEQAKQA LNQAGCERMV ALTTKLSHPF YEYDFAQTDS GDKIENIALV FGSETAGLAD
     DIRADIGEKN WLRLPMLPDS RSLNLANSVS ICLYEVWRQQ GFVGDEGRST GYTELTPYDP
     K
//