ID   A0A2A3S4L5_9GAMM        Unreviewed;       181 AA.
AC   A0A2A3S4L5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-FEB-2018, entry version 3.
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_00105 {ECO:0000313|EMBL:PBN95514.1}, A6J60_13275
GN   {ECO:0000313|EMBL:PBN97803.1};
OS   Psychrobacter sp. FDAARGOS_221.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=1975705 {ECO:0000313|EMBL:PBN95514.1, ECO:0000313|Proteomes:UP000217719};
RN   [1] {ECO:0000313|EMBL:PBN95514.1, ECO:0000313|Proteomes:UP000217719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_221 {ECO:0000313|EMBL:PBN95514.1,
RC   ECO:0000313|Proteomes:UP000217719};
RA   Minogue T., Wolcott M., Wasieloski L., Jaissle J., Tallon L.,
RA   Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S.,
RA   Nadendla S., Geyer C., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx
RT   tests.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble
CC       position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and
CC       tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-
CC       adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
CC       {ECO:0000256|HAMAP-Rule:MF_01885}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 5-
CC       carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L-
CC       homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34)
CC       in tRNA(Leu). {ECO:0000256|HAMAP-Rule:MF_01885}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(34) in tRNA
CC       = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(34) in tRNA.
CC       {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
CC       methyltransferase superfamily. RNA methyltransferase TrmH family.
CC       TrmL subfamily. {ECO:0000256|HAMAP-Rule:MF_01885}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PBN95514.1}.
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DR   EMBL; NWFK01000001; PBN95514.1; -; Genomic_DNA.
DR   EMBL; NWFK01000001; PBN97803.1; -; 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   Complete proteome {ECO:0000313|Proteomes:UP000217719};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00120900, ECO:0000313|EMBL:PBN95514.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217719};
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:SAAS00121476, ECO:0000313|EMBL:PBN95514.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN        3    154       SpoU_methylase. {ECO:0000259|Pfam:
FT                                PF00588}.
FT   BINDING      82     82       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
FT   BINDING     112    112       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01885, ECO:0000256|PIRSR:PIRSR029256-
FT                                1}.
FT   BINDING     134    134       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
FT   BINDING     142    142       S-adenosyl-L-methionine.
FT                                {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
//