GenomeNet

Database: UniProt
Entry: A0A1A0FHY5_9GAMM
LinkDB: A0A1A0FHY5_9GAMM
Original site: A0A1A0FHY5_9GAMM 
ID   A0A1A0FHY5_9GAMM        Unreviewed;       269 AA.
AC   A0A1A0FHY5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-JUL-2019, entry version 17.
DE   RecName: Full=tRNA 5-carboxymethoxyuridine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_02057};
DE   AltName: Full=cmo5U methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
GN   Name=cmoM {ECO:0000256|HAMAP-Rule:MF_02057};
GN   ORFNames=ADS46_01355 {ECO:0000313|EMBL:OAZ99090.1};
OS   Halomonas sp. G11.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1684425 {ECO:0000313|EMBL:OAZ99090.1, ECO:0000313|Proteomes:UP000092250};
RN   [1] {ECO:0000313|EMBL:OAZ99090.1, ECO:0000313|Proteomes:UP000092250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G11 {ECO:0000313|EMBL:OAZ99090.1,
RC   ECO:0000313|Proteomes:UP000092250};
RA   Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M.,
RA   Ghedira K., Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA   Eddine Masmoudi A.S., Cherif A.;
RT   "Genomic basis for crude oil degradation, heavy metal resistance and
RT   high salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated
RT   from Tunisian Chott El-Djerid salt lake.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of 5-carboxymethoxyuridine
CC       (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at
CC       position 34 in tRNAs. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-
CC         methionine = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:54080, Rhea:RHEA-
CC         COMP:13383, Rhea:RHEA-COMP:13781, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:136879, ChEBI:CHEBI:138053;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02057};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. CmoM family. {ECO:0000256|HAMAP-
CC       Rule:MF_02057}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02057}.
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:OAZ99090.1}.
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; LYXG01000012; OAZ99090.1; -; Genomic_DNA.
DR   RefSeq; WP_066317741.1; NZ_LYXG01000012.1.
DR   EnsemblBacteria; OAZ99090; OAZ99090; ADS46_01355.
DR   Proteomes; UP000092250; Unassembled WGS sequence.
DR   GO; GO:0097697; F:tRNA 5-carboxymethoxyuridine methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02057; tRNA_methyltr_CmoM; 1.
DR   InterPro; IPR033664; Cmo5U_methylTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000092250};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057,
KW   ECO:0000313|EMBL:OAZ99090.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092250};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02057,
KW   ECO:0000313|EMBL:OAZ99090.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02057}.
FT   REGION       58     59       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02057}.
FT   BINDING      35     35       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02057}.
FT   BINDING      79     79       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02057}.
FT   BINDING     127    127       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02057}.
SQ   SEQUENCE   269 AA;  30347 MW;  A56AA8013BF69FF9 CRC64;
     MHPHYELTQA GDRYFDGLVD KFSRSLYQAP RGELRLAMLD YLLPQMLNLQ QQAVLDIGGG
     LGQQTAWFAE RGHKVTMAEP SGEMLDHAKN WHRDANELPS DAIEYLQAPL QTIRQHAPGP
     WPLIACHAVL EWLGEPRLAM QTLASLLAPG GQLSLMVFNR DALRFSNAMK GNLQKALSDQ
     LEGQGRGQRL TPISPITHDQ VVQWSGENGL VVESVAGIRV FQDYLRQPAL APRERDTLLA
     LEKCYCRQDP HWRLGRYLLY TLSKPETSE
//
DBGET integrated database retrieval system