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Database: UniProt
Entry: A8T5U3_9VIBR
LinkDB: A8T5U3_9VIBR
Original site: A8T5U3_9VIBR 
ID   A8T5U3_9VIBR            Unreviewed;       263 AA.
AC   A8T5U3;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=AND4_03574 {ECO:0000313|EMBL:EDP59015.1};
OS   Vibrio sp. AND4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP59015.1, ECO:0000313|Proteomes:UP000005159};
RN   [1] {ECO:0000313|EMBL:EDP59015.1, ECO:0000313|Proteomes:UP000005159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AND4 {ECO:0000313|EMBL:EDP59015.1,
RC   ECO:0000313|Proteomes:UP000005159};
RX   PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA   Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA   Milton D.L., Gonzalez J.M., Pinhassi J.;
RT   "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT   starvation.";
RL   PLoS Biol. 8:E1000358-E1000358(2010).
CC   -!- FUNCTION: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U)
CC       to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in
CC       tRNAs. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine
CC         = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:54080, Rhea:RHEA-COMP:13383, Rhea:RHEA-
CC         COMP:13781, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136879,
CC         ChEBI:CHEBI:138053; Evidence={ECO:0000256|HAMAP-Rule:MF_02057};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. CmoM family. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02057}.
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:EDP59015.1}.
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DR   EMBL; ABGR01000006; EDP59015.1; -; Genomic_DNA.
DR   RefSeq; WP_009842742.1; NZ_ABGR01000006.1.
DR   AlphaFoldDB; A8T5U3; -.
DR   OrthoDB; 4697647at2; -.
DR   Proteomes; UP000005159; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0097697; F:tRNA (5-carboxymethoxyuridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_02057; tRNA_methyltr_CmoM; 1.
DR   InterPro; IPR033664; Cmo5U_methylTrfase.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43464:SF96; TRNA 5-CARBOXYMETHOXYURIDINE METHYLTRANSFERASE; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02057};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02057}.
FT   DOMAIN          52..148
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
FT   BINDING         27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT   BINDING         55..56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT   BINDING         122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
SQ   SEQUENCE   263 AA;  30042 MW;  64979B141BF8BC84 CRC64;
     MTEDRNFDDI AHKFAKNIYG SDKGEIRQII VWEDFLQILS ELDADHQALQ VLDAGGGLAQ
     MSQKLAELGH HVALCDLSSE MLQLAKLDIE KNGLLEQYRL IHSPVQSIGD FMEEQVDLVM
     FHAVMEWLVD PKAALDTVLE QVKPGGIASV MFYNHHGLVY KNVVCGNIPH VLDGMPHRKR
     FKLQPQKGLK PEEVYQWIED SGFSICGKSG IRSFSDYIGN MEYMGDYEFE DVLALEKQLC
     RQEPYLSLGR YIHVWAKKND KQE
//
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