ID A0A2A2ISN2_9PSED Unreviewed; 249 AA.
AC A0A2A2ISN2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CK486_17080 {ECO:0000313|EMBL:PAV46698.1};
OS Pseudomonas sp. HAR-UPW-AIA-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1985301 {ECO:0000313|EMBL:PAV46698.1, ECO:0000313|Proteomes:UP000243299};
RN [1] {ECO:0000313|Proteomes:UP000243299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAR-UPW-AIA-41 {ECO:0000313|Proteomes:UP000243299};
RA Kumari P., Krishnamurthi S.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PAV46698.1}.
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; NSLB01000016; PAV46698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2ISN2; -.
DR OrthoDB; 4697647at2; -.
DR Proteomes; UP000243299; Unassembled WGS sequence.
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; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43464:SF96; TRNA 5-CARBOXYMETHOXYURIDINE METHYLTRANSFERASE; 1.
DR Pfam; PF13489; Methyltransf_23; 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 ECO:0000313|EMBL:PAV46698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243299};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02057, ECO:0000313|EMBL:PAV46698.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02057}.
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 49..50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
SQ SEQUENCE 249 AA; 28180 MW; 4F08F89C89E888C2 CRC64;
MSDRHFDELA TRFAEKIYGG AKGAIRLAVL QADLKEALPE RPLRVLDIGG GLGHMSLWLA
EHGHQVTFSE PAAPMLEGAR ARFAEAGQQA SFIQAPWQDL LGQLDDPFDL VLCHAVLEWL
AEPHAILPVL HQLTAPGGWL SLAFYNKDAL IYRNLLKGHF RKLRKERFAG EGQSLTPQRP
LDPRELALQL TPHWTVEQQS GVRVFHDYMP QEFQAKAELT DLLEMELAYR RHPGFAGLGR
YLHWICRPL
//
