ID K4PKN2_9GAMM Unreviewed; 201 AA.
AC K4PKN2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
DE Flags: Fragment;
GN Name=metG {ECO:0000313|EMBL:AFV66697.1};
OS Aeromonas sp. REm-amp_20.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1246257 {ECO:0000313|EMBL:AFV66697.1};
RN [1] {ECO:0000313|EMBL:AFV66697.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=REm-amp_20 {ECO:0000313|EMBL:AFV66697.1};
RX PubMed=23204414; DOI=10.1128/AEM.03171-12;
RA Voolaid V., Tenson T., Kisand V.;
RT "Aeromonas and Pseudomonas Species Carriers of ampC FOX Genes in Aquatic
RT Environments.";
RL Appl. Environ. Microbiol. 79:1055-1057(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
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DR EMBL; JX899533; AFV66697.1; -; Genomic_DNA.
DR AlphaFoldDB; K4PKN2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039}.
FT DOMAIN 1..193
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFV66697.1"
FT NON_TER 201
FT /evidence="ECO:0000313|EMBL:AFV66697.1"
SQ SEQUENCE 201 AA; 22605 MW; 850C15F82A280D1D CRC64;
YANGSIHLGH MLEHIQADIW VRYQRMRGHQ VHFICADDAH GTPIMLKAQQ MGITPEEMIA
AVSKEHQTDF AGFNISFDNY HSTHSNENRE LAELIYGRLK AGGFIKGRTI TQLFDPEKSM
FLPDRFVKGT CPKCKSPEQY GDNCDSCGAT YSPTELIDPK SAVSGATPVM KDSEHFFFDL
PQFETWLAGW VRGSGAIQEE M
//