ID A0A143DF39_9PROT Unreviewed; 519 AA.
AC A0A143DF39;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN Name=metG {ECO:0000256|HAMAP-Rule:MF_01228};
GN ORFNames=AY555_08465 {ECO:0000313|EMBL:AMW35199.1};
OS Haematospirillum jordaniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Haematospirillum.
OX NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW35199.1, ECO:0000313|Proteomes:UP000076066};
RN [1] {ECO:0000313|EMBL:AMW35199.1, ECO:0000313|Proteomes:UP000076066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5569 {ECO:0000313|EMBL:AMW35199.1,
RC ECO:0000313|Proteomes:UP000076066};
RA Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.;
RT "Complete Genome of H5569, the type strain of the newly described species
RT Haematospirillium jordaniae.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC also for the initiation of all mRNA translation through initiator
CC tRNA(fMet) aminoacylation. {ECO:0000256|ARBA:ARBA00003314,
CC ECO:0000256|HAMAP-Rule:MF_01228}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2B subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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DR EMBL; CP014525; AMW35199.1; -; Genomic_DNA.
DR RefSeq; WP_066135570.1; NZ_JAAVTE010000001.1.
DR AlphaFoldDB; A0A143DF39; -.
DR STRING; 1549855.AY555_08465; -.
DR GeneID; 53317187; -.
DR KEGG; hjo:AY555_08465; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000076066; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_01228};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01228}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000076066}.
FT DOMAIN 7..366
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 377..516
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT MOTIF 14..24
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 302..306
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 519 AA; 59086 MW; 7544F814AC746476 CRC64;
MTGSRSYYVT TPIYYVNDRP HIGHAYTTLA CDVLARFKRL DGYRVMFLTG TDEHGQKVEK
SAHAKGIDPQ VFTDEVSQNF RDLASVMKYS HDDFIRTTEP RHKAACAALW KRLVDRGDIY
AGKYAGWYAV RDEAFYAESE LQTAPDGTRI APTGAPVEWV EEPSYFFRLS AWQDKLLRFY
DEHPDFIAPE SRRNEVISFV QGGLQDLSVS RTTFRWGVPV PGDSEHIMYV WLDALTNYLT
ATGYPDTGHE RYKAFWPADL HMVGKDILRF HAVYWPAFLM AADLPLPKRV FAHGWWTNEG
QKISKSLGNV IDPYELVGTF GLDQTRYFLL REVPFGNDGV FSRQAFVRRM NTELANDLGN
LVQRTLSMIA KNCSGKVPEV GVLEDSDRHM LDSAYSLLDV LREQLDRQAF HEALESIWVV
VRAANAYVDH QAPWSLRKTD PKRMETVLWV LAESIRQVAL LMQAFVPDGA GRILDQLGLG
QEQRGFDTFG PRFALVTGSD LPAPQGIFPR YAEEEVVRS
//
