ID A4YUL8_BRASO Unreviewed; 705 AA.
AC A4YUL8;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 115.
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 OrderedLocusNames=BRADO3829 {ECO:0000313|EMBL:CAL77594.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL77594.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL77594.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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|ARBA:ARBA00004496,
CC 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; CU234118; CAL77594.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YUL8; -.
DR STRING; 114615.BRADO3829; -.
DR KEGG; bra:BRADO3829; -.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_3_5; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000001994; 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; IPR001412; aa-tRNA-synth_I_CS.
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; PS00178; AA_TRNA_LIGASE_I; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000001994}.
FT DOMAIN 196..553
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 565..697
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 203..213
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 490..494
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT COMPBIAS 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 76417 MW; 9E94D88177EB5CD7 CRC64;
MAKASKTTVK KGKPATKGAA TKAAAKKASK SPAKAKAGAT KAKAAADKDK KAKAAKANAA
KAKATKGKAS SAPAKGKSPK AAKKAAKSAT KPAVPAKKTA AKAAATKPAP SKKPAETKPA
PAPKLVAPAV AESPKPPPRA AKPKTPRKRK VEAAAAPEIE IAEIEVAEVE IVEIEATDTA
EDATPVAAAT ENANTFYVTT AIAYPNGSPH IGHAYEAIAT DAIARFARLD GKDVFFLTGT
DEHGLKMVQT AQNEGLTPSE LAARNAGRFR EMDERLNVSF DRFIRTTEPA HHKSVQAIWT
RMLENGDIYA DTYSGWYSVR DEAYYAEEET VVGEDNVRRG PQGTPVEWVE EKSYFFRLSA
YQDKLLALYE NQPDFIGPDA RRNEITSFVR GGLKDLSISR TTFDWGVRVP HDDEHVMYVW
VDALTNYITG VGFPDENDAN WKFWPADVHV IGKDIIRFHA VYWPAFLMSA GVPVPKRVYA
HGFLFNRGEK MSKSVGNVVD PFNLADQYGV DQLRYFFLRE VPFGQDGNYN HEAIVARINA
DLANDLGNLA QRSLSMITKQ FGGVLPEPGE FSANDQAILA EADAMIGAAR KAMATQQIHQ
WLNAVWSVVA EANRYFAGEA PWALAKTDPK RQHTVLYVTA EVIRQVAILT QPVMPAASAK
LLDSLGIPED ERSFARLGGE VRIAPGTQLP APQAVFPRYI EPSAA
//
