SYM_DEIRA
ID SYM_DEIRA Reviewed; 681 AA.
AC Q9RUF3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; OrderedLocusNames=DR_1433;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2B subfamily. {ECO:0000305}.
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DR EMBL; AE000513; AAF11005.1; -; Genomic_DNA.
DR PIR; C75395; C75395.
DR RefSeq; NP_295156.1; NC_001263.1.
DR RefSeq; WP_010888072.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RUF3; -.
DR SMR; Q9RUF3; -.
DR STRING; 243230.DR_1433; -.
DR EnsemblBacteria; AAF11005; AAF11005; DR_1433.
DR KEGG; dra:DR_1433; -.
DR PATRIC; fig|243230.17.peg.1629; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_0; -.
DR InParanoid; Q9RUF3; -.
DR OMA; SDMHGTP; -.
DR OrthoDB; 761140at2; -.
DR Proteomes; UP000002524; Chromosome I.
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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR43326; PTHR43326; 1.
DR Pfam; PF09334; tRNA-synt_1g; 2.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR TIGRFAMs; TIGR00399; metG_C_term; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..681
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139218"
FT DOMAIN 580..681
FT /note="tRNA-binding"
FT REGION 522..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..37
FT /note="'HIGH' region"
FT MOTIF 316..320
FT /note="'KMSKS' region"
FT COMPBIAS 526..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 681 AA; 75270 MW; 99E6E83EE2468C89 CRC64;
MQNPPQHPEA QSPETRDREF FITAAIDYAN GTPHIGHVYE KILADAIARY QRLAGRDVTF
VMGTDEHGEK ISKAAAKGGV TPQELVDDLS ERAFQGLWKK LGISYDFFIR TTSAKHKKYV
QDVLQRVYDA GDIYFAEYEG LYSVGAERYV TEKELVEGPD GVRRFPGDKD PPELRREANY
FFNMQKYQPW LLETLQQNPD LIQPAGYRNE VLEMLKEDIG PLSISRPKAR VPWGIELPWD
TDHVTYVWFD ALLSYLTPLV SQGQDASMSG KAWHVIGKDI LKPHAVFWPT MLRAAGLPLY
RRLVVHSHIL AEDGRKMGKS LGNAIDPEEL VAAWPVDAIR YALLREASLG ADSPFGEGVL
VSRLNSDLAN DLGNLLSRTV SMIQKYRGGV IPAATEPTDR EREIEAAARA LPDEVLRLVD
ELKINMAIDA AMSFVRDLNR YIAESTPWTL AKSPETQGRL DTVLYTAAEG LRVASVALEA
VIPTKAKELR EQLGLGRQGY PLQAAWGLTP AGTRVQGGAI LFPKPEPKAD ETKNAEAKPP
KPQAKKEKKT VTDTAPAKTT EQKPEAAAPA QNDGLISIDD FAKIDLRIAE VVACEAVEKA
DKLLKLTVKL GDETRTVVSG IRKWYEPEAL VGRKVVLVAN LKPAKLRGIE SQGMILAAED
DAGNLDLVGT ELDLPSGTKV R
