SYM1_BACCR
ID SYM1_BACCR Reviewed; 660 AA.
AC Q81JA8;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Methionine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE AltName: Full=Methionyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_01228};
DE Short=MetRS 1 {ECO:0000255|HAMAP-Rule:MF_01228};
GN Name=metG1 {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metG;
GN OrderedLocusNames=BC_0043;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2B subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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; AE016877; AAP07141.1; -; Genomic_DNA.
DR RefSeq; NP_829940.1; NC_004722.1.
DR AlphaFoldDB; Q81JA8; -.
DR SMR; Q81JA8; -.
DR STRING; 226900.BC_0043; -.
DR PRIDE; Q81JA8; -.
DR EnsemblBacteria; AAP07141; AAP07141; BC_0043.
DR KEGG; bce:BC0043; -.
DR PATRIC; fig|226900.8.peg.60; -.
DR HOGENOM; CLU_009710_9_4_9; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000001417; 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; 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; IPR001412; aa-tRNA-synth_I_CS.
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; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
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; PS00178; AA_TRNA_LIGASE_I; 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..660
FT /note="Methionine--tRNA ligase 1"
FT /id="PRO_0000139208"
FT DOMAIN 560..660
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT MOTIF 15..25
FT /note="'HIGH' region"
FT MOTIF 310..314
FT /note="'KMSKS' region"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ SEQUENCE 660 AA; 75203 MW; E87BB62F8268C776 CRC64;
MTEENKSFYI TTPIYYPSGK LHIGHAYTTV AGDAMARYKR MQGYNVHYLT GTDEHGQKIQ
KKAEELNITP QAYVDNIVAG IKELWEKMNI SYDDFIRTTE DRHKDVVEKI FKQLVDQGDI
YLDEYEGWYS VQDETFYTEH QLVDPIMEGD KVVGGKSPDS GHDVELVREE SYFFRMGKYV
DRLLKFYEDN PHFIQPESRK NEMINNFIKP GLEDLAVSRT SFDWGVRVPG NPKHVIYVWV
DALSNYITAL GYGTANEEKY KKFWPADVHL VGKEIVRFHT IYWPIILMAL DLPLPKKVFA
HGWILMKDGK MSKSKGNVVD PVTLIDRYGL DALRYYLLRE VPFGSDGVFT PEGFVERINF
DLANDLGNLL NRTVAMIDKY FSGEIPAFKA NVTEFDETLV AFAQDTLKKV EEAMENMEFS
VALGSIWQLV SRTNKYIDET QPWVLAKDEN DREKLASVMA HLAEVLRQTG IMLMPFLTVA
PSKMFAQLGL TDEAHKSWES LSTIGCIPAG TKVEKGNPIF PRLEMEVEVE YIKEQMKSSA
PKVEEKKEEE PKAEEITIDD FFKVELRVAE VLSAEPVKKA DKLLKIQLDL GTEKRQVVSG
IAKFYSPEDL KGKKVICVTN LKPVKLRGEL SQGMILAGEE NGVLSLASID QNLPNGTKIK
