ID D2EJY7_PEDAC Unreviewed; 675 AA.
AC D2EJY7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 76.
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 ECO:0000313|EMBL:EFA26809.1};
GN ORFNames=HMPREF9024_01099 {ECO:0000313|EMBL:EFA26809.1};
OS Pediococcus acidilactici 7_4.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=563194 {ECO:0000313|EMBL:EFA26809.1, ECO:0000313|Proteomes:UP000005738};
RN [1] {ECO:0000313|EMBL:EFA26809.1, ECO:0000313|Proteomes:UP000005738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_4 {ECO:0000313|EMBL:EFA26809.1,
RC ECO:0000313|Proteomes:UP000005738};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., McDonald J., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Pediococcus acidilactici strain 7_4.";
RL Submitted (OCT-2009) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001234, ECO:0000256|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00005328,
CC 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; GG730085; EFA26809.1; -; Genomic_DNA.
DR AlphaFoldDB; D2EJY7; -.
DR HOGENOM; CLU_009710_9_4_9; -.
DR Proteomes; UP000005738; Unassembled WGS sequence.
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:0000049; F:tRNA binding; 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 CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00398; metG; 1.
DR NCBIfam; TIGR00399; metG_C_term; 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 Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 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};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01228}.
FT DOMAIN 573..675
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT MOTIF 15..25
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 310..314
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 675 AA; 76690 MW; 25BB3EFAA7ADBABA CRC64;
MMAENNTYYI TTPIYYPSGK LHIGNSYTTI ACDAEARFQR LQGKDVFFLT GTDEHGLKIE
QKAEALHTTP QAYVDDMAKG IKELWKLLEI SNDKFIRTTD EAHEKSVQYI FQKLLDQGDI
YLGEYEGWYS VSDEEYFTES QLAEVYRDEN GKVIGGKAPS GNEVELVKEE SYFFKMSKYA
DWLLDYYEKH PDFIQPASRM HEMINNFIKP GLEDLAVTRT SFKWGVPVKN DPKHVIYVWI
DALSNYITAL GYGSDDDSLF KRYWPANVHM VGKEIVRFHT IYWPIMLHAL GLEMPKQIYG
HGWLLMKDDK MSKSKGNVIY PETIVEKYGL DALRYYLLKA MPYSNDGNFT PEDFVSKINF
DLANDLGNLL NRTVAMINKY EGGVIPTFQS GVNEVDADLE KVAAETIKNY QELMESMHFS
DALAEVWKLV SRSNKYIDET TPWILARNDD EESKQKLASV MNHLAESLRI IAILIQPVMT
QSPAKIFGQL GLDPATMELQ GLHFGEIPAG TKVVEKGTPI FPRLDIEKEA AFLKGQMTQS
DKKKGRAAMA EANQAKATEE NVNEAKKEIR IEAFDKVELR VAEILEAGHV EGADRLLKFK
LDAGDEEPRQ ILSGIAQWYP NPEELVGKKV VIVANLKPRK MRGEISQGMI LSTERDGQVN
VVMVDEKHEN GDVLG
//