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Database: UniProt
Entry: A0A2V1MYT5_9LACO
LinkDB: A0A2V1MYT5_9LACO
Original site: A0A2V1MYT5_9LACO 
ID   A0A2V1MYT5_9LACO        Unreviewed;       688 AA.
AC   A0A2V1MYT5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=DCM90_09515 {ECO:0000313|EMBL:PWF99334.1};
OS   Levilactobacillus bambusae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=2024736 {ECO:0000313|EMBL:PWF99334.1, ECO:0000313|Proteomes:UP000245080};
RN   [1] {ECO:0000313|EMBL:PWF99334.1, ECO:0000313|Proteomes:UP000245080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS-W1 {ECO:0000313|EMBL:PWF99334.1,
RC   ECO:0000313|Proteomes:UP000245080};
RA   Wang L.-T.;
RT   "Lactobacillus bambusae sp. nov., isolated from a traditional fermented Ma-
RT   bamboo shoots of Taiwan.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWF99334.1}.
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DR   EMBL; QCXQ01000007; PWF99334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1MYT5; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000245080; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245080};
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          586..688
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   688 AA;  77475 MW;  B3CD101BEBACC5E8 CRC64;
     MSDTKSTFYI TTPIYYPSGR LHIGNTYTTV IADAMARYKR SMGADVFFLT GTDEHGEKIE
     KKAESLGQTP KEYVDGMADQ IKDLWKTMAI TYDKFIRTTD ADHVKSVQKI FQKLLDKGDI
     YLGEYEGWYS VDDEEYFTES QLAEVYHDEA GNMVGGKAPS GHEVELVKEE SYFFKMSRYA
     DWLLDYYHSH PNFIQPNTRM NEMINNFIKP GLEDLAISRT SYSWGVPVDS DPKHVVYVWI
     DALSNYITAL GYATDHDEDY QKFWPADVQL VGKEIVRFHT IYWPIMLHAL DLPLPKTVFG
     HGWLLMKNGK MSKSRGNVIY PETLVDRYGL DAVRYYLTKA IPYGNDGVFT PEDFVDRINY
     DLANDLGNLL NRTIAMINKY EGGEVPSFVS GVTNFDADLE NTAAETITNF DHLMDTLHFS
     DALAEIWKLV SRTNKYIDET EPWRLAKSDV LADQQLLDAV MSHLAASLRV IATLISPVMP
     NAPIQIFNQL GLDAATISLA DLKLADFPNG VHTVAKGTPI FPRLDAEEEI DFIAGQMTKS
     TKVKGRAAKA EAEATKAQTV DDWTNFDPEQ TDLVLGEEHK EIRFEAFEKI ELKVAEVLAV
     KKVEGADKLL QFRLDAGDQG NRQILSGIAE WYPNPTELVG KKVIIVANLK PRKMRGNVSQ
     GMLLSAEHDG QVTLITVPDN LVNGSIIA
//
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