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Database: UniProt
Entry: A0A117SES5_9FIRM
LinkDB: A0A117SES5_9FIRM
Original site: A0A117SES5_9FIRM 
ID   A0A117SES5_9FIRM        Unreviewed;       660 AA.
AC   A0A117SES5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=APF77_14475 {ECO:0000313|EMBL:KUO67533.1};
OS   Clostridia bacterium BRH_c25.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO67533.1, ECO:0000313|Proteomes:UP000057710};
RN   [1] {ECO:0000313|EMBL:KUO67533.1, ECO:0000313|Proteomes:UP000057710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO67533.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258}.
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:KUO67533.1}.
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DR   EMBL; LOES01000257; KUO67533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117SES5; -.
DR   STRING; 1734399.APF77_14475; -.
DR   Proteomes; UP000057710; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
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|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039}.
FT   DOMAIN          15..249
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          309..458
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   660 AA;  75525 MW;  2C436C905B9C36FC CRC64;
     MIMTENRPIF PKRAVVTAGM PYGNKELHLG HIGGVFIHAD TFARFLRDRI GKENVIFVSG
     TDCYGSPIFE YYRQLTGNGL FQGTIDEFVQ LNHNKQKEVL DSYHVGIDLY AASSFGPAAA
     IHREVSSDFI RELYSKGHLV KLTTSQFYDT ELEVFLNGRQ VVGQCPIAGC TSERGYADEC
     SLGHQYMPTE LISPKSTLTC KQPEMRDVTN WYLKLDSFHE LLTKWVEELK EHPVSRHFVR
     KSILEFLEPP AIYIKRDQLY LVNALDSIPE YTLRDVEKKS SVLLVFDSLE KREKACTILA
     ANSIRYRTGK TLVPFRLTGN IEWGVPAPTL EGTEDLTVWV WPESLWAPIS FTKACLELRR
     KDGDTWRDWW CSKDSKVYQF MGEDNIYFYG PAEMAMFMGM QGGTPSADPP EGELQLPELI
     VNSHILFLDK KASSSGQIKP PMAADLLNYY TSEQLRAHFL GLGLGIRSVG FQPKPLNPMA
     SEKDGDPVLK EGNLLSNALN RAVRSCFYTT QKYYYGKIPV GDISSEILTE SHNTILEFEK
     LLHKCDFHQV MNLMDTYIRS INKYWSKNIR EAEASNDMKF HRQVLIDAFH MVRTAVVLMH
     PIAPAGTKMV LEYLGLGEDF WSWDKIFDPV YAFMINPDEH KLKFLEPRID FFKKHPSQIK
//
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