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Database: UniProt
Entry: A0A011UX23_RUMAL
LinkDB: A0A011UX23_RUMAL
Original site: A0A011UX23_RUMAL 
ID   A0A011UX23_RUMAL        Unreviewed;       669 AA.
AC   A0A011UX23;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=RASY3_15635 {ECO:0000313|EMBL:EXM37762.1};
OS   Ruminococcus albus SY3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM37762.1, ECO:0000313|Proteomes:UP000021369};
RN   [1] {ECO:0000313|EMBL:EXM37762.1, ECO:0000313|Proteomes:UP000021369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY3 {ECO:0000313|EMBL:EXM37762.1,
RC   ECO:0000313|Proteomes:UP000021369};
RA   Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA   Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six Ruminococcal strains.";
RL   Submitted (JUN-2013) 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:EXM37762.1}.
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DR   EMBL; JEOB01000004; EXM37762.1; -; Genomic_DNA.
DR   RefSeq; WP_051506636.1; NZ_JEOB01000004.1.
DR   AlphaFoldDB; A0A011UX23; -.
DR   PATRIC; fig|1341156.4.peg.2726; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000021369; Unassembled WGS sequence.
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; 3.40.50.620; HUPs; 2.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR029038; MetRS_Zn.
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.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021369}.
FT   DOMAIN          23..257
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          313..470
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   669 AA;  76707 MW;  D824229DE7A0B884 CRC64;
     MAKNKEGGKP FEIPRPEFPK RAVITGGMPY GNKELHFGHV GGMFVFADAY ARFLRDRIGK
     DNVLFVGGTD CYGSPIAEGW RKKVADGEFE GSLTDFVQRN HDKQQKTLDD YGISPDIFAA
     SGLGRSKEIH AEVTDWFISS LYKKGQLNKI STMQFYDEKA GCFLNGRQVI GKCPIEGCTS
     EKGYADECDL GHQYMPENLI DPVSTLTGEK PSMRPVTNWY FKLRDYEELL KNWIEMLKKR
     KDVRPVVCKT IEEFLKPPVI YIKREFEEKY LSLKDQMPEH EYFEEPKKPS FTVQFRTLSD
     CDEAVKVLVN NGIRYRTGKT LVPFRLTGNI EWGVPAPVMD NVEGLTVWVW PESLWAPISF
     TQTLLEQRGR SRDEWKDYWC SKDSGVYQFI GQDNIYFYGI AEPAMWMAQQ ESDVKTADPA
     EGEMQMPTII ANHHILFLDK KASSSGAVKP PMADDLLNFY TPEQLRMHWL GLGLGQRSVS
     FMPKPYNPDA KPDDADPVVK DGLLLSNVYN RMVRTAFYTT QKHFNGIMPS NTPSENILAE
     GKKAVLDYER HMSKFAFHQC TYVLDSYIRN GSKYMAKTIK EDTPAEELSQ ALADLFYMIK
     IAAVLLHPLA PFGTEKVREY LQVGEEMWSW DNIFEPLTFF VGEGHELKFL PPRTDFFTRH
     ESQFETAEK
//
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