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Database: UniProt
Entry: A0A023WZM1_9ACTN
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ID   A0A023WZM1_9ACTN        Unreviewed;       578 AA.
AC   A0A023WZM1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   13-SEP-2023, entry version 49.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098};
DE            EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098};
DE            Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098};
GN   Name=metG {ECO:0000256|HAMAP-Rule:MF_00098};
GN   ORFNames=RradSPS_0379 {ECO:0000313|EMBL:AHY45662.1};
OS   Rubrobacter radiotolerans.
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY45662.1, ECO:0000313|Proteomes:UP000025229};
RN   [1] {ECO:0000313|EMBL:AHY45662.1, ECO:0000313|Proteomes:UP000025229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY45662.1,
RC   ECO:0000313|Proteomes:UP000025229};
RA   Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA   da Costa M.M.S.;
RT   "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT   RSPS-4.";
RL   Submitted (MAR-2014) 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_00098}.
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_00098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00098};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258,
CC       ECO:0000256|HAMAP-Rule:MF_00098}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00098}.
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DR   EMBL; CP007514; AHY45662.1; -; Genomic_DNA.
DR   RefSeq; WP_051589231.1; NZ_CP007514.1.
DR   AlphaFoldDB; A0A023WZM1; -.
DR   STRING; 42256.RradSPS_0379; -.
DR   KEGG; rrd:RradSPS_0379; -.
DR   PATRIC; fig|42256.3.peg.383; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_1_2_11; -.
DR   Proteomes; UP000025229; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; 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   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00098};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00098}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00098};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00098}; Reference proteome {ECO:0000313|Proteomes:UP000025229};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   DOMAIN          16..421
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          441..533
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   578 AA;  65569 MW;  343CDA58D6370680 CRC64;
     MSEPFAGGTE EKTGRYLVTS ALPYANGPLH VGQIVGAYLP ADIFVRYLRM RGEDVVYICG
     TDEHGVPITL TAEREGKSAQ EVVDYWYAHM KETFERFGIS FDNFSRTSRP VHAENTQAFY
     RKLKAGGYIS EAASKQMYSP TEDRFLPDRY VEGTCPFCGY REARGDQCDN CGNWYEAYEL
     IEPHSKVTGG AVEVRETTHL YLDLSQFSER LKSWISSQEH WRSAVKNFIL GTINSGLEKR
     PITRDISWGV PVPEPGFEEK RFYVWFDAPI GYVSSTMEWA ERIGEPDRWR EYWQEPDTKM
     IHFIGKDNTV FHTIIWPAML MGVAEGSDEP YILPYDVPAN EFMNLEVAVG DERRAMQMST
     SRNLAVWLHE ALERFPADPL RFYLASTLPE TGDVNFSWRE FQARVNGDLI GNLGNYANRV
     LSFTNKYFGG ELRRPDDLPK EARAVLADFA EIEAAYDRKM LDERPREALA ELLALGKRAN
     RYFDAAAPWK SRKEDPARTE ADLYVCCALL GSIGYHASPY VPEAMEDLAK FFDGPLAPTS
     GLPLPDAYRT NGAKPLFARI EDAEVEAADR QLTEAVTG
//
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