ID   R0A5G7_9FIRM            Unreviewed;       683 AA.
AC   R0A5G7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   22-APR-2020, entry version 51.
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=HMPREF1085_04500 {ECO:0000313|EMBL:ENZ47321.1};
OS   [Clostridium] bolteae 90A9.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=997894 {ECO:0000313|EMBL:ENZ47321.1, ECO:0000313|Proteomes:UP000013126};
RN   [1] {ECO:0000313|EMBL:ENZ47321.1, ECO:0000313|Proteomes:UP000013126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90A9 {ECO:0000313|EMBL:ENZ47321.1,
RC   ECO:0000313|Proteomes:UP000013126};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium bolteae 90A9.";
RL   Submitted (JAN-2013) 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|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00621504}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01228, ECO:0000256|SAAS:SAAS01159305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01228};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01228};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00621513}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00578164}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2A subfamily. {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:ENZ47321.1}.
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DR   EMBL; AGYH01000016; ENZ47321.1; -; Genomic_DNA.
DR   EnsemblBacteria; ENZ47321; ENZ47321; HMPREF1085_04500.
DR   PATRIC; fig|997894.4.peg.4693; -.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   Proteomes; UP000013126; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159323};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159304};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|SAAS:SAAS00104184};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|RuleBase:RU363039,
KW   ECO:0000256|SAAS:SAAS01159317, ECO:0000313|EMBL:ENZ47321.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01228};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159262};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159279};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|PROSITE-
KW   ProRule:PRU00209, ECO:0000256|SAAS:SAAS00104020};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|PROSITE-
KW   ProRule:PRU00209, ECO:0000256|SAAS:SAAS00469761};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   DOMAIN          582..683
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   REGION          548..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          411..431
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           35..45
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   MOTIF           322..326
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   METAL           150
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   METAL           153
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   METAL           167
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   METAL           170
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   683 AA;  77050 MW;  1210C70D338F9B03 CRC64;
     MNCSAPALCF RSEKEGINHM CQDCKKPYYI TTAIAYASGK PHIGNTYEII LADSIARYKR
     EQGYDVFFQT GTDEHGQKIE EKAEAAGVTP QEFVDKAAAE IKRIWDLMNT SYDKFIRTTD
     QDHEAQVQKI FKKLYDQGDI YKGYYEGLYC TPCESFFTES QLVDGKCPDC GREVKPAKEE
     AYFFRMSKYA PRLIEYINEH PEFIQPVSRK NEMMNNFLLP GLQDLCVSRT TFSWGIPVDF
     DPKHVTYVWL DALTNYITGI GYDCDGSSTD QFKKYWPADL HLIGKDIIRF HTIYWPIFLM
     ALDVPLPKQV FGHPWLLQGD GKMSKSKGNV LYADTLVDFF GVDAVRYFVL HEMPFDNDGV
     ISWELMVERM NSDLANILGN LVNRTISMSN KYFDGVVCDK GVCGEADEDL KKVVLEEVKK
     ADAKMEQLRV ADAMTEIFNI FRRCNKYIDE TTPWTLAKDE SQKDRLATVL YNLTEAIAIG
     ASLLYSFMPE TAEKILAQIH TDKRELSQMD AFGLYPNGQK VTDKPEILFA RMDIKEVLEK
     VEAMHGAEAA DQKQAGGQDG SSDNAEDSGI DLEAKPEITY DDFAKLQFQV GEIIKCEAVP
     KSKKLLCSQV KIGSQVRQIL SGIKAYYSPE EMVGKKVMVV TNLKPAKLAG MVSEGMILCA
     EDAEGSLALM TPEKSMPAGA QIC
//