ID   R0A5G7_9FIRM            Unreviewed;       683 AA.
AC   R0A5G7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   18-JAN-2017, entry version 30.
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.,
RA   Wortman J., 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
CC       but also for the initiation of all mRNA translation through
CC       initiator tRNA(fMet) aminoacylation. {ECO:0000256|HAMAP-
CC       Rule:MF_01228, ECO:0000256|SAAS:SAAS00629317}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC       diphosphate + L-methionyl-tRNA(Met). {ECO:0000256|HAMAP-
CC       Rule:MF_01228, ECO:0000256|SAAS:SAAS00654290}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01228};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01228};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00629338}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00654270}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 2A subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01228}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENZ47321.1}.
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DR   EMBL; AGYH01000016; ENZ47321.1; -; Genomic_DNA.
DR   EnsemblBacteria; ENZ47321; ENZ47321; HMPREF1085_04500.
DR   Proteomes; UP000013126; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
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; 1.
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:SAAS00654294};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654376};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013126};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|SAAS:SAAS00654286};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654316,
KW   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:SAAS00654333};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654288};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|SAAS:SAAS00514389};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|SAAS:SAAS00514462};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   DOMAIN      582    683       TRNA-binding. {ECO:0000259|PROSITE:
FT                                PS50886}.
FT   MOTIF        35     45       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01228}.
FT   MOTIF       322    326       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01228}.
FT   METAL       150    150       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       153    153       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       167    167       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       170    170       Zinc. {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
//