ID A0A0G0CZH7_9BACT Unreviewed; 447 AA.
AC A0A0G0CZH7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00018753};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=UR91_C0049G0004 {ECO:0000313|EMBL:KKP87419.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWC2_35_8.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618752 {ECO:0000313|EMBL:KKP87419.1, ECO:0000313|Proteomes:UP000034798};
RN [1] {ECO:0000313|EMBL:KKP87419.1, ECO:0000313|Proteomes:UP000034798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
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:KKP87419.1}.
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DR EMBL; LBQZ01000049; KKP87419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0CZH7; -.
DR PATRIC; fig|1618752.3.peg.623; -.
DR Proteomes; UP000034798; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 14..127
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT DOMAIN 135..369
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 447 AA; 52000 MW; BCCEAD2E46077576 CRC64;
MTKKNSFYIT TTLPYVNADL HLGHALEFVR ADAIARYKKL IGFDVFFNTG TDEHGMKIFE
VAKKNGKNPQ EFVDESFLKF KDSVKIFGMD EEILHFVRTT DEYHIKSAQE FWKRVNDNGY
IYKKNYEAKY CVGCEETKSD SELVNGECML HTGKKLEIIA EENYFFKYSE FRDKLLKFYK
NNPNFVVPDF RFNEIKAFVE RGLQDFSISR LKSKMPWGIE MPGDSGHVMY VWFDALTNYV
STLGWPENKE QFEKFWVNGN PTQYCGKDNN RFQSAMWQAM LMAADLPNSK QIIINGFITA
GEGIKMSKTL GNVADPKEIV KEYGTDALRY FLLREVSSFE DSPFTMERFK DAYNANLANG
LGNLVSRVMK MAETNLKKSV EIPENTIRED YKNAFEKFDL QEVTNIIWKE IGELDKKIQE
TKPFSLIKTD KIKAVEIIKE CQKLQKK
//
