ID A0A0G0SGN8_9BACT Unreviewed; 480 AA.
AC A0A0G0SGN8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=UU01_C0019G0002 {ECO:0000313|EMBL:KKR61546.1};
OS Parcubacteria group bacterium GW2011_GWA2_40_37.
OC Bacteria.
OX NCBI_TaxID=1618817 {ECO:0000313|EMBL:KKR61546.1, ECO:0000313|Proteomes:UP000034813};
RN [1] {ECO:0000313|EMBL:KKR61546.1, ECO:0000313|Proteomes:UP000034813}
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 -!- 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:KKR61546.1}.
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DR EMBL; LBYZ01000019; KKR61546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0SGN8; -.
DR PATRIC; fig|1618817.3.peg.642; -.
DR Proteomes; UP000034813; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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; 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; 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; 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.
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}.
FT DOMAIN 139..365
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 480 AA; 56171 MW; 8F55399B438C7DD4 CRC64;
MKKDSFYITT TIPYVNAEPH IGFALELTQA DALARYQRLN DREVFFSTGT DEYGQKIWEA
SIKEGKNVQD YVDHYTQKFL ELKGILNLSY DNFIRTTSVG HITAVQEFWR LCNKKGDIYK
KIYRGLYCVG CEKFITEKDL KDGFCPLHPN KKPEIVEEEN YFFRLSKYKK ELLQYLANDK
VIFPEWRRKE AIDFVQNGME DFSISRDKRR FSWGIPIPGD ETQVMYVWFG AFVNYISTLG
WPNSKGLFDK FWVGGERVQI AGKDMVKFQS VMWQGMLLSA GMPTTDKIIY HGFITGEGGI
KMSKSLGNVI NPNDIVKEYG TDALRYFLLR EISSFEDSPF TMERFKDAYN ANLANGLGNL
ISRVMTMAVT YNVNLSKDEL EIKYFDHNSR NYLKDFDINQ CLNEIWSKLK SLDEYIQKKE
PFKNIKINPK EAKQDVHYLL FHLYSHALEL EPFLPETSDK IKKLIRENKK PEKSLFPRKD
//
