ID A0A0G0R6V3_9BACT Unreviewed; 464 AA.
AC A0A0G0R6V3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=UT82_C0027G0008 {ECO:0000313|EMBL:KKR45521.1};
OS Parcubacteria group bacterium GW2011_GWB1_40_14.
OC Bacteria.
OX NCBI_TaxID=1618865 {ECO:0000313|EMBL:KKR45521.1, ECO:0000313|Proteomes:UP000034935};
RN [1] {ECO:0000313|EMBL:KKR45521.1, ECO:0000313|Proteomes:UP000034935}
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:KKR45521.1}.
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DR EMBL; LBYG01000027; KKR45521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0R6V3; -.
DR STRING; 1618865.UT82_C0027G0008; -.
DR PATRIC; fig|1618865.3.peg.909; -.
DR Proteomes; UP000034935; 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; 2.
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 5..135
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 138..361
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 464 AA; 52659 MW; 5E9F58CB30523F89 CRC64;
MSKFYLTTSI AYVNAPPHVG FALELCQGDV IARYRKLLGN DVYYLTGTDE HGQKIAKAAE
ATGKDPAEFV DHISESFRAL TSALNISNND FIRTSDKNKH WPGASEMWRA LSDSGTLYKK
DYNGLYCEGC EAFKALSDLT DGMCSDHKKK PEIIKEENYF FRLSDYQDKL LRLYEEGVIK
IIPEHRQNEV NNFIKQGLED VSFSRPRKDL PWGIPVPGDE DHTIYVWADA LVNYISALGY
GRGDSELFNK FWPADLHIIG KDILRFHAII WPAMLLAAEL LLPKSILVHG HIQSGGQKMS
KSLGNVIDPF ELIDKYGADA VRYFLLKEIP TTQDGDMTKE RMADIYSSEL ANGLGNLVAR
VAAIAEKKFD EITVSNSIFK KNVEAIWKKY TENIENYKFN DALQNVFSLV REGNTYIDRE
KPWEGDNAKN VIPNVVYLII NIGWLLMKQK PHVVKGEALF PRVQ
//
