ID A0A1F7VC85_9BACT Unreviewed; 476 AA.
AC A0A1F7VC85;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=A3I41_02900 {ECO:0000313|EMBL:OGL88031.1};
OS Candidatus Uhrbacteria bacterium RIFCSPLOWO2_02_FULL_48_18.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802408 {ECO:0000313|EMBL:OGL88031.1, ECO:0000313|Proteomes:UP000176593};
RN [1] {ECO:0000313|EMBL:OGL88031.1, ECO:0000313|Proteomes:UP000176593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGL88031.1}.
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DR EMBL; MGEQ01000002; OGL88031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7VC85; -.
DR Proteomes; UP000176593; 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; IPR041872; Anticodon_Met.
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; PF19303; Anticodon_3; 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 137..358
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 382..458
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 476 AA; 54719 MW; 8D9992C32EAD7576 CRC64;
MPNKYYITTT LPYVNAKPHI GFALEIVQAD MIARYRRMLG DEVIFNTGTD EHGQKIYEKA
IAEGKELQAY TDEYAAQFDD LKASLNLSYD HFIRTTNPSH KAAAQEFWKR CLANDDIYKK
QYQVKYCVGC ELEKTNSELV NEKCPVHPNL DLQFIDEENY FFRFSKYQQP LLDLYASRPD
FVMPDFRLHE IKNFVEGGLN DFSISRLKEK MPWGVPVPDD DSQVMYVWFD ALVNYISTLG
WPDTSREFSF WPGVQVAGKD NLRQQSAMWQ AMLMSAGIEP SHQIFIHGFI TANGQKMSKS
LGNVVDPFEE VKEYGTDAIR YYLLREIPPG DDGDFSRPRL EERYAELANR LGNLVGRVAA
MTQKYFAGDV GTFVFEHTSV EKELEVHMNN YNFKAYIDRV FAIVDDANEL IDKKAPFKLI
KEDEAAAKAV LAEASEMIRF VARSLACVIP KTSEEILRRY GTIIEIGDPL FPRRDA
//
