ID A0A1F6BL65_9BACT Unreviewed; 538 AA.
AC A0A1F6BL65;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
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=A2110_00205 {ECO:0000313|EMBL:OGG37593.1};
OS Candidatus Jorgensenbacteria bacterium GWA1_54_12.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1798468 {ECO:0000313|EMBL:OGG37593.1, ECO:0000313|Proteomes:UP000176273};
RN [1] {ECO:0000313|EMBL:OGG37593.1, ECO:0000313|Proteomes:UP000176273}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258}.
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:OGG37593.1}.
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DR EMBL; MFKH01000007; OGG37593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6BL65; -.
DR STRING; 1798468.A2110_00205; -.
DR Proteomes; UP000176273; 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: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; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 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; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 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 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..399
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 415..536
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 538 AA; 62172 MW; F829CFE2081B8464 CRC64;
MQKIFVGVAW PYVNGHLHVG HLAGYLLPAD IFARFCRLRG ADILMVSGSD CFGTPITTEA
DKRGITPQEV VNEYYPEHVK LFEEAGIRFD IFTKTMTENH IRLAQDFFLA FLKNGYLFKK
RTKQYYDPSA QRFLPDRYVE GTCPSCGAER ARGDQCDECG RVFEAGELVN PVSALSGAPV
ELKESEHYFF DLKKLQPFIE RYVEGRGENW KEWVRNETDA WLARGLVARA FSRDLEWGVP
FPIDKIPKAE RIEGIEHKRF YVWWEALMGY YTASRERDDW KEWWYNRDAE HYYFMGKDNL
PFHTMFWPAE LHAYDEELHL PDVISVNQFL TLDGKQFSKS RGVTVDSREL IARYGADAVR
FYLTYIMPEY ADTSFSWGDF AERVNSVLIG NLGNFLNRAL TLAKDQTFNA RDVGADVSAA
VAEKCRAARE ALEKPEFRTY LDAVLMLSDF GNKYVAREEP WKRDGNKRDA AVTNACYIAL
ALQLLIQPLL PHASERLAEM TGVRFNSWDD DVSRQVLDAL ERMKARNPEP LFQKIEIE
//
