ID A0A1F5FTQ9_9BACT Unreviewed; 471 AA.
AC A0A1F5FTQ9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A2572_02235 {ECO:0000313|EMBL:OGD83006.1};
OS Candidatus Collierbacteria bacterium RIFOXYD1_FULL_40_9.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1817731 {ECO:0000313|EMBL:OGD83006.1, ECO:0000313|Proteomes:UP000179237};
RN [1] {ECO:0000313|EMBL:OGD83006.1, ECO:0000313|Proteomes:UP000179237}
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:OGD83006.1}.
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DR EMBL; MFAQ01000032; OGD83006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5FTQ9; -.
DR Proteomes; UP000179237; 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..145
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 150..360
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 471 AA; 54045 MW; 21CAAAA7A9AEE1AA CRC64;
MDKFYITTTL PYVNSDPHIG FAMEIIRADV VARVKRARGN QVWFNTGTDE HGQKIYQKAV
EEGVLPQEYC DRFAEKFKGL KSKLNLSNDT FIRTTDKKHI KAAQDFWTAC FNNGDIYKKN
YQVKYCVGCE LEKTDSDLVD NKCPDHPNYE LELRDEENYF FRFSKYQEKL LDFYKKNPDF
VCPDFRMKEI TNFVESGLSD FSISRLKSKM PWGVEVPGDR GQVMYVWFDA LVNYISVLGW
SSTASAEFGE YWPGVQVCGK DNLRQQSAMW QAMLMSAGLP NTKRIYVNGF ILSDGVKMSK
SLGNVIDPLE WVEKYGTDAV RYFLLSSISS FEDGDATEER FKEVYTAGLV NGLGNLTARV
AAMIEKAETE FEDAVNTPDN EVFRAVEEYN FALAIELIWK KIKTADTIIN EKKAWSLTGV
EQKEVLSELV RIIRQVAVDL DVFLPEMAKK IQNQFGGEKI TKSEHLFARL K
//