ID A0A1F5CAB3_9BACT Unreviewed; 482 AA.
AC A0A1F5CAB3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=A3I30_02145 {ECO:0000313|EMBL:OGD39781.1};
OS Candidatus Azambacteria bacterium RIFCSPLOWO2_02_FULL_44_14.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1797306 {ECO:0000313|EMBL:OGD39781.1, ECO:0000313|Proteomes:UP000177197};
RN [1] {ECO:0000313|EMBL:OGD39781.1, ECO:0000313|Proteomes:UP000177197}
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 -!- 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:OGD39781.1}.
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DR EMBL; MEYV01000018; OGD39781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CAB3; -.
DR Proteomes; UP000177197; 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; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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 PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 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 3..94
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 137..368
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 384..467
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 482 AA; 55198 MW; 696D03D8F460556E CRC64;
MAKFYITTAI DYVNAKPHIG HAIEKIQADV LARFHRQKGD EVWFLTGTDE HGAKIARAAQ
AAGKDPKDFV DDGAGHFKDL KKALNLSWDD FIRTSSQKRH WPGAQKLWLK LFEAGDLYKK
SYKGLYCVGH EAFITEKDLV DGKCRDHQTA PELIEEENWF FRLSKYSDKI KSVIESGELK
IIPESRENEI LSLIRQGLED VSFSRPRKDL SWGIPVPNDP EHTMYVWCDA LTNYITAIGY
GQEQNIEISK YRNFEYWWPA DLHIIGKDIL RFHTAIWPGM LLSAGLPLPK AIFVHGFITV
EGQKMSKTIG NVIDPAELVK KYGTDPVRYY LLREIPAYED GDFSIAKFEE RYSADLVHGL
GNLVARVLAL AKKSDIVEKE AFKKEIKQAK QNSEKLIVEF RFNDALAAIW QLIFIGDKYV
DEKKPWMLKP ESVEFQEIIG SLLHLISEIG KLIEPFLPET SEKIEIQLSG KNPQILFPKI
EN
//
