ID A0A0E3YWJ8_9BACT Unreviewed; 515 AA.
AC A0A0E3YWJ8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=IMCC26134_06825 {ECO:0000313|EMBL:AKC82558.1};
OS Verrucomicrobia bacterium IMCC26134.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1637999 {ECO:0000313|EMBL:AKC82558.1, ECO:0000313|Proteomes:UP000033046};
RN [1] {ECO:0000313|EMBL:AKC82558.1, ECO:0000313|Proteomes:UP000033046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26134 {ECO:0000313|EMBL:AKC82558.1,
RC ECO:0000313|Proteomes:UP000033046};
RA Choi A., Kang I., Cho J.-C.;
RT "Complete genome sequence of Verrucomicrobia strain IMCC26134.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
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DR EMBL; CP011265; AKC82558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3YWJ8; -.
DR STRING; 1637999.IMCC26134_06825; -.
DR KEGG; vba:IMCC26134_06825; -.
DR PATRIC; fig|1637999.3.peg.1493; -.
DR HOGENOM; CLU_009710_9_2_0; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000033046; Chromosome.
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; cd07957; Anticodon_Ia_Met; 1.
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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033046}.
FT DOMAIN 5..136
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 151..356
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 515 AA; 58514 MW; 54AB9DC61C7C9AE7 CRC64;
MKTFYITTAI DYVNGSPHLG HAYEKVLTDV IARFRRLMGD EVYFLTGVDE HGQKVQQSAK
KRGIDPQQFC DEVSEEFRAM CVKLNISNND FIRTTELRHK SVVSRLLQQL FDKGEIYKAE
YQGFYSTRQE QFLQDKDRNP DGSWPEIFGE VTQITESNYF FKLKAYQEWL VQYLKDNDDF
VFPRYRQKQV LEFLAEPLND LCISRPRERL EWGIPLPFDT NYVTYVWFDA LVNYYSAVEG
KPGLWPADFH VIGKDILVPP HAVYWPIMLK ACGLPIPKAL LAHGWWSING SKMSKSTGNF
VDPMGFADQY GVDALRFFMI REMSVGQDSD FSVNQFLVRY NSELANNLGN LVNRTLNMVN
RFAGGKVPAA AAPDAELESE LKTLWAKTRD EFITLSEGFQ FHIALERAFA FVTATNRYVE
QRAPWKLGKS AEAADQALLA TALATMAESL RLAVTLLPAV MPETTEKVYR VIGYAPSGIW
RERLEWGSAL TGASVAETAI LFPRPQAPEA GAAKA
//
