ID A0A1T4X319_9BACT Unreviewed; 523 AA.
AC A0A1T4X319;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=SAMN02745166_00972 {ECO:0000313|EMBL:SKA84004.1};
OS Prosthecobacter debontii.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobiaceae; Prosthecobacter.
OX NCBI_TaxID=48467 {ECO:0000313|EMBL:SKA84004.1, ECO:0000313|Proteomes:UP000190774};
RN [1] {ECO:0000313|EMBL:SKA84004.1, ECO:0000313|Proteomes:UP000190774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700200 {ECO:0000313|EMBL:SKA84004.1,
RC ECO:0000313|Proteomes:UP000190774};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUYE01000003; SKA84004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4X319; -.
DR STRING; 48467.SAMN02745166_00972; -.
DR Proteomes; UP000190774; 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; 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; PF19303; Anticodon_3; 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 4..137
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 155..369
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 389..518
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 523 AA; 58829 MW; CF8C49FAD2C2A1E3 CRC64;
MKPYYITTAI DYTNAPPHIG HAYEKVLADV MARFQRLNGR EVYFLTGVDQ HGQKVQKSAD
KAGLTPQAFV DGVTEHFLAL WDKLNVRYDG WAATTDPTHK KVVQAMLQKL HDCGQLYKQA
YTGFYSVRQE QFLTDKERGA DGSFGEEWGE VVELQEENWY FRLSDHVEWL KNYIKTHPDF
IFPTHRASAV LNALEGTPQD LCISRPIERL SWGIPLPFDE RFVNYVWFDA LTNYISFAGY
LADECGNTDL PDFSKLWPSE AHVIGKDILV PAHAVYWPIM LHALGFSDDQ IPRLIVHGWW
NVKGAKMSKS LGNVIDPNVL AGTFTPDGLR YYLMRDIATG YDSDFSDERI IMSYNKELAG
GLGNLLNRSI NMAQKYRSGV LTPGSYDDAE NAALRQTVAE ALPAYLESME GWGIHDGIAA
AWKIVTAANA YVDSTKPFSL AKDPEQAARL DSVLYHLAES WVHISVLLNP IMPTAMATAR
AQIGWEMPEA FQLSDLKWGM LKDGHQLGAP VPLFPRLEIA TAE
//
