ID A0A0S7WZ10_9BACT Unreviewed; 464 AA.
AC A0A0S7WZ10;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=AMJ47_00825 {ECO:0000313|EMBL:KPJ55393.1};
OS Parcubacteria bacterium DG_72.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703764 {ECO:0000313|EMBL:KPJ55393.1, ECO:0000313|Proteomes:UP000051392};
RN [1] {ECO:0000313|EMBL:KPJ55393.1, ECO:0000313|Proteomes:UP000051392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_72 {ECO:0000313|EMBL:KPJ55393.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ55393.1}.
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DR EMBL; LJND01000001; KPJ55393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7WZ10; -.
DR STRING; 1703764.AMJ47_00825; -.
DR PATRIC; fig|1703764.3.peg.696; -.
DR Proteomes; UP000051392; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 124..356
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 374..453
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 371..398
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 464 AA; 53338 MW; 0D8F413DCB761F7B CRC64;
MDKFYITTSI PYANAVPHIG FALEVVQADV LARYHKSLGE NVFYLTGTDE HGLKIKKAAQ
EVNKSPQEFV DEISVRFKEL TKSLNICNDD FIRTTEERHK LAVEKLWEKI KADIYKKKYK
GYYCSGCEAF VTGKDLVNNK CLIHKKEPEF VEEENYFFKL SNYLDEIKEK IESNEIRIIP
ETRKNEVLGY IKTGIKDISF SRVKDKYWGF EVPGDNSQII YVWGDALPNY ISAIGYEKET
KQFKSLWPAD VHCIGKDILK FHALLWPAML LAAGLALPKA IFVHGFITVA GQKMSKSLGN
VVDPFELVAR YGPDAVRYYL LREIPSTEDG DFTVEKFEQR YNADLASGIG NLVARVSKMA
ENIDKGSGIN NPGIEKEIQK AQKNCKKYLE EFKFSEALRA IWELISFCDK YIEKEKPWEQ
KENSKNVLND LLFAVDNIAD LLDPFLPETS EKIRKRIIPL FPRI
//
