ID A0A366MBW3_9EURY Unreviewed; 994 AA.
AC A0A366MBW3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049,
GN ECO:0000313|EMBL:RBQ22992.1};
GN ORFNames=ALNOE001_12640 {ECO:0000313|EMBL:RBQ22992.1};
OS Methanobrevibacter sp. NOE.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=2006182 {ECO:0000313|EMBL:RBQ22992.1, ECO:0000313|Proteomes:UP000253099};
RN [1] {ECO:0000313|EMBL:RBQ22992.1, ECO:0000313|Proteomes:UP000253099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOE {ECO:0000313|EMBL:RBQ22992.1};
RA Lind A.E., Lewis W.H., Spang A., Guy L., Embley M.T., Ettema T.J.G.;
RT "Genomic insight into two independent archaeal endosymbiosis events.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00049, ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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:RBQ22992.1}.
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DR EMBL; NIZT01000030; RBQ22992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366MBW3; -.
DR Proteomes; UP000253099; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000253099}.
FT DOMAIN 4..684
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 730..882
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 32..42
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 646..650
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 994 AA; 115464 MW; DB27A8E51B7522D7 CRC64;
MEKKWQEKWE KSKLFQADHG EKKKIFLTVA YPYPSGAMHI GHGRTYTVPD VYARFKRMQG
YNVLFPMGWH VTGAPVIGIA SRIKNKDPWT LDLYEKVHKV PKEELPKLAD PEYIVKYFST
EYHNVMSSMG YSIDWRREFK TTDPSYNKFI EWQIRKLKDK GLVRKGNHPV KHCPEDDNPV
GDHDLLEGEG VAVNELTLLK FKIEENNDDL YLVSATFRPE TIYGATNLWL NPDVEYIKVK
SNFDGENSTN GETWIISKDS YYNISNQIKD LEILGDIDPK PLIGANIINP VTQKLHPILP
ASFVDPEYGS GSVFSVPGHA PADYIALQDL KNNKDLIEEY DLKEIVNNVE PLNVVTLKKY
SEIPAKDIIE RLNVQSQEDP KLEEATNELY KVEHSKGIIS EHIPIYAGEK VAVAREHIKK
GMIEKNQATI MYDFAEHPVI CRCGTKCVVK IMDNQWFLEY SDEDWKEETR YLLRNETIVP
SEVRSNLEYY IGWLEGWACS RKIGLGTKLP WDKQWLIEPL TDSTIYMSYY TIAKYLKDMD
PEDLNDAFFE KIFFDNDMDS NKMNKNYELE DGASPDNWEL KVSQDIVNEI QNEFSYWYPL
DWRLSAKDLV GNHLSFHMFH HAAIFPQENW PQGMVVFGMG LLEGNKMSSS KGNVILLNDA
IEEYGADVVR LFLMSSAEPW QDFDWREKEV IGTKRRLEWF FEFAEKIESI KKSPLNLNNI
KRIDLTRRID LWMMNQLYIR INDATTALEG FQTRKTLQDS LFLLKKDVDH YMYRIKHLLD
DPDEAIIFVF SSILESWIRI LAPFTPHSSE ELWNKYGGEG FVSEAKWPIT YQYFPMKCTP
TLNLKTDSCI PSEIIEKSED MVQSIVKDIN EIKKIVEVDP KKIHVYLAPN WKWEIYKIAA
DIGKPDIGQI MGKAIGQNIY DDKKEIADCA KKIGREMTKT RYIGKIDEYD VLSDALDFIS
EEVNSEVIIH KDDSYDPQNK AKNAMPYKPA IFME
//
