ID A0A249E0P5_9GAMM Unreviewed; 863 AA.
AC A0A249E0P5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=BA172_01045 {ECO:0000313|EMBL:ASX27261.1};
OS Candidatus Portiera aleyrodidarum MED (Bemisia tabaci).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Portiera.
OX NCBI_TaxID=1163752 {ECO:0000313|EMBL:ASX27261.1, ECO:0000313|Proteomes:UP000215611};
RN [1] {ECO:0000313|Proteomes:UP000215611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEAM1 {ECO:0000313|Proteomes:UP000215611};
RA Chen W., Hasegawa D.K.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ASX27261.1, ECO:0000313|Proteomes:UP000215611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEAM1 {ECO:0000313|EMBL:ASX27261.1,
RC ECO:0000313|Proteomes:UP000215611};
RA Kaur N., Kliot A., Pinheiro P.V., Luan J., Zheng Y., Liu W., Sun H.,
RA Yang X., Xu Y., Luo Y., Kruse A., Fisher T.W., Nelson D.R., Elimelech M.,
RA MacCoss M., Johnson R., Cohen E., Hunter W.B., Brown J.K., Jander G.,
RA Cilia M., Douglas A.E., Ghanim M., Simmons A.M., Wintermantel W.M.,
RA Ling K.-S., Fei Z.;
RT "The genome of whitefly Bemisia tabaci, a global crop pest, provides novel
RT insights into virus transmission, host adaptation and insecticide
RT resistance.";
RL Submitted (SEP-2017) 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|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP016304; ASX27261.1; -; Genomic_DNA.
DR RefSeq; WP_014895123.1; NZ_CP016304.1.
DR AlphaFoldDB; A0A249E0P5; -.
DR GeneID; 66280087; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000215611; Chromosome.
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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}.
FT DOMAIN 38..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..402
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 608..651
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 701..823
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 617..621
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 99802 MW; 3617D3D805286CCE CRC64;
MMYPFSYKKI ELEAQNFWYN HNCFEIVEIP NKEKFYCLCM FPYPSGNLHI GHVRNYTIGD
VISRSQRMLG KNVLNPIGWD AFGMPAENAA KKNIVSPTDW TNSNIYYMYN QLKSLGFSYN
WDRKITTCKI DFYRWEQWFF IKLIEHGVIY KNNAIINWDP LEKTILANEQ VINGIGWRSG
AKIEHRKIPS WFLKITDYAY ELLRCLANID WPESVKKMQV NWIGKYKGIE VSFKVIGSVP
NCYSYLKVFT QRPDTLFGVT YILLAPDHHL VELAAQYNYQ IKKLCNTFTF CGKCSLATLK
NKELGLYVGY NVLHPITNEI LPLYVSSFRY FEYGATASMG VPAHSHRDWD FANTYGLPFK
TVVSDINGKV PDISKNAYTD FGFIINSGIF NNITCFEAFD YIFYFIKQYK SGVVKQKLKL
RDWGISRQRY WGTPIPVKYG ITGKQTPLTD EEIPVYLPKH GCLNSKFNLK KIPSFYVLGN
GWVRDTETFD TFIESSWYYA RFCCTDNNNS ILDARVNYWL PVDMYIGGIE HAILHLMYAR
FFHKLMRDFG LVDCDEPFKK LITQGMVLTY TYYRESFGIK EWFNPLDVCL LKDKKNGNII
PTVKRDGGIV IRNGIEKMSK SKNNGIDPNV LINRFGADTL RLFVMFSAPT EQVLIWSESG
IIGSSRFIKR LWNIVHTYIY ISGSEHTIIK LSSLRPDQFN LYRQLQKTIK KATSDMIGRH
VFNTVISTVM KLTNLVLHFI DIDSSIIGLA VTREALKSII LILAPIVPHI THVLWKVLGF
SYAVIDAKWP SYNKHCMLGQ LFTVLAQING KIRKEIKLPL NYHTKTFAST ILSSISIKGY
LNCKEIHTLI FVHAKVINIV VSL
//
