ID A0A150AGA4_9BACT Unreviewed; 924 AA.
AC A0A150AGA4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AVL50_18400 {ECO:0000313|EMBL:KXX68807.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX68807.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX68807.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX68807.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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}.
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:KXX68807.1}.
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DR EMBL; LQAQ01000091; KXX68807.1; -; Genomic_DNA.
DR RefSeq; WP_062618300.1; NZ_LQAQ01000091.1.
DR AlphaFoldDB; A0A150AGA4; -.
DR STRING; 1775430.AVL50_18400; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000075267; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
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; 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000075267}.
FT DOMAIN 12..145
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 278..458
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 696..723
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 774..886
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 697..701
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 924 AA; 105949 MW; DAC6F6AC5AEE5879 CRC64;
MSEYNHNSFE PKWQKYWQDN NIYKVDIDKS KPKYYTLDMF PYPSGAGLHV GHPMGYIASD
IVSRYKRLKG FNVLHPMGFD SFGLPAEQYA IETGQHPAIT TEQNISTFKS QMNKIGFSFD
WSREVQTSSP EYYRWTQWIF EQLFNAYYDK DENKAKDIAE LVKHFEANGS EGINAECDDD
ATVFTAEDWK GYSDNEKATI LLQYRLTFLS EAMVNWCPAL GTVLANDEVK DGVSERGGHP
VERKKMKQWM MRITAYADRL LGNLDRLDWS DALKEMQRNW IGKSIGCELD FKVADSDITL
TAFTTRVDTV YGVTYVVLAP EHELIPTLTT DAQKEAVETY VEEAKNRSER DRQSDVKTVS
GVFTGSYVIN PLTGEKVQLW IADYVLSGYG TGVVMAVPSS DDRDFRFANH FDLPIIRVIE
GTEDMEDPTQ VKKGKMINSG FLNGLDSDEA IKVAIDKLVE SGQGKAKVNF RIRDAVFSRQ
RYWGEPVPVY FDENDSPQLV PDQQLPLNLP EVENYLPTPE GDPPLGNAKD WKFDDKFGYE
LTTMPGWAGS SWYFLRYMDP QNKEAFVSKE AVEYWNQVDL YVGGTEHATG HLLYSRFWNM
FLFDMGFIGH EEPFQRIVNQ GMIQGRSNFV YRVKGTNQFV SYGLRKDYDV QPLYVDVNIV
NNDELDTEKF KEWRKDYADA EFILEDGKYM CGHVVEKMSK SKYNVVNPDV VIEKYGADTL
RLYEMFLGPI EQSKPWSMQG IDGVWKFLRK MWRLFYNDQG QLVVTDGKAT PEELKILHKT
IKKAGEDMES LSLNTTVPAF MVCVNELAAA KCHKKEVLEQ LLVILSPFAP HIAEELWHEA
LGHEDSVILA SFPEFDASLL VEASHTYPVS INGKMRVKID LPMDISQEEA KEAVFANEVV
KKWVEDKPIK KFIFVPKRIV NVVV
//
