ID J3CII3_9FLAO Unreviewed; 943 AA.
AC J3CII3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=PMI13_02112 {ECO:0000313|EMBL:EJL72121.1};
OS Chryseobacterium populi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1144316 {ECO:0000313|EMBL:EJL72121.1, ECO:0000313|Proteomes:UP000007509};
RN [1] {ECO:0000313|EMBL:EJL72121.1, ECO:0000313|Proteomes:UP000007509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF314 {ECO:0000313|EMBL:EJL72121.1,
RC ECO:0000313|Proteomes:UP000007509};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL72121.1}.
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DR EMBL; AKJY01000034; EJL72121.1; -; Genomic_DNA.
DR RefSeq; WP_007843360.1; NZ_AKJY01000034.1.
DR AlphaFoldDB; J3CII3; -.
DR PATRIC; fig|1144316.3.peg.2124; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000007509; 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 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; 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-RELATED; 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..144
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 278..462
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 711..744
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 795..905
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 718..722
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 943 AA; 108638 MW; 731FE80B862BC431 CRC64;
MFYDHQQIEK KWQKYWEENQ TYKTSDAPDK PKFYVLDMFP YPSGAGLHVG HPLGYIASDI
YARYKRHQGF NVLHPVGYDS FGLPAEQYAI QTGQHPAITT EQNINRYEEQ LRKIGFSFDW
SREVRTSDAS YYKWTQWIFI QLFHSWYNKN TDKAESIETL IQHFKEKGTE DLNANQNDEL
RFTAEEWNNA SDIDKEDILL NYRLSYRAET TVNWCPALGT VLANDEVKDG KSERGGFPVF
QKKMMQWSMR ISAYSERLLQ GLATLDWPQP LKDSQEYWIG KSQGAQVKFI IDGLKAKEGT
DNFVEVFTTR PDTIFGATFM VLAPENPLVE TITTAVQKAE VDHYIEETSK KTERDRMADV
KNVSGAFTGS YAINPFSNEK MPIYISDYVL MGYGTGAVMA VPAHDERDHR FAKKFNLEIK
KVVETDEDVQ EKSFDSKTSV CVNSDFLNGL NYDEAKALII TAIEKKGIGH GTTNYRQRDA
IFSRQRYWGE PVPIYYKDGM PYTLPDSALP LELPEVEKYL PTEDGDPPLG NAKVFAWDEA
NQKVVSTDLI DDKTIFPLEL STMPGWAGSS WYFLRYMDPN DEEVFAKKEL TDYWGQVDLY
IGGSEHATGH LLYSRFWNMF LKDRGFINHD EPFQKLINQG MILGMSAFVY RIDGTNQYVS
KNLANDYKTQ KIHVDVSLLK GASDELDTEA FIQWRPDYAD AEFILEDGKY ITEREVEKMS
KSKYNVVNPD DICEEYGADG LRLYEMFLGP LEQSKPWNTQ GLSGVYGFLK KFWNLYFNGD
VFEVSDDEPT KAEYKVLHTL IKKVVFDIEN FSFNTSVSSF MIAVNELQKI KCNKRNILEP
LAVIISPYAP HICEELWSLL GHNSSIEFEK FPVLNEDYLV EDEIEYPVSV NGKMKFKLSL
SAQFSAKEVE DLVIQDQKVL QVLEGKTPKK IIVVHHRIVN IVI
//