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Database: UniProt
Entry: J3CII3_9FLAO
LinkDB: J3CII3_9FLAO
Original site: J3CII3_9FLAO 
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
//
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