ID F9YT77_CAPCC Unreviewed; 452 AA.
AC F9YT77;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN OrderedLocusNames=Ccan_18800 {ECO:0000313|EMBL:AEK23996.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23996.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK23996.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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DR EMBL; CP002113; AEK23996.1; -; Genomic_DNA.
DR AlphaFoldDB; F9YT77; -.
DR STRING; 860228.Ccan_18800; -.
DR KEGG; ccm:Ccan_18800; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_6_2_10; -.
DR OMA; KATHECA; -.
DR Proteomes; UP000008895; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
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 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 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEK23996.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895}.
FT DOMAIN 221..253
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 305..417
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 452 AA; 51566 MW; 369DE05683214BCA CRC64;
MPVYYKNGVP YTLPLSALPL ELPEVEKYLP TEDGDPPLGN AKEYAWNEAE EKIVSTDLID
NQSVFPLELS TMPGWAGSSW YWLRYMDAHN EKEFASQESL NYWQNVDLYI GGSEHATGHL
LYSRFWNKFL KDRGFIQAEE PFQKMINQGM ILGTSAFVYR LEGTNTFISK GQIGDKKVQA
IHADVSLVNT SSELDIEGFK QWRPDFADAE FILDENGKYI VGHEVEKMSK SKYNVVNPDD
ICEQYGADTL RLYEMFLGPL EQAKPWNTAG ITGVSGFLKK FYNLYFDGDV VSISDEEPTK
EEYKILHTLI KKVEYDIENF SFNTSVSAFM IAVNELQKIK CNKRAILEPM AVLISPYAPH
IAEELWEVLG YNESISRVPF PTFEEKYLVE STKEYPVSFN GKVRFKIELP LDMPNEEVEK
IILADERTQA QLGGNPPKKI IVVKGKIVNV VV
//