ID A0A0B7HH96_9FLAO Unreviewed; 952 AA.
AC A0A0B7HH96;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ECO:0000313|EMBL:CEN38630.1};
GN ORFNames=CCYN2B_50106 {ECO:0000313|EMBL:CEN38630.1};
OS Capnocytophaga cynodegmi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=28189 {ECO:0000313|EMBL:CEN38630.1, ECO:0000313|Proteomes:UP000038055};
RN [1] {ECO:0000313|Proteomes:UP000038055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ccyn2B {ECO:0000313|Proteomes:UP000038055};
RA MANFREDI Pablo;
RL Submitted (JAN-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}.
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DR EMBL; CDOD01000045; CEN38630.1; -; Genomic_DNA.
DR RefSeq; WP_041993891.1; NZ_CDOD01000045.1.
DR AlphaFoldDB; A0A0B7HH96; -.
DR STRING; 28189.CCYN74_30179; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000038055; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000038055}.
FT DOMAIN 38..143
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 276..473
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 721..753
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 805..917
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 727..731
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 952 AA; 109193 MW; 272AFDB539885EE0 CRC64;
MNYNHKDIEA KWQKYWSENQ TFKTENHSEK PKFYVLDMFP YPSGAGLHVG HPLGYIASDI
FARYKRHKGF NVLHPQGYDS FGLPAEQYAI QTGQHPEKTT RENIARYREQ LDKIGFSFDW
SREVRTSNAD YYKWTQWIFI QLFHSWYNNT TNKAEDIQTL VQHFEKFGTE NLNAAQTEEL
HFTAEQWKSY SEEEKQNILL NYRLAFRAET TVNWCPALGT VLANDEVVNG VSERGGYPVF
QKKMTQWSMR ITAYSERLLQ GLETVDWSES VKESQRNWIG KSKGASIKFK VLSSKFQDIE
PETSSVEHIT VFTTRPDTIF GVTYLTLAPE HELVLQITTE AQKQAVLDYI EATSKRSERD
RMADTKTISG VFTGAYAEHP ITKRPVPIWI GDYVLAGYGT GAVMAVPTGD ERDYAFAKHF
AGAEGMPEII NIFDKDISEN AFTEKGGFKL QNSDFLNGMD YEEATEKILE ELEKTGVGKA
KINYRQRDAI FSRQRYWGEP VPVYYKNGMP YTLPLSALPL ELPEVEKYLP TEDGDPPLGN
AKEYAWNEAE EKIVSTDLID NQTVFPLELS TMPGWAGSSW YWLRYMDAHN EKEFASQESL
NYWQNVDLYI GGSEHATGHL LYSRFWNKFL KDRGFIQVEE PFQKMINQGM ILGTSAFVYR
LEGTNTFVSK GQIGDKKVQA IHADVSLVNT SSELDIEGFK QWRPDFADAE FILDENGKYI
VGHEVEKMSK SKYNVVNPDD ICEQYGADTL RLYEMFLGPL EQAKPWNTAG ITGVSGFLKK
FYNLYFDGDA VSISDEEPTK EEYKILHTLI KKVEYDIENF SFNTSVSAFM IAVNELQKIK
CNKRAILEPM AVLISPYAPH IAEELWEVLG HNESISRVLF PTFEEKYLVE STKEYPVSFN
GKVRFKIELP LDMPNEEVEK IILADERTQA QLGGNPPKKI IVVKGKIVNV VV
//
