ID A0A1H4CNL7_9FLAO Unreviewed; 943 AA.
AC A0A1H4CNL7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05421540_10886 {ECO:0000313|EMBL:SEA61908.1};
OS Psychroflexus halocasei.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=908615 {ECO:0000313|EMBL:SEA61908.1, ECO:0000313|Proteomes:UP000198820};
RN [1] {ECO:0000313|EMBL:SEA61908.1, ECO:0000313|Proteomes:UP000198820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23581 {ECO:0000313|EMBL:SEA61908.1,
RC ECO:0000313|Proteomes:UP000198820};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNQF01000008; SEA61908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4CNL7; -.
DR STRING; 908615.SAMN05421540_10886; -.
DR Proteomes; UP000198820; 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; 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:UP000198820}.
FT DOMAIN 43..177
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 282..463
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 714..744
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 791..907
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; 108491 MW; F1DF87C6203A146D CRC64;
MAYNFKEIEA KWQKKWADNK TFAAQQPQDF KEKAKPPYYV LDMFPYPSGA GLHVGHPLGY
IASDIFARYK RHQGFNVLHP QGYDSFGLPA EQYAIQTGQH PAKTTEDNIK RYREQLDRIG
FSFDWDREVR TSSPEYYKWT QWIFSELFNS YYCHKADQAK PIDEIIKIFS KEGNININVA
CDENVENFSA DEWNAFSNEK KEEILLDYRL TYLAETEVNW CPALGTVLAN DEIINGVSER
GSHPVVRKKM KQWSMRISAY AERLLQGLNK LDWTDSLKES QRNWIGKSIG AQVFFNLKDQ
DQKIEVFTTR PDTIFGASFL TLAPEHDLVQ KITTPEQKEA VDNYITQTSK RSERERMADV
KTITGVFTGS YAEHPLTNEP IPIWIGDYVL AGYGTGAVMA VPSGDQRDHD FARHFDLPIP
NVFKNIDISE KAHTEQDNTV IANSEFLNDL EPQKAIRKAI EALENKKSGY AKINYRLRDA
VFSRQRYWGE PFPVYYVNGL PKIIETKYLP LELPEVEKYL PTEDGAPPLG RANKWAWNTT
TNEVVHNSEI DHKTVFPLEL NTMPGWAGSS WYLFRYMETE NRDKCFASEE ALDYWENVDL
YIGGSEHATG HLLYSRFWTK FLKDRGFIKV DEPFKKLINQ GMILGESAFV HRIDANTYIS
SDLKTEKEAL KIHVDVSFVN TSNELDIEAF KKWRPEFENA EFIKNDDGKV LVSREVEKMS
KSKFNVVNPD DVCDEYGADS LRLFEMFLGP IDQSKPWNTA GLSGVSSFMK KLWKLYHKGD
DFEVSENPAS KEALKALHQT IKKLTEDIEN FSFNTSVSSF MICVNTLLSE KCNSREVLEP
LAILISPFAP HIAEELWEKL GHTESISQAK FPVFEEKFLV EDTKTYPISF NGKMRFKLDL
SLDLSKDEIE KIVMADERTQ KQLDGRTPKK VIIVPGKIVN IVG
//
