ID A0A1G7USG5_9FLAO Unreviewed; 1030 AA.
AC A0A1G7USG5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 34.
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=SAMN04488027_102217 {ECO:0000313|EMBL:SDG49680.1};
OS Psychroflexus sediminis.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=470826 {ECO:0000313|EMBL:SDG49680.1, ECO:0000313|Proteomes:UP000199296};
RN [1] {ECO:0000313|EMBL:SDG49680.1, ECO:0000313|Proteomes:UP000199296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19803 {ECO:0000313|EMBL:SDG49680.1,
RC ECO:0000313|Proteomes:UP000199296};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469, 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; FNCW01000002; SDG49680.1; -; Genomic_DNA.
DR RefSeq; WP_093365302.1; NZ_FNCW01000002.1.
DR AlphaFoldDB; A0A1G7USG5; -.
DR STRING; 470826.SAMN04488027_102217; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000199296; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000056; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000060; Leucine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000011; Leucine--tRNA ligase chloroplastic/mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 2.
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 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:UP000199296}.
FT DOMAIN 43..150
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 282..462
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 788..822
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 880..994
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 858..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 796..800
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1030 AA; 117176 MW; 48BA69E2568C218A CRC64;
MAYDFKRIEQ DWQKYWAKHQ TFKAKQPQDF SGEPKPPFYV LDMFPYPSGA GLHVGHPLGY
IASDIYARYK RHSGYNVLHP QGYDSFGLPA EQYAIQTGQH PAKTTEANIK RYREQLDKIG
FSFDWSREVR TSDPKYYKWT QWIFIQLFES WYDEAAQKSK PISDLIQIFE SEGNSEVQAV
CDGDTPEFSA EDWKAFSDDE KEQHLLNYRL TYLAETEVNW CPALGTVLAN DEIVNGVSER
GGHTVVRKKM KQWSMRISAF AERLLSGLDD LDWSESLKET QKNWIGKSVG AQLKFKIQNS
KFLIEAFTTR PDTIFGVSFI TLAPEHDLVS QITTPEQKEA VDTYVKAAAR RSERERMADV
KSITGVFTGA FAEHPLTQKP IPIWIGDYVL ASYGTGAVMA VPCGDQRDHD FAKHFGIPIP
NVFQGIDISE EAYTDKTNTT KIANSDFLDG LGVLEAIPKA IEALADIGAG DKKINYRLRD
AVFSRQRYWG EPFPVYYVND LPKMIAEKHL PLKLPEVEKY LPTEDGAPPL GRATEWAWDT
ETNQVVSNDK IDHKSVFPLE LNTMPGWAGS SWYLFRYMEE QNNRDQHIAS DEALNYWKNV
DLYIGGSEHA TGHLLYSRFW TKFLNDRGVL PVDEPFKKLI NQGMILGESA FVYRYKASGG
EGRIGENIYI TYDFVKSIKE ELSKFENIFI RENGIFDKNN NIIDSEIIIK YTPILKKIFS
LGQSNMLIME RSFDPIHVDV SVVNTSNQLD IEGLKKIKPE FSEAKFILSN GELYDANSSP
LGRSGGDFTV SREVEKMSKS KFNVVNPDDV CEEYGADSLR LYEMFLGPIE QAKPWNTAGL
SGVHNFLKKL WKLYSQASPD PSQGGESDFQ ISDEPGSKES LKTLHKTIKK VTQDIEDFSF
NTSVSTFMIC VNELTQQKCN SREILEPLAI LISPYAPHIA EELWEGLGHS EGISEVAYPK
FEEKYLKEDS KTYPISFNGK MRFTMDLSLD LSKDEIEEIV MADERTQKQL EGKTPKKVII
VPGKIVNIVG
//
