ID A0A1H1M8K2_9FLAO Unreviewed; 938 AA.
AC A0A1H1M8K2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=SAMN04515667_0784 {ECO:0000313|EMBL:SDR83154.1};
OS Formosa sp. Hel1_31_208.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1798225 {ECO:0000313|EMBL:SDR83154.1, ECO:0000313|Proteomes:UP000199458};
RN [1] {ECO:0000313|EMBL:SDR83154.1, ECO:0000313|Proteomes:UP000199458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_31_208 {ECO:0000313|EMBL:SDR83154.1,
RC ECO:0000313|Proteomes:UP000199458};
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; LT629733; SDR83154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1M8K2; -.
DR STRING; 1798225.SAMN04515667_0784; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000199458; Chromosome i.
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:UP000199458}.
FT DOMAIN 38..154
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 277..457
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 711..739
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 789..902
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 713..717
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 938 AA; 106977 MW; CAC8C7FA649B127B CRC64;
MSYHFNTIEA KWQKYWAEHQ TFKAKNNSDK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
YARYKRHKGF NVLHPQGYDS FGLPAEQYAI QTGQHPAITT ETNIKTYRRQ LDQIGFSFDW
SREVRTSDPN YYKWTQWIFI QLFESWYNND TNQAEHMDTL ISKFSSEGNA FVNAVCDDNI
LAFTAQDWAR FSSIEQQEIL LKYRLTYLAE TEVNWCPALG TVLANDEIVN GVSERGGHPV
IRKKMTQWSM RISAYAERLL QGLETIDWTD ALKESQRNWI GKSVGASVTF NVNSHDEVIE
VFTTRPDTIF GVSFMTLAPE HDLVSKITTA DQKTEVEAYI QATAKRSERD RMADVKTISG
VCTGAYAEHP FTKEPIPIWI GDYVLAGYGT GAVMSVPCGD QRDYDFATHF NIPIPNIFEG
VDISEAAFDD KANTIITNSD FLNGMNYKKA TKRAIYELEQ LGQGEGKTNY RLRDAVFSRQ
RYWGEPFPAY YVNGMPQMIN KEHLPIRLPE VEKYLPTEEG EPPLGRADVW AWCTKTNTVV
TNDNINNKTV FPLELNTMPG WAGSSWYFFR YMEEAMRDEV FASEEALSYW ENVDLYIGGS
EHATGHLLYS RFWVKFMHDR GFVNVDEPFK KLINQGMILG TSAFVYREEG TNRFLSKGLI
ANTKVQPIHS DVAFVNASDE LDIDAFKTWR DEFKDAEFIL EKGVYKVGRE VEKMSKSKYN
VVNPDAICEQ YGADSLRLYE MFLGPLEQAK PWNTAGITGV HGFLKKLWKL YVGDNGLNVN
DAQPTKDNLK TLHKTIKKVE EDIENFSFNT SVSTFMIAVN ELTAQKCTSK VILEPLLIVL
SPYAPHIAEE LWSSLGNDES ISIATFPKFE AQHLVESSKN YPISFNGKTR FTLELPLDMN
KEEIEKTVMA HEKTIAQLQG RTPKKVIVVP GKIVNIVG
//
