ID A0A1Y1CJK6_9BACT Unreviewed; 920 AA.
AC A0A1Y1CJK6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ALGA_2237 {ECO:0000313|EMBL:BAX80569.1};
OS Labilibaculum antarcticum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Labilibaculum.
OX NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX80569.1, ECO:0000313|Proteomes:UP000218267};
RN [1] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:BAX80569.1, ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|EMBL:BAX80569.1,
RC ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 39:1-2(2018).
RN [3] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL Antonie Van Leeuwenhoek 113:349-355(2020).
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; AP018042; BAX80569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1CJK6; -.
DR KEGG; mbas:ALGA_2237; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000218267; Chromosome.
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; 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; 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 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}.
FT DOMAIN 11..144
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 276..455
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 771..882
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 694..698
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 920 AA; 106000 MW; 49A409C4FA884CEA CRC64;
MEYNFKEIEQ KWQKYWTEEK TYKVEVDSER PKFYVLDMFP YPSGAGLHVG HPLGYIASDI
YSRYKTLKGF NVLHPMGYDA YGLPAEQYAI QTGQHPAVTT ETNIKRYREQ LNKIGFSYDW
DREVRTCQPE YYKWTQWAFI QMFNHFFNND IEKAESIESL ISKFEFEGNV NVNAACSETE
PFSAEEWKAF SDNEKQATLL NHRLAYLADT MVNWCPKLGT VLANDEVKDG LSARGGYPVE
QKRMRQWSLR VSAYAKRLLD GMETLEWTDS LKEIQKNWIG RSVGAEVNFG VKGSDIKMEV
FTTRPDTIFG VTFMVLAPES DWVKELTTPE YQADIDAYIE ATNKRTERER LADVKTISGA
FTGAYAINPF TGQEIPIWIS DYVLAGYGTG AIMAVPAHDS RDYAFAKHFD LPIIQVVSGG
DISEESYDAK TGKSMNSDFL NGLDVKDAIV KANEEVEARG LGKKKINYRL RDAIFSRQRY
WGEPFPVYFK DGMPQMMDLD KLPLKLPEID KYLPTESGEP PLGRAKNWVT EDGYPIELNT
MPGFAGSSAY YLRYMDPRNN DALVSTEANE YWQDVDLYIG GTEHATGHLI YSRFWNKFLF
DINEVCKDEP FKKLINQGMI QGRSNFVYRD KKSNKYVSHG LIKEYDTTAI HVDVNIVKND
VLDLEAFKNW MPEYKDAEFI LEDGKYHCGW AVEKMSKSMF NVVNPDVIVE EYGADTLRLY
EMFLGPLEAH KPWDTNGIDG VHKFLKKLWR LFHNEAGEFE LTNSQPTPDE LKVLHKTIKK
IQDDIERFSF NTSISAFMIC VNEFYTLKCN NKAIFEDLLV ILAPFAPHVA EELWGLCGNT
TSITKARFPE FNESFVQENN HKYPVSFNGK MRFILELPID LSRDEIEKEV LSLEKSQKWI
EGKTPKKIII VPNKIINIVV
//
