ID A0A1J5I1A0_9BACT Unreviewed; 815 AA.
AC A0A1J5I1A0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AUK57_01505 {ECO:0000313|EMBL:OIP86126.1};
OS Candidatus Saccharibacteria bacterium CG2_30_41_52.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1805375 {ECO:0000313|EMBL:OIP86126.1, ECO:0000313|Proteomes:UP000183829};
RN [1] {ECO:0000313|EMBL:OIP86126.1, ECO:0000313|Proteomes:UP000183829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_41_52 {ECO:0000313|EMBL:OIP86126.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIP86126.1}.
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DR EMBL; MNZN01000002; OIP86126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5I1A0; -.
DR STRING; 1805375.AUK57_01505; -.
DR Proteomes; UP000183829; 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; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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.
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}; Cytoplasm {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 49..184
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 414..608
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 655..779
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 579..583
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 815 AA; 93057 MW; 0E5E5404E81A2C4D CRC64;
MKRYNPTEIE QKWQKIWEDE GTYKVDFSDH IKPKYYSMSM LPGITGAGIH TGHGRTFQFS
DIKVRAKRQQ GYNAYHPIGW DSFGLPVENY AIKIGKKPRI AHDEALVHFK QQLKRLGYSY
DWSKEISTAD PSYYKWTQWI FNKLYEHGLA YQKESPQWWC ETDQTVLANE QVIGGKCWRC
NNQVTKKNLN QWFFKITEYA DEILEATDDL NWTEMVKTMQ KNWIGRSQGA EVEFKIDGRD
EILTVFTTRP DTLFGATFVV LAPEHELAKT LSTDETRESV EGYILEAARK SEIERMNESR
EKTGVFTGSY AINPVNSNKT PIWIADYVLA GYGTGAIMSV PAHDERDFTF AEKFNLPIIE
VIEKPATDEE VGVYCGEGPL VNSGRFDGID SADAREQIVD WLEQEGAGKT KVTYKMRDWL
ISRQRYWGAP IPIIHCLEHG AVAVPDDQLP VILPDVDDFK PHGGETSALA GVTEWVNTTC
PKCGGPAKRE TDTLDGYACS SWYFLRYIDP FNDKQAWDPE VENHWGPVDF YNGADHAVAH
LLYSRFWMRF FYKLGLVSTP EPFKRMMYNA YILAPDGTKM SKSKGNTIDP LEIMDSGYGA
DSLRVYEMFI APYDLEAPWD TRGVPGTYRF LNRVWTLVQD YIDAGEVSLT DAAIKEILVI
AHKTAKKITS DIEDDKFNTA VSSMMEAVNS YYKIRTEQPI GKSAAWTFAV ESLLQLLSPF
APHITEELWH QMGNSDTIHV DHWPAWDNKY LQADNMTIVV QVNGKLRAKL EIAADTSEDE
IKQLALVESN VQTFMDNKKP TKVIYVPGRL VNIVV
//
