ID A0A1F7I7C3_9BACT Unreviewed; 877 AA.
AC A0A1F7I7C3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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=A3A74_07405 {ECO:0000313|EMBL:OGK39264.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_35_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802055 {ECO:0000313|EMBL:OGK39264.1, ECO:0000313|Proteomes:UP000179270};
RN [1] {ECO:0000313|EMBL:OGK39264.1, ECO:0000313|Proteomes:UP000179270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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 -!- 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:OGK39264.1}.
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DR EMBL; MGAF01000054; OGK39264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7I7C3; -.
DR STRING; 1802055.A3A74_07405; -.
DR Proteomes; UP000179270; 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; 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; 2.
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.
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 13..224
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 232..416
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 424..631
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 692..835
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 601..605
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 877 AA; 101293 MW; 75F1D836D972E920 CRC64;
MAKYQPQEFE GKWREKWKEE GLYGTPLRSL NQRATLGAGK KKFYTLVELP YTSGDLHVGH
WFSFTIPDIL SRFKRMNGFN VFYPIGYDAF GLPAENAAIK HKIHPKDWTL KNVENMTKQF
QTMGTMLNNW DDVVITCLPE YYRWNQWIFL KFWEKGLAYR GKALSNWCPS CQTVLANENI
ENGKCWRCGN PVIQKQVEQW FLKITDYADR LLWNNHSNGV DWPVSVRVGQ NNWIGKKEGV
LIKHKVRDLD LVFESFSAFP AWLWADTFIV IAPEHPLVER LVQGTKYEKE SEIFVKRMKG
KTQEERLKEI DTKEGVFTGR YAKDPFAYAQ GKPADMPIWI SNFALMDFGS GIIRCSAHDP
RDYAFAQKYK IELKEVVERS DKKTPVNAHD NKGILKNSGL FTGKKIEESL AEIVGWIVKQ
KIGKKHFNYH LRDWSVSRQR YWGTPVPMIN CSNCGTVPVP EKDLPVGLPY EVDFTPKGKP
FGSAQGKPPL ASNEKWLNVK CPKCGKNAKR DAETLDTFFD SAWYWFRYVS PHYDKAPFDK
KMVKDLTPVD VYFGGSEHTL GHTMYARFFT KFFHDLGLVD YEEFALKRIQ HGVVLGPDGN
RMSKSKGNVI NPDEVVKEYG TDTVRMYLCF MMPYEATGPW SDKTIAGVHR FLNRVWKIYQ
NFQFSILNFQ SNPNSQNPND KSNPKSKIQN QDKTLVAKLN KTIQKVTSDI EKIKMNTAIA
AMMEMINDWE TVVNSQFLIS KFQSNPKSQI QNKKNNETMK QLNNSLSVEN AKKFLQILAP
FAPHMTEEIW RNVFGEKESI HLSSWPKAME TVAETITIPV QVNGKVRDLL IVNSELLIDE
KKVTDLALKS EKVKKYLAKK KYRAIYVQGK ILNLVVQ
//
