ID A0A1F6CPG5_9BACT Unreviewed; 1126 AA.
AC A0A1F6CPG5;
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=A2763_04220 {ECO:0000313|EMBL:OGG51048.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_54_36.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798482 {ECO:0000313|EMBL:OGG51048.1, ECO:0000313|Proteomes:UP000178370};
RN [1] {ECO:0000313|EMBL:OGG51048.1, ECO:0000313|Proteomes:UP000178370}
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:OGG51048.1}.
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DR EMBL; MFKV01000003; OGG51048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6CPG5; -.
DR STRING; 1798482.A2763_04220; -.
DR Proteomes; UP000178370; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010662; Hydrolase_RBBP9/YdeN.
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; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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; PF00293; NUDIX; 1.
DR Pfam; PF06821; Ser_hydrolase; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 565..699
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 905..909
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1126 AA; 128249 MW; 9F337C07EE4980BE CRC64;
MKSYDHKSIE KKWRNKWEKD GLYKTPDSAK GRENFYLLTE FPYPSGNLHV GHWYAFALPD
IRARFESMRG KNVLFPIGFD AFGLPAENAA IKNKVNPRNW TESNIEYMKG QIKSMGTSFD
WSREVQTIDP DYYRWTQWMF LQFFKNNLAY RKDTPVNWCP KDKTVLANEQ VVDGKCERCD
TEVVQKQMLQ WNLKITNYAD RLIDDLEPLD WPKEIKDSQR NWIGRSEGAE IDFPLVGNVK
DDSRFLLLHG RESTSAGEYQ PWLKAELEKR GYEVEVVDLP NPNEPNDKEQ ADYVEKHCKL
DERTVVVGHS FGGVVALRLL ERGHKVRRVV LVSTPYSGRF LDKKVRKSVT AALKKRFDFE
TIKKNAKTFM VVPDAKDPVV PASDGEALRK ELGAMYMPGK ANSSHFTADI EQDVLMMCAP
TIRVFTTRAD TLYGGTYLVL APEHPWVQLA LAHKGLLENE DEVVRYIDTS SKKTEIERQA
VEKEKTGVKL KGVRAINPAT GKEIPIWVAD FVIGSYGTGA VFADAHDERD YAFAKKYGIP
FKETLEPVAT KTTGADALKP NMPLIDRQAA MAIVRHPTED KYLGVTYKPT SVKGFISGGI
EDNEKPEEAL KREIREEAGF TNIKNVRQLG SVIHSRFWSV KYNRNTNSHY LPFLVELEDL
AREEVSAAEK AEHDMEWMSP TELETFINRD DWRAAWNRLQ GRAYAGKGIL FDSGEFSGLT
SDEAIPKIGA KFGRIVKQYH LRDWIVSRQR YWGVPIPIIH CAKCGMVAVP DKDLPVKLPE
VKDYLPEGSG KSPLAKATKW VKVKCPQCKG PAERETDTLD TFVDSSWYFL RYSDPKNKKK
FADRKKMDAW MPVDLYSGGA EHTTMHVLYS RFWQKALFDL GLVKDSEPYK RRMNRSLILG
PDGQKMSKSR GNVVDPDEVV ARLGADTVRM YLAFIGPYNE VSSFPWNPDG VAGIRRFLER
VVRLSECVVN EEVPENESIL HKTIKKVGDD IQALKFNTAI SQLMISVNHI EKRGKIAESQ
WDVFLRLLAP FAPFVSEELW YDAGHKTSLY SAEWPAYDAE RLVDEKVTIA VQINGKTRGT
ALIDVGIDSI AQEAEAQKSV QDRLIGKKIA RTVVVPGRLV NFVLEE
//
