ID A0A1F5S045_9BACT Unreviewed; 1178 AA.
AC A0A1F5S045;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A3I35_02275 {ECO:0000313|EMBL:OGF20070.1};
OS Candidatus Falkowbacteria bacterium RIFCSPLOWO2_02_FULL_45_15.
OC Bacteria; Candidatus Falkowbacteria.
OX NCBI_TaxID=1797988 {ECO:0000313|EMBL:OGF20070.1, ECO:0000313|Proteomes:UP000177878};
RN [1] {ECO:0000313|EMBL:OGF20070.1, ECO:0000313|Proteomes:UP000177878}
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 ECO:0000256|RuleBase:RU363035}.
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:OGF20070.1}.
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DR EMBL; MFFV01000014; OGF20070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5S045; -.
DR STRING; 1797988.A3I35_02275; -.
DR Proteomes; UP000177878; 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 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; IPR001412; aa-tRNA-synth_I_CS.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
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; PF06821; Ser_hydrolase; 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; 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; PS00178; AA_TRNA_LIGASE_I; 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};
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 46..191
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 229..383
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 857..979
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 1032..1139
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 952..956
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 955
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1178 AA; 133989 MW; D184AE021ECD90C6 CRC64;
MNKKRYVTYD DFIKNGGEEY WQTGWQSSDL YQAEDFAKKK KKYILIEFPY PSGAGLHVGH
VRSYTALDIM SRMLRLQGYN VLYPIGWDAF GLPTENYAIK NKIHPRLATE ANIKTFRRQL
KSLGLSFDWS REVDTTDPKY YQWTQWIFLQ LFKKGLAYKK KIPINWCPSC KIGLAHEEVI
DGKCERCGTA VEQREKEQWL LAITKYADRL IKDLDPVDYL EKIKTQQVNW IGRSKGAELK
FEVRSKKLEK KEYLNVFTTK PDTLFGATYM VLAPEHELVT QLKDQIENWR EVEKYINQAK
TKSELQRTSL EKAKTGVELE GIKAINPANN EEIPVWIADY VLASYGTGAI MAVPAHDERD
FEFAKKFKLP IKQVIAPETG NKRDGENVVQ GGCGVVFDPK SQKYAVAAWN NGMIGLFSGN
VGKTEDEQAG ILREVTEESG LHDFLHIEKI ATAYPHYYNS AKNSNRHGSA ACYLAVLKTA
NMRPTKREAH EKFELQWRSP AEILNNWRKY NQKNDLDHWV WFLRQAVGKA IELGYDSTSD
NSIFYISAYV GKGVIINSGG FNGLSSDEAK KKITAKVGGK MKVQYKLRDW IFSRQHYWGE
PIPMVYCEQC AQRKPKVLLI HGLYGHSKEN WLPWFKKQME KNGYEVLIPD LPNNERPSLA
EWLKALGNLG IRKGDQLFIV GHSLGAPTAC QFILKNKLRV EKLILVAPTG KSQNENNFAN
LQKAGCSKEA INCIKDFNDA NTGLGKLKKS VENSVVYFSD NDPYIPLDVQ NDYRALGAEE
KLLRSKGHFN SNAGVVELPE ILEEFPSALD FGWIPVPEKD LPVELPKVKH YEPTDTGESP
LAVIKDWVNT ECPRCGGKAK RETDTMPNWA GSSWYFLRYC DPKNNKAFAD AVKLKYWLPV
DLYNGGMEHT TLHLLYSRFW NKFLYDCGLV PVSEPYARRV SHGMVLAEDG KKMSKSLGNV
INPDEVVNNV GADSLRLYEM FMGPFADTIP WSMEGVKGVR RFLEKVFALT PQPPLPRGEG
KRVPASGVRV LLHKTIKKIT EDIENMKFNT AVSAMMIFVN EAQAEGLAKD ELEKFLIILA
PFAPHMTEEL WSRLGHKQSI FKEKWPAYDA NLTKDEIVRL AIQVNGKLRD TMEAAADISA
DEAKAKALAS EKVKKWTEGK LIAKVIVVKN RLVNIVVK
//
