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Database: UniProt
Entry: A0A0P9A6G7_9PROT
LinkDB: A0A0P9A6G7_9PROT
Original site: A0A0P9A6G7_9PROT 
ID   A0A0P9A6G7_9PROT        Unreviewed;       838 AA.
AC   A0A0P9A6G7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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   ECO:0000313|EMBL:KPU81965.1};
GN   ORFNames=JI56_03910 {ECO:0000313|EMBL:KPU81965.1};
OS   SAR11 cluster bacterium PRT-SC02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=1527298 {ECO:0000313|EMBL:KPU81965.1, ECO:0000313|Proteomes:UP000050662};
RN   [1] {ECO:0000313|EMBL:KPU81965.1, ECO:0000313|Proteomes:UP000050662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRT-SC02 {ECO:0000313|EMBL:KPU81965.1};
RA   Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA   Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT   "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT   Rico Trench Inferred From Single Cell Genomes.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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:KPU81965.1}.
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DR   EMBL; JPUP01000096; KPU81965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9A6G7; -.
DR   PATRIC; fig|1527298.3.peg.768; -.
DR   Proteomes; UP000050662; 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; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 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; 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; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000050662}.
FT   DOMAIN          37..167
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          218..398
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          608..647
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          684..799
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           38..48
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   838 AA;  98043 MW;  A63042B69BABFBFC CRC64;
     MERIVFNKIE KKWQDIWSEK KVKKKKNQKK FYCLEMFPYP SGKIHMGHVR NYTIGDVIAR
     HKIMKGFDVM HPMGWDAFGL PAENAAKENN LNPKEWTFQN IETMKKQLQM LGFSIDWERE
     ISTCKEDYYK QQQSLFIDLY KNDFVGRKET YVNWDPVEKT VLANEQVIDG KGWRSNQPVE
     RKKLNQWFFK ITKFSEDLLN DMKTLDNWPN KVKLMQSNWI GKSVGCEIDF QLSNSKEKIK
     VFTTRPDTIF GATFLSISVD HPICKIIKSQ KEFQNFKLKC LKTGTTEEAI ANAEKEGFKT
     EFSAINPFNK KEIPVYVSNF VLMDYGTGAI FGCPAHDQRD LDFAIKYDLE VIQVVKENDL
     IDFKKTGTAF TDHGIMVNSS MLNGLSTSDA KIKIIKEVEK NKIGKKKISY RLRDWGVSRQ
     RYWGCPIPIV YDKKGKIHVL DKSELPVKLP EDVDFNQPGN PLDKHKNWKY YKNSKGEEFI
     RETDTLDTFV DSSWYFLRFC SPQNNQEPFN LSEVNYWMPV DQYIGGVEHA ILHLLYSRFF
     VKALKKCGYK IEFDEPFKNL FTQGMITHET YKDENGKWLS PDEIEKVGDK LAKKKKDKSD
     VTVGAPESMS KSKKNIIDPE ETVKIYGADS IRWFVLSDSP PDKDILWSDR GINAAYKFLQ
     KVWNLNSQIN LLSERKGNLD IEKKYEKEFS KYILKIDDHI EKFNLNVMIA NIYEYFNALN
     ECFKLSASKT FLEKHLINLM KIMFPITPHL SSECLETLKC KSDEWPSVDK KLVKDDEIKL
     VVQINGKTRL VTSMKVDMEE NKITETLLKN DKLKKYLVEN KIKNKIFIKN KLINYIIK
//
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