ID A0A1F1KGT2_9MICO Unreviewed; 984 AA.
AC A0A1F1KGT2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=HMPREF3099_00470 {ECO:0000313|EMBL:OFS16035.1};
OS Kytococcus sp. HMSC28H12.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=1581067 {ECO:0000313|EMBL:OFS16035.1, ECO:0000313|Proteomes:UP000176675};
RN [1] {ECO:0000313|EMBL:OFS16035.1, ECO:0000313|Proteomes:UP000176675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC28H12 {ECO:0000313|EMBL:OFS16035.1,
RC ECO:0000313|Proteomes:UP000176675};
RA Ploux O.;
RL Submitted (MAR-2016) 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: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:OFS16035.1}.
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DR EMBL; LWPN01000014; OFS16035.1; -; Genomic_DNA.
DR RefSeq; WP_070703251.1; NZ_KV824262.1.
DR AlphaFoldDB; A0A1F1KGT2; -.
DR Proteomes; UP000176675; 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; 3.40.50.620; HUPs; 3.
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; 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; 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:UP000176675}.
FT DOMAIN 66..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 303..513
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 836..945
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 572..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 757..761
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 760
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 984 AA; 109431 MW; C69F8A9E1D7F64D0 CRC64;
MSENHRDETP YRYTARLAGE IEKRWQDRWE AEGTFRAPNP VGDLAPQDPA ARAAVADQPK
LMIQDMFPYP SGAGLHVGHP LGFIATDVYA RYQRTTGRNV LYTMGFDAFG LPAEQYAVQT
GQHPRTTTEA NIETYRRQLR QLGLSHDDQR TYATIDPAYY KWTQWIFLQI YNSWYDPQAP
GRRPGTTGRA RPIEELEAAY ASGEVPTPDG RPWDQLDAGE RADAVDARRL AYLSDAPVNW
VPGLGTVVAN EEVTAEGRSE RGNFPVFQRN LPQWMMRITA YADRLVDDLD RLQWPDSVAT
MQRNWIGRST GARVFFDVAV PQSATLPTGP DGQPRLEVFT TRPDTLFGVT FMVVAPEHPV
ADAVPAAWPE GTEDAWTGGH ETPREAVAAY REATARKSDL DRQADDKSKT GVFTGIWATN
PVTGQQVPVF VADYVLMGYG TGAIMAVPGQ DQRDHDFATQ YGIDVVRTVQ PTEGHPDDQA
FTGEGPAINS SNEKVDLDGL GVAEAKARML EHLQSAGTGE EAITYKLRDW LFSRQRYWGE
PFPIVWDADG RAHAVPADQL PVELPEVADY SPKTYDPEDW DTQPESPLGR NTDWVNVTLD
LGDGPKQYRR ETNTMPNWAG SCWYELRYAD PTNSEAFIDP ELEEYWLGAG RGFGEGVADD
PGGVDLYVGG VEHAVLHLLY ARFWHKVLFD LGHVSSEEPF RRLFNQGMVQ AFAYRDDRGQ
PVPAAEVTER EDADHPRAQD GIVYEWNGQP VTREYGKMGK SLKNVVTPDE MCESYGADVF
RVYEMSMGPL DASRPWDTRA VVGSQRFLQR LWRAVVDEAT GELRVTEDAP DADTTRALHR
TIAGVADDYE NLRFNTAVSK LIELTNAVTK LGAVPRAVAE PLVQMVAPLA PHLAEELWSR
LGHAESLATV DFPQADEGQL VAETVTCVVQ VKGKVRDRLE VAPDIADDEL EATALASEKV
QAFIDGAPVR KVIVRAPNLV NIVV
//
