ID A0A1H7SA15_STRJI Unreviewed; 964 AA.
AC A0A1H7SA15;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=SAMN05414137_111209 {ECO:0000313|EMBL:SEL68584.1};
OS Streptacidiphilus jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=235985 {ECO:0000313|EMBL:SEL68584.1, ECO:0000313|Proteomes:UP000183015};
RN [1] {ECO:0000313|Proteomes:UP000183015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC / KCTC 19219 / NBRC 100920 / 33214
RC {ECO:0000313|Proteomes:UP000183015};
RA Varghese N.;
RL Submitted (OCT-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}.
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DR EMBL; FOAZ01000011; SEL68584.1; -; Genomic_DNA.
DR RefSeq; WP_042444484.1; NZ_FOAZ01000011.1.
DR AlphaFoldDB; A0A1H7SA15; -.
DR STRING; 235985.SAMN05414137_111209; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000183015; 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 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:UP000183015}.
FT DOMAIN 66..170
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 295..509
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 811..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 566..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 737..741
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT COMPBIAS 566..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 740
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 964 AA; 106680 MW; CE01E0F0C985E9ED CRC64;
MSESTSEAAA AAPYRYTHAL AAQIEARWQD RWEKDGVFAA PNPVGPLADA ADADAASRPH
AFIMDMFPYP SGAGLHVGHP LGYIATDVYA RHLRMTGHNV LHTMGFDAFG LPAEQYAVQT
GTHPRVTTEA NIAKYREQLR SLGLGHDLRR SISTIDPSYY KWTQWIFLQI FNSWYDPEAQ
AARPIAELVE KFASGAVQTP DGRAWSALTP AERDELLGEY RLAFVKQAPV NWCPGLGTVL
ANEEVTADGR SERGNFPVFK ANLRQWMMRI TAYADRLIDD LDLLDWPEAI KLQQRNWIGR
SEGAKVDFKV HTTEAGDGDA AITVFTTRPD TLFGATYMVL APEHELVESI VPAAWPTADG
DLPVEWTGGY ATPTEAVDAY RRQAAAKSDV ERQADAKTKT GVFTGSYAVN PVSGELVPVF
IADYVLMGYG TGAIMAVPAH DSRDFAFARA FRLPMRCVVQ PSDDRGTDPS TWDDSFDSYD
AAIVNSKNDF ISLDGLGVVD AKKAITDWLA TQGIGAGTVN YKLRDWLFSR QRYWGEPFPI
VYDEDGVAHP LPASMLPVEL PEIEDYSPRT FDPDDADTKP ETPLSRAEDW VSVTLDLGDG
PKQYRRETNT MPNWAGSCWY ELRYVDPEDD TEVVNPVNEA YWMGPTEVKK AGGADLYVGG
AEHAVLHLLY ARFWHKVLFD LGHVSSCEPF HKLFNQGMIQ AYVYRDERGF PVPAAETEER
DGVWYFEGKP VSREIGKIGK SLKNVVAPEE VTGEYSVDTL RLYEMAMGPL DVSRPWDTRA
VVGSFRFLQR LWRTVVDEET GEVVVTDETP DEETLRALNK AIDGVRTDML NLRFNTAVAK
ATELNNFLVK RGSTPRAVAE QAVLLVAPLA PHIAEELWEK LGHEESLVHA QLPEADPAYL
VEDSVTCVVQ IKGKVKARLE VPPAIGDAEL ETLALADPAV VAALGGAEVR KVIVRAPKLV
NIVV
//
