ID A0A1I0DNV6_9BACT Unreviewed; 996 AA.
AC A0A1I0DNV6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN04487998_1490 {ECO:0000313|EMBL:SET34220.1};
OS Hymenobacter actinosclerus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=82805 {ECO:0000313|EMBL:SET34220.1, ECO:0000313|Proteomes:UP000198697};
RN [1] {ECO:0000313|Proteomes:UP000198697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15310 {ECO:0000313|Proteomes:UP000198697};
RA Varghese N., Submissions S.;
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:RU363035}.
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; FOHS01000002; SET34220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0DNV6; -.
DR STRING; 82805.SAMN04487998_1490; -.
DR Proteomes; UP000198697; 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; 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; 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; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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:UP000198697}.
FT DOMAIN 13..145
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 279..477
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 766..795
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 846..958
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 769..773
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 772
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 996 AA; 113351 MW; DC6A347AAB2E96C7 CRC64;
MPGYNPQKIE KEWQDFWQAH QTFQADNHSD KPKYYVLDMF PYPSGAGLHV GHPLGYIASD
IVARYKRLRG FNVLHPMGFD SFGLPAEQYA IQTGQHPAIT TEQNISTYIR QLSALGFSYD
WSREIRTSDP AYYKWTQWIF LKLFNSWYNL DTDQAEPLKT LLAKFAQSGS AGIRAAGDEA
ERHEFTAGQW QSFSEKQRLQ AVHPYRLAYQ QDTYVNWCPG LGTVLSNDEV KDGLSERGGF
PVERRLMPQW NLRITAYADR LLAGLDQLDW PDAVKEMQRN WIGKSQGASV RFPVYLRDAS
GEMKPQPEEI EVFTTRVDTI FGATFLVLAP ELDLTLALGE RAAAQADYSP AASRTWSELQ
AYVKTAVNRS ERERQTDVKT VSGAPTGFYV QNPFTLEYVP VWTADYVLAG YGTGAVMGVP
SGDQRDWLFA THFALPIRQV LDAQQNLDQQ ADPTKEGRYI NSGFITGLTY DEATEQLRLR
LRANRVGEPK VTYRIRDAIF GRQRYWGEPI PIYYKDGVAY GVAEADLPLV LPEIDAYKPT
ETGEPPLARA QNWKYKGQYD YELSTMPGWA GSSWYYLRYM DPHNAERFVG EEAEAYWQNV
DLYLGGAEHA TGHLLYSRFW HLFLKDLGLV TAPEPFQKLI NQGMILGRSS FVRQMSVDTT
WHPGDTEPKF PKIFISSDLI DDSYQVREDK LEYVKKQLND IGDKIANKLQ LNHVRFSSNG
VFNRHVEVSY VENDILNIDK FKAWRPENKD AEFIRNENNE YLCDWEIEKM SKSKHNVVNP
DDLVERYGAD ALRMYEMFLG PLEQFKPWNT NGMSGVAGFL KKLWRLYHPQ DGPLAVTDAP
AEPAELKALH KAIRKVEEDI ERFSFNTTVS ALMITVNELT ALACHKRAIL EPLVVLLSPY
APHLAEELWA ELGHAPGSIS QAPYPEFREQ YLVEDTVNYP VAVNGKVREQ LQFPAAATAA
EIEAAVRATD ILARFGEGKE AKKVIVVPGR MVNIVV
//
