ID A0A0M4RRV9_9MICC Unreviewed; 841 AA.
AC A0A0M4RRV9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=AOC05_07395 {ECO:0000313|EMBL:ALE94071.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE94071.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-2015) 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}.
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DR EMBL; CP012677; ALE94071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4RRV9; -.
DR KEGG; aaq:AOC05_07395; -.
DR PATRIC; fig|656366.3.peg.1584; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000062833; Chromosome.
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; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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:UP000062833}.
FT DOMAIN 59..199
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 240..427
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 442..643
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 679..803
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 60..70
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 606..610
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 841 AA; 92660 MW; 3A61EBD8EF14D8B7 CRC64;
MIEKAGYVSV QSQTEENSEE GVYSFAAMEA KWPAIWDELK VFTPLDDGSK ERRYVLDMFP
YPSGDLHMGH AEAFAMGDVV SRYWRQLGYD VLHPIGWDSF GLPAENAAIK RNAHPSEWTY
ANIDTQAESF KRYAISVDWS RRLQTSDPEY YRWTQWLFKR FYERGLAYRK NSPVNWCPKD
QTVLANEQVV NGACERCGTI VTKKSLNQWY FKITDYADRL LDDMDSLKGH WPDRVLAMQK
NWIGRSEGAH VTFAIKAAGE GKPAQDLTVF TTRPDTLYGA TFFVVAADAP LALDLVTAEY
AEALSEYREN VKALSDIERQ STDRPKSGVF TGRFAINPLT GEKLPVWAAD YVLADYGTGA
IMAVPAHDQR DLDFAKAFNL PVRAVLDTGM QDPAETGIAT TGDGTLINSG ELNGLSKTEG
IPAAIEVLEK LGTGEKYVNF RLRDWLLSRQ RFWGTPIPII HCADCGEVPV PDDQLPVRLP
ENLRGEDLSP KGTSPLAAAA DWVNVACPKC GGAAKRDTDT MDTFVDSSWY FLRFVSPDFT
EGPFDPAKVN DWMPVGQYVG GVEHAILHLL YARFFTKVIH DMGMLEATEP FSALLNQGQV
LNGGKAMSKS LGNGVDLGEQ LDKFGVDAVR LTMVFAGPPE DDVDWADVSP SGSAKFLGRA
WRLARDVSSD ARTDAAAGDA ALRSLTHRTV HETKTLLEGH KFNVVVAKLM ELVNATRKVI
DSGAGAGDPA VREAAEAVAI VLSLFAPYTA EDMWETLGHP ASVANAGFPD VDEALLVQQS
ITAIVQIQGK VRHRLDVSPN ITAEQLRELA LASEDVQKAL AGRDIRTVIV RAPKLVNIVP
V
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