ID Q6SFY4_9BACT Unreviewed; 873 AA.
AC Q6SFY4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
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:AAR38078.1};
GN ORFNames=MBMO_EBAC080-L12H07.27 {ECO:0000313|EMBL:AAR38078.1};
OS uncultured marine bacterium 577.
OC Bacteria; environmental samples.
OX NCBI_TaxID=257398 {ECO:0000313|EMBL:AAR38078.1};
RN [1] {ECO:0000313|EMBL:AAR38078.1}
RP NUCLEOTIDE SEQUENCE.
RA Heidelberg J.F., Eisen J.A., Nelson W.C., DeLong E.F.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAR38078.1}
RP NUCLEOTIDE SEQUENCE.
RA DeLong E.F.;
RT "Monterey Bay Coastal Ocean Microbial Observatory environmental clone
RT sequencing.";
RL Submitted (DEC-2003) 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; AY458645; AAR38078.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6SFY4; -.
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 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 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; 2.
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}.
FT DOMAIN 39..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..413
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 429..585
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 634..671
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 717..835
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 633..637
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 636
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 873 AA; 99468 MW; 1C19CC139EF756C8 CRC64;
MQEKYNPQKI ELGAQSYWDK TCAFSATEVQ GKKKYFCLSM FPYPSGKLHM GHVRNYTIGD
LLSRYHRMQG YNVLQPMGWD AFGLPAENAA IQNKVPPAEW TYDNINYMRK QLKSLGLAID
WDREFATCDQ DYYRWNQWLF LRMLEKGIAY KKTQVVNWDP VDQTVLANEQ VIDGRGWRTG
ALIERREIPG YYLGITQYAE ELLNGLDKLS GWPDRVKTMQ ANWIGKSFGV NITFPADAPA
NTLQAIKVFT TRADTLMGAT YVAVAAEHPI ALHAAKDNLE LSNFISECRN SVTMEADLAT
QEKKGLFTGL FVVHPLTGSK LPIWIANYVL MGYGEGAVMA VPAHDERDFE FAKKYSLPIK
QVISVPAKSQ SESHPEFSTD QWQEWYSSKK GVCVNSGKYD DMNFQAAVNA IALDLSALNL
GDKKTRFRIR DWGISRQRFW GCPIPLIHCN TCGVVPVPDE QLPVVLPENL VPDGSCNPLE
KMSSFYNCDC PKCGRTARRE TDTMDTFVDS SWYYIRYTCT DQNKSMTDSR TNYWLPVDQY
IGGIEHAILH LLYSRFWTKV MHNLGLVEFD EPFSDLLTQG MVLNEIFFRK EETGRITYFN
PADVDIQTDD QGKRSNAILR EDNNPVEFGG VGTMSKSKNN GVDPQKLVDK YGADTARLFI
MFASPPEQTL EWTDTGADGA FRFLNRLWNQ VYRHLQFGIV EPEISGNLSA ELKSFRFQLH
HTISKVSDDL GRRHTFNTAI AAVMELMNSL TKIHGSDKSS RSVIQEALEN IVLLLSPIVP
HICHTLWREL RPETELLDQP WPEADKKILV QDEIEMVVQV NGKLRGQIRV VKEAERETIE
QIALENEQVK KFVAGNEIKK IIVVPKRLVN IVI
//
