ID A0A1S9B102_9BACT Unreviewed; 927 AA.
AC A0A1S9B102;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=B0919_09185 {ECO:0000313|EMBL:OON69439.1};
OS Hymenobacter sp. CRA2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1955620 {ECO:0000313|EMBL:OON69439.1, ECO:0000313|Proteomes:UP000189843};
RN [1] {ECO:0000313|EMBL:OON69439.1, ECO:0000313|Proteomes:UP000189843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRA2 {ECO:0000313|EMBL:OON69439.1,
RC ECO:0000313|Proteomes:UP000189843};
RA Kabwe M.H., Vikram S., Govender N., Bezuidt O., Makhalanyane T.P.;
RT "Draft genome sequence of Hymenobacter sp. CRA2 isolated from the shrubland
RT biome in South Africa.";
RL Submitted (FEB-2017) 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}.
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:OON69439.1}.
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DR EMBL; MVBC01000004; OON69439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9B102; -.
DR STRING; 1955620.B0919_09185; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000189843; 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; 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 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 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:UP000189843}.
FT DOMAIN 12..145
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 279..460
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 777..890
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT BINDING 703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 927 AA; 105976 MW; 75A3B9F19647FF89 CRC64;
MPGYRPQEIE KKWQQFWQQN QTFRAQNHSD KPKYYVLDMF PYPSGAGLHV GHPLGYIASD
IVSRYKRHRG FNVLHPMGFD SFGLPAEQYA IQTGQHPALT TEKNIETYIR QLNLLGFSYD
WSREVRTSDP NYYKWTQWIF LKLFNSWYNL DTNKAESIRT LQEKFAAEGS QDVRAVCDAE
EVHDFSAGQW QMMTEAQKVA AVHPYRLAYQ SETYVNWCPQ LGTVLSNDEV KDGVSERGGY
PVERRLMPQW NLRITAYAER LLQGLDTIDW PDAVKEMQRN WIGRSVGAEV RFDVQNHPEL
PLTVFTTRPD TLFGVSYLAV APESELIDVL TTAEQREAVQ KYVEYAKNRS ERDRMADVKT
ITGEFTGAYA LHPFTQEPLP IWVADYVLAG YGTGVVMAVP AHDTRDFAFA QHFSLPIVPV
VEGYDEAAGE AYVAKEGRIF NSDFLNGLDV KPAIQAAIGR LEEMGIGTGK VNYRLRDAIF
GRQRYWGEPI PIYYRDGMAF GVAEEDLPLV LPEIDEYKPT ETGEPPLGRA QDWKYRGQFD
FELSTMPGWA GSSWYYLRYM DPKNDERFVG EEAEQYWHNV DLYMGGAEHA TGHLLYSRFW
HLFLKDLGLV TAAEPFQKLI NQGMILGRSN FVYRINGTNK FVSLGKKDQY DTTSLHVDIS
IVENDVLDPE AFRKWRPDYA SAEFILEDDG RYVCGWEVEK MSKNRFNVAS PDDLVERFGA
DVLRLHEMFL GPLEQYKPWN TQGMTGVLSF LRKLWRLFYP EDRDWAVTDE PATPAELKAL
HKAIRKAQED IERFSFNTSV STFMICVNEL SALNCRKRAI LEPLVVLISP YAPHLAEELW
EALGHEAGSL STAPFPEFNE AYLVEDTVNY PVAINGKVRE QMQFAASATA AEIEEAVRAT
DILARFAEGK PAKKVIVVPG RMVNVVV
//
