ID A0A136MRE5_9BACT Unreviewed; 946 AA.
AC A0A136MRE5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=UZ09_BCD002002540 {ECO:0000313|EMBL:KXK36396.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK36396.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK36396.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK36396.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-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:RU363039}.
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:KXK36396.1}.
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DR EMBL; LNBW01000079; KXK36396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MRE5; -.
DR STRING; 1617420.UZ09_BCD002002540; -.
DR PATRIC; fig|1617420.3.peg.2701; -.
DR Proteomes; UP000070267; 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 CDD; cd00812; LeuRS_core; 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}.
FT DOMAIN 38..144
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 276..456
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 798..906
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 719..723
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 946 AA; 108857 MW; A58E1881779C1F22 CRC64;
MLYHPENIEA KWRKEWKKTG LYKVSNHSNK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
FARYKRLKGF NVLHPMGYDA FGLPAEQYAI QTGVHPANST ETNVNRYREQ LDNIGFSFDW
NREVRTSDPS YYKWTQWIFL KLFNHYYDLV TQKAAPISEL IKIFETSGNF HLQVANSQDA
TFTAEEWKVM SDKEKDAVLM NYRLAYRKIG YVNWCEALGT VLANDEVKDG LSERGGYPVE
KKAMMQWSLR ITAYAERLLA DLDTLEWTDA LKAMQRNWIG KSEGAQLFFE VAQSHQKIEI
FTTRPDTIFG STFMVLAPEH DLVDILVTTD QAETVKSYKE YVASRSDVDR MSEIKEVTGV
FTGAYATNPF TGKNVPIWLG EYVLKDYGTG AIMAVPGDDE RDYNFAKKFG LEIIDIVDRT
DYPNAAPHEK VGKMINSDFL TGMEVKDAIT AMLNKIEERG IGTRKTNYKL RDANFSRQRY
WGEPFPIMYN HNGVAIPLTT QQLPLILPQL ENFKPAPGGK SPLVRVESWV NQFEGFQLET
DTMPGFAGSS WYFLRYMDPD NKDNFASEQA LNYWQDVDLY VGGTEHAVGH LMYSRFWHKF
LYDLGYVPTT EPFKKLINQG MITAYGYYAD HLKMPDGSIL TGNIKDLVNI DEITAGNPVR
LSYIYDYLDS QNRITQSKFK EYWEHIGKDY HVDGNLSKYF WITEDGSEPY FTVNIVQEKM
SKSKFNVQNP DEIVARYGAD CFRMYEMFLG PIEQSKPWDT KGIDGVNRFL RKYWALYFNN
NEWSVSDEKP TGEEYKILHT AIKKITDDIE RFSFNTCVSA FMMCVNELKR IECNNRTILN
SLNILLAPFA PFITEELHHL LGNDGSVHEA AYPEYDEQHM IQDAVEYPVC VNGKKRDVIA
VASSMTPKEI QDYVMTLDAV KRHVGDKAVQ RVIVVPGKMI NLVVKE
//
