GenomeNet

Database: UniProt
Entry: A0A0Q9JZH4_9MICO
LinkDB: A0A0Q9JZH4_9MICO
Original site: A0A0Q9JZH4_9MICO 
ID   A0A0Q9JZH4_9MICO        Unreviewed;       857 AA.
AC   A0A0Q9JZH4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=ASG80_15815 {ECO:0000313|EMBL:KRE30739.1};
OS   Agromyces sp. Soil535.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=1736390 {ECO:0000313|EMBL:KRE30739.1, ECO:0000313|Proteomes:UP000051793};
RN   [1] {ECO:0000313|Proteomes:UP000051793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil535 {ECO:0000313|Proteomes:UP000051793};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE30739.1, ECO:0000313|Proteomes:UP000051793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil535 {ECO:0000313|EMBL:KRE30739.1,
RC   ECO:0000313|Proteomes:UP000051793};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:RU363035}.
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:KRE30739.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMRW01000002; KRE30739.1; -; Genomic_DNA.
DR   RefSeq; WP_056728611.1; NZ_LMRW01000002.1.
DR   AlphaFoldDB; A0A0Q9JZH4; -.
DR   STRING; 1736390.ASG80_15815; -.
DR   Proteomes; UP000051793; 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; 3.10.20.590; -; 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}.
FT   DOMAIN          51..192
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          233..444
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          458..659
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          696..817
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           621..625
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         624
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   857 AA;  95021 MW;  6BDD3F76E1685BA6 CRC64;
     MAHDQDQANA DAGAYDFAAL QAKWLPVWDE LRPFRAGRPG EKKPRKYILD MFPYPSGDLH
     MGHAEAFGYG DTVARYWRHQ GFDVLHPVGW DSFGLPAENA AIKRGVDPRA WTYENIEQQK
     RSFRQYAPSF DWSRELHTSD PEYYRWNQWL FLKLYEKGIA YRKAGLVNWC PVDLTVLANE
     QVVDGHCERC GAVVTKKALT QWYFRVTDYA DRLLDDLNQL EGSWPSKVVT MQRNWIGRSS
     GADVEFAIEG RDEPVSVFTT RPDTLYGATF MVVAPDSEIA VELAAGASAE VQARFQDYLD
     SVRAESDIDR LSTERPKTGV FLERYAVNPV NGERLPIWAA DYVLADYGHG AIMAVPAHDQ
     RDLDFARAFE LPVRVVVDTN APVTGVIPVI KLDENGDPIL PDEVPPSDPA STGVALAGEG
     RLINSGPLDG LSKSNAIRRI IEILEQRGTG HAAKNFRLRD WLISRQRYWG TPIPIIHCPD
     CGEVPVPEAD LPVRLPDAAG LDLKPKGASP LGAAEDWVNV ACPNCGGAAR RDSDTMDTFV
     DSSWYYLRYL DPSDETQAFD MAEAEKWMPV DQYVGGVEHA ILHLLYSRFV TKVLFDLGYL
     SFTEPFTSLL NQGMVIMDGS KMSKSKGNLV EFASELGAHG ADALRVTLAF AGPPEDDIDW
     ADVSPVGAAK FLARAWRISG EVTSSPEVEW KTGDTSLRRM THRLLADAPA LIEAFKFNVV
     VARLMELVNA TRKTIDSGAG PADAAVREAS EVTAMILDLF APYTAEDMWQ RLGYQPSVAL
     VPWRKADPAL LVEESVTAIV QVDGKVRDRL DVSPKISGEE LEALARESAG VARAIGEREI
     ANVIVRAPRL VNIATRR
//
DBGET integrated database retrieval system