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Database: UniProt
Entry: A3U6X8_CROAH
LinkDB: A3U6X8_CROAH
Original site: A3U6X8_CROAH 
ID   A3U6X8_CROAH            Unreviewed;       944 AA.
AC   A3U6X8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   28-JAN-2026, entry version 120.
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   OrderedLocusNames=CA2559_04530 {ECO:0000313|EMBL:EAP87995.1};
OS   Croceibacter atlanticus (strain ATCC BAA-628 / JCM 21780 / CIP 108009 / IAM
OS   15332 / KCTC 12090 / HTCC2559).
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceibacter.
OX   NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP87995.1, ECO:0000313|Proteomes:UP000002297};
RN   [1] {ECO:0000313|EMBL:EAP87995.1, ECO:0000313|Proteomes:UP000002297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC   {ECO:0000313|Proteomes:UP000002297};
RX   PubMed=20639333; DOI=10.1128/JB.00733-10;
RA   Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT   "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL   J. Bacteriol. 192:4796-4797(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC         diphosphate; 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:ARBA00047469, 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}.
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DR   EMBL; CP002046; EAP87995.1; -; Genomic_DNA.
DR   RefSeq; WP_013186671.1; NC_014230.1.
DR   AlphaFoldDB; A3U6X8; -.
DR   STRING; 216432.CA2559_04530; -.
DR   GeneID; 89452697; -.
DR   KEGG; cat:CA2559_04530; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002297; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   FunFam; 3.40.50.620:FF:000056; Leucine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000060; Leucine--tRNA ligase; 1.
DR   FunFam; 1.10.730.10:FF:000011; Leucine--tRNA ligase chloroplastic/mitochondrial; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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:UP000002297}.
FT   DOMAIN          39..146
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          278..462
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          713..745
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          792..907
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   944 AA;  108066 MW;  40F39EA51ED94931 CRC64;
     MSNYHFNEIE KKWQQYWSKN GTFHASNTSE KPKYYVLDMF PYPSGAGLHV GHPLGYIASD
     IYARYKRHKG FNVLHPQGYD SFGLPAEQYA IQTGQHPRIT TEENIKTYRR QLDQIGFSFD
     WSRELRTSEP EFYKWTQWIF TELFNHYYDN DSDKAESIES LIKRFETEGN SNVNAVCDAD
     TETFSAEEWS NYSEKEQADI LLKYRLTYLA ESEVNWCPEL GTVLANDEIV NGVSERGGFP
     VVRKKMTQWS MRISAYAERL LQDLNDIDWP EPLKESQRNW IGKSIGAHVD FKVKGHNEKI
     GVFTTRPDTI FGVTFMTLAP EHELVAKLTT PKQKDAVEAY IEKTAKRSER ERMADVKTIS
     GVFTGAYAEH PFTKEPVAIW IGDYVLAGYG TGAVMAVPCG DQRDYDFANH FAGQEGMTPI
     VNIFKDVDVS EEAFADKEKT IITNSNFLND LPYKKAMKLA IYKLEEQGSG QGQTNYRLRD
     AVFSRQRYWG EPFPVYYKNG IPQMIEEKHL PITLPEVEKY LPTEEGEPPL GRADVWAWNT
     ENAQVVSNDL VNSDTVFPLE LNTMPGWAGS SWYFFRYMEK AMRNETFASK DAMNYWQEVD
     LYIGGSEHAT GHLLYARFWT KFLYDIKAVP VKEFAKKLIN QGMILGTSAF VYRKEETNVF
     ISKNLIGDEN VQPIHADVSM VNASSELDLE AFKAWRPEFK DAEFILEDNK YIVGHEVEKM
     SKSKYNVVNP DDICAQYGAD TLRLYEMFLG PLEQAKPWNT AGITGVHSFL KKLWKLYHNG
     ENFEVTDAEP NKESLKTLHK TIKKVEEDIE NFSFNTSVST FMIAVNELSS QKCNSRAILE
     PLAVLISPYA PHIAEELWEK LGHSTSIATA EFPKFEEKHL VESSKAYPIS FNGKMRFTME
     LPLDLSKDDI EKAVMAHEKT AGYLDGRTPK KVIVVPGKIV NIVG
//
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