ID   SYL_PSYA2               Reviewed;         921 AA.
AC   Q4FU71;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=Psyc_0576;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; CP000082; AAZ18437.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4FU71; -.
DR   SMR; Q4FU71; -.
DR   STRING; 259536.Psyc_0576; -.
DR   KEGG; par:Psyc_0576; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000546; Chromosome.
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   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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..921
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334797"
FT   MOTIF           80..90
FT                   /note="'HIGH' region"
FT   MOTIF           667..671
FT                   /note="'KMSKS' region"
FT   BINDING         670
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   921 AA;  103244 MW;  A3E4AA9983B25748 CRC64;
     MLWHYKISPH LSVITNSEPT MSNAVTAETA NTNNTSIENA QYQPQLIEAA QQAKWATDKR
     FEVSNEPSDK PSRYMLSMFP YPSGKLHMGH VRNYTISDVL SRYYRLKGYE VMQPMGWDGF
     GLPAENAAIA NQTPPAKWTF ENIDSMRAQL KLLGLSIDWS REFATCSPEY YQWEQWLFLQ
     LYKKGLVYKK LATVNWDPID NTVLANEQVI DGKGWRSGAM VEKRDIPMYY FNITDYADEL
     LDDLDQLEGH WPSEVITMQR NWIGRSSGME VHFPYELAGE SNSLDVFTTR PDTLMGVTYV
     AVAAEHPLAQ YASEHNEAIA AFCALCKKGS VAEADLAKAE KVGIDTGLTV THPLTGEEVP
     VWVANYVLMS YGSGAVMAVP AHDERDYEFA TKYSLPIKQV IDIPARYFDD IEEGNDNRAY
     TERNTLVNSG EFDGMDFEQA FAAMLAKLEP QSLAKKKIQY RLRDWGVSRQ RYWGCPIPMV
     NCEHCGTVPV EEQDLPVILP TDVVPDGRGN PLKNIPEFVN TTCPKCGNPA ERETDTFDTF
     VESSWYYARF ASPNDTTNMV NKSAANKWLP VDQYIGGVEH AVMHLLYARF FHKLMRDENL
     VSGDEPFANL MTQGMVLAGT FYRVNPDGST TYYFTKDIDI DFNERGQPIK AILKSDGQPV
     TIGKIEKMSK SKNNGVDPQI TIDKYGADTV RLYTLFTAPA DQTLEWSDDA LKGPYNFVKK
     VWRIASEHMQ ALTAANLSLD TLNNGTLNND ALNTEGLSKE AKALRRKTHE TIGKIDSDLG
     KRLALNTPVS SLMELANELS NFKANSEQEL QVQHEALIDL LIMLSVYAPH IGEHLLEQLG
     LDTVTLNYPA VDESALVQDM ITMVIQVNGK MRGKMDVAPN SDPEALKAQA RAIEGVAKFL
     TGEIKKEIVV PNKLVNIVVA G
//