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Database: UniProt
Entry: B9D3P2_CAMRE
LinkDB: B9D3P2_CAMRE
Original site: B9D3P2_CAMRE 
ID   B9D3P2_CAMRE            Unreviewed;       823 AA.
AC   B9D3P2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 85.
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   ECO:0000313|EMBL:EEF13387.1};
GN   ORFNames=CAMRE0001_0461 {ECO:0000313|EMBL:EEF13387.1};
OS   Campylobacter rectus RM3267.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF13387.1, ECO:0000313|Proteomes:UP000003082};
RN   [1] {ECO:0000313|EMBL:EEF13387.1, ECO:0000313|Proteomes:UP000003082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM3267 {ECO:0000313|EMBL:EEF13387.1,
RC   ECO:0000313|Proteomes:UP000003082};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (AUG-2008) 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: 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:EEF13387.1}.
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DR   EMBL; ACFU01000021; EEF13387.1; -; Genomic_DNA.
DR   RefSeq; WP_004320388.1; NZ_ACFU01000021.1.
DR   AlphaFoldDB; B9D3P2; -.
DR   STRING; 553218.CAMRE0001_0461; -.
DR   eggNOG; COG0495; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000003082; 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   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-RELATED; 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; 2.
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..183
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          224..415
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          548..634
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          671..788
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   823 AA;  94055 MW;  F288A0D44123D088 CRC64;
     MSEILKYEPS KIEKKWQEIW NKSGEFEPKD DYSLPKKYIL SMFPYPSGRI HMGHVRNYTI
     GDALARYYRK RGYNVLHPIG FDSFGMPAEN AAIKHKIHPK IWTYENIDYM RGELEALGLS
     FSKKREFATS DPLYTKFEQE FFIKMYEKGL VYRKSAVVNW CEFDQTVLAN EQVEDGCCWR
     CGNAVIQREL PGYYLKITDY AQELLDDLKR LEGKWPSQVL TMQENWIGKS FGLEFKFELD
     EESKGILEGG EQIDGFEVFT TRPDTIYGVS YTALAPEHKI VKRILDSGKL EAAKAERIRK
     ILNQSPRERQ ASEKDGLYLG INVLHPLTGE KVPVWVANFV LADYGSGAVM AVPAHDERDY
     EFASKFGLPI KQVIKPAQGE FEDAKAFTEY GISINSPLIN GLGSEEAKLK IIEKFEADKI
     GKRVVNFKIR DWGISRQRYW GAPIPIVHCK CCGVVPEKIE NLPVTLPDDV QITGEGNPLD
     KHESWKHVKC PKCGGEAIRE TDTMDTFFES SWYFARYASD EKTWQERAFD AKSVNYWMNV
     DQYIGGIEHA ILHLLYARFF QKALRDLSYL RDDEPFERLL TQGMVLKDGK KMSKSKGNVV
     DPDDIINKYG ADTARLFILF AAPPQKELEW NDSAVEGAFR FINRLYERSA GIKKCTQIPQ
     IAHANLSKEE KYARMKVYEA LKKSSDVYEE NFTFNTLIAA CMEALNAVNA QDNQDVTTEA
     FFIILNLLEP IVPHVANELS EQLFGRANFT KIEILDEVFE KDSLNLAITV NGKRRGEFEV
     PSSASEDEVL ALAGQCAAKW LEGKEIIKQI YVSGKLVNFV IKG
//
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