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SYL_BRUA4
ID   SYL_BRUA4               Reviewed;         877 AA.
AC   A6WXW1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=Oant_1095;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS13815.1; -; Genomic_DNA.
DR   RefSeq; WP_012091253.1; NC_009667.1.
DR   AlphaFoldDB; A6WXW1; -.
DR   SMR; A6WXW1; -.
DR   STRING; 439375.Oant_1095; -.
DR   PRIDE; A6WXW1; -.
DR   EnsemblBacteria; ABS13815; ABS13815; Oant_1095.
DR   KEGG; oan:Oant_1095; -.
DR   PATRIC; fig|439375.7.peg.1145; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; A6WXW1; -.
DR   Proteomes; UP000002301; Chromosome 1.
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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..877
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009384"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           628..632
FT                   /note="'KMSKS' region"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   877 AA;  98210 MW;  29A56EA8E314F5F4 CRC64;
     MAAERYNPRV AEAHWQKVWE EDRTFETDNS DSREKYYVLE MFPYPSGRIH MGHVRNYAMG
     DVVARYKRAK GFNVLHPMGW DAFGMPAENA AMQNKVHPKE WTYQNIATMR SQLKSMGLSL
     DWAREFATCD VEYYHRQQML FIDLFEKGLV TRKTSKVNWD PVDNTVLANE QVVDGRGWRS
     GALVEQRELT QWFFKITDFS EELLAGLDTL DQWPEKVRLM QRNWIGKSEG LQVRFTLDGK
     TAPEGFSEVE VYTTRPDTLF GAAFVGISAD HPLAKKLAEN NASLTGFIEE CHQHGTSLAA
     LETAEKKGFD TGVKVKHPFD ENWELPVYVA NFVLMEYGTG AVFGCPAHDQ RDLDFANKYK
     LKVTPVVMPK GEDAAGFSIG ETAYTDDGVM INSRFLDGMT PEAAFNEVAN RLEQTSLGNS
     PQASRKVQFR LRDWGISRQR YWGCPIPMIH CESCGVNPVP RADLPVKLPD DVEFDRPGNP
     LDRHATWRHV KCPKCGADAR RETDTMDTFV DSSWYYARFT APWENEPTDR KVADHWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMKVAGHVG IDEPFKGLFT QGMVVHETYK ANGQWVAPAD
     IRIEETDGKR SAALLSTGEP VEIGSIEKMS KSKKNVVDPD DIIASYGADT ARWFMLSDSP
     PERDVIWTEA GAEGAHRFVQ RVWRLVAEAA EHLKDVAPKT GTQGEALVVS KAAHKAVKAV
     GDDIEKLAFN RGVARLYELV NTAAASLQQV ASGNADDELK SAVRDVTEKL ILMLAPMMPH
     LAEQCLAVLG GKIAGRETLV ARSAWPEFDP ALVVENEIVM PVQINGKKRG DLTIARDADQ
     ASIQQAVLEL DFVKAALNGS SPKKVIVVPQ RIVNVVA
 
 
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