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SYL_AROAE
ID   SYL_AROAE               Reviewed;         873 AA.
AC   Q5P252;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=AZOSEA24870;
GN   ORFNames=ebA4386;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI08612.1; -; Genomic_DNA.
DR   RefSeq; WP_011238298.1; NC_006513.1.
DR   AlphaFoldDB; Q5P252; -.
DR   SMR; Q5P252; -.
DR   STRING; 76114.ebA4386; -.
DR   PRIDE; Q5P252; -.
DR   EnsemblBacteria; CAI08612; CAI08612; ebA4386.
DR   KEGG; eba:ebA4386; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006552; 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   Gene3D; 3.40.50.620; -; 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   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..873
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091289"
FT   MOTIF           42..52
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   873 AA;  97432 MW;  17317CB2086C0B1F CRC64;
     MQDKYTPAAV EATAQQHWES TQAFKVAEDA GKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLARYHRMRG FNVLQPMGWD AFGMPAENAA IQNNVPPAKW TYANIDYMKT QLKRLGFALD
     WSRELATCKP DYYRWEQWLF TRLYQKGLIY KKLGTVNWDP VDETVLANEQ VIDGRGWRSG
     ALIEKREIPM YYMKITAYAD ELLEALDTLT GWPEQVKLMQ KNWIGRSEGV EVHFPYEVST
     IGASGVLKVF TTRADTLMGA TYVAVAAEHP LALQAAVNDP ELAAFIEECR HGGVAEADLA
     TMEKKGMPTG LRVVHPLTGE HLPVWIANYV LMGYGEGAVM AVPAHDERDF AFATKYRLPI
     RMVVRSTRDA YTDTVAPWQD AYAEQGRLVN SGKYDGLHFH DAIEAIAAEL TAKGLGAKRT
     QYRLRDWGIS RQRYWGCPIP MIHCADCGDV PVPDEQLPVV LPEDVAVTGR GSPLAKMPRF
     YECDCPKCGK PAKRETDTMD TFVESSWYFL RYASADNGQA MVDERVNYWA PVDQYIGGIE
     HAILHLLYSR FFTRAMRDEG LVNVSEPFTN LLTQGMVVAE TYYRDADGGK KQWINPADVE
     VERDEKGRIV AAKLTADGAP VVIGGIEKMA KSKNNGVDPQ ALVDQYGADT ARLFIIFAAP
     PDQQLEWSDS GVEGAYRFLR RVWSFGHAFV SEFRPQLPAD RQLDAVQLPE ALAAVRREIH
     VCLRQANYDF GKHQFNTVVS AAMKILNALE KAPRDVAAAH AQVAEEGLDI LLRLLAPITP
     HVAHALWQDC GFTGDVLHAS WPEPSEDALR QDEIDLVLQV NGKLRGSLRV AAGASNSAIE
     ALALGSETAQ KFMEGKPPRK VVVVPGRLVN IVV
 
 
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