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SYL_BORAP
ID   SYL_BORAP               Reviewed;         840 AA.
AC   Q0SNR0; G0IR93;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=BAPKO_0261, BafPKo_0253;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(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; CP000395; ABH01518.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69479.1; -; Genomic_DNA.
DR   RefSeq; WP_011600919.1; NC_017238.1.
DR   AlphaFoldDB; Q0SNR0; -.
DR   SMR; Q0SNR0; -.
DR   STRING; 390236.BafPKo_0253; -.
DR   EnsemblBacteria; AEL69479; AEL69479; BafPKo_0253.
DR   KEGG; baf:BAPKO_0261; -.
DR   KEGG; bafz:BafPKo_0253; -.
DR   PATRIC; fig|390236.22.peg.247; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000005216; 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; 1.
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.
FT   CHAIN           1..840
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009299"
FT   MOTIF           44..55
FT                   /note="'HIGH' region"
FT   MOTIF           617..621
FT                   /note="'KMSKS' region"
FT   BINDING         620
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   840 AA;  98167 MW;  B488A7FF899B0BB3 CRC64;
     MSKYEFIKIE KKWQEFWDNN KTYKVIEDPN IPKEKRLYIL DMFPYPSANG LHVGHPEGYT
     ATDIFARYKI LNGFHVLHPI GFDSFGLPAE NYAIQTGTHP KKSTEENINK FKKQIKALGF
     AYDWDREIRT HDENYYKWTQ WIFLQLYKKG LAYAKEMPVW YCPELGTVLA NEEIIQTPNG
     PKSERGFHNV EKKYLRQWVL KITKYAERLL NDLEELEWPE SVKEMQRNWI GKSTGVEIDF
     EIEGYNDKIK VFTTRPDTIF GITYLVIAPE NKLVEKITKD NFKSNVLKYI KQEELKSDLK
     RTSLEKDKSG VFTGSYAFHP ITNVKIPIWV GSYVLGTYGS GAVMGVPAHD ERDFQFAKKY
     KLKILPVISK SGKNEILEKA FINDGISINS PDEFNNLKNS EVKDKVIKWL TKNKKGKETV
     TYKLRDWVFS RQRYWGEPIP ILFDKLGNAI PLEKNDLPLK LPETANYKPS GTGESPLSRI
     KNWVNVKDTD FTRETNTMPQ WAGSCWYYLR YLDPKNSKEF ANHKKIEYWM PVDLYIGGAE
     HTVLHLLYSR FWHKVLYDLG HVNTKEPFKK LINQGIITAF SYQKENGVLI PNDQVIEKDN
     KFFDKKDNKE VTQVIAKMSK SLKNVINPDG IIKEFGADSI RIYEMFMGPL TDSKPWNTKG
     IIGVFRFLNK IWNLREKELS KDNPPKEIMS QLHKVIKKVT EDTEKLNFNT AISAMMIFIN
     ELSKYEKNYL NIFKPFIIIL SPYAPHLAEE LWEYIGETPS LFKNSKWPKF DETLIIKETK
     EIVLQINGKI KDKILLNKET DEEELKEIAM ENSKIKSNLF NKKIVKIIVI KNKLVNIVIK
 
 
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