位置:首页 > 蛋白库 > SYL_HELPY
SYL_HELPY
ID   SYL_HELPY               Reviewed;         806 AA.
AC   P56457;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=HP_1547;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000511; AAD08585.1; -; Genomic_DNA.
DR   PIR; C64713; C64713.
DR   RefSeq; NP_208338.1; NC_000915.1.
DR   RefSeq; WP_000345715.1; NC_018939.1.
DR   AlphaFoldDB; P56457; -.
DR   SMR; P56457; -.
DR   DIP; DIP-3469N; -.
DR   IntAct; P56457; 1.
DR   MINT; P56457; -.
DR   STRING; 85962.C694_08015; -.
DR   PaxDb; P56457; -.
DR   EnsemblBacteria; AAD08585; AAD08585; HP_1547.
DR   KEGG; hpy:HP_1547; -.
DR   PATRIC; fig|85962.47.peg.1662; -.
DR   eggNOG; COG0495; Bacteria.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; P56457; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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; 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; 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; Reference proteome.
FT   CHAIN           1..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152026"
FT   MOTIF           38..48
FT                   /note="'HIGH' region"
FT   MOTIF           572..576
FT                   /note="'KMSKS' region"
FT   BINDING         575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  93164 MW;  731807226C288678 CRC64;
     MDFINIEKKW QEFWWKNKSF EPKDDFNLPK KYILSMLPYP SGEIHMGHVR NYTIGDALAR
     YYRLHHYNVL HPMGFDSFGM PAENAAIKHG IHPKTWTYEN IENMQKEFEA LGFSFSKNRE
     FATSDPDYTK FEQRFFIDLW EKGLIYRKKA MLNWCPNDKT VLANEQVIDG RCWRCDTEVI
     QKELYQYYLK ITNYAEELLK DLEALEDHWP SQVLIMQKNW IGKSSGLQFG FKIADECLKA
     CNGIQEIEVF TTRADTIYGV TYIAIAPEHP LVEHAIKQVS QEVSKMIKAI LNTTQRERAL
     EKKGAFLGIY AIHPLTKQKI PVWVANFALA NYGSGALMGV PACDERDFEF ANLYHIPIKV
     ITQSPQNLPH TKEEVLKNSG EWSDLSSSVA REQIIAYFEK ENLGKRVINY RLQDWGVSRQ
     RYWGAPIPMI HCNHCGIVPE TQLPVTLPED IVIDGEGNPL EKHASWKFTQ CPKCHKNALR
     ETDTMDTFIQ SSWYFLRYTT PKNQRENQAF DQNYLKYFMP VDTYIGGIEH AILHLLYARF
     FTKALRDLGY LHLDEPFKQL ITQGMVLKNG AKMSKSKGNV VSPKEILKKY GADAARLFIL
     FAAPPAKELE WNDSALEGAH RFIKRLYDKA NAINPTTSKP EFKEVSLNEA QKLGRKKVYE
     ALKKSHEIFN KAESAYSFNT LIASCMEALN ALSAQNNERI LCEGYFVLLQ ILEPIIPHTA
     WELSERLFKR ENFKPIAIDE DALMEDFMTL GLTINGKRRA ELKVNINASK EEIIVLAKKE
     LEKYLENASV KKEIYVPNKL VNFVIA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024