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SYL_VESOH
ID   SYL_VESOH               Reviewed;         815 AA.
AC   A5CY09;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=COSY_0005;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Vesicomyosocius.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA   Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT   clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
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; AP009247; BAF61144.1; -; Genomic_DNA.
DR   RefSeq; WP_011929414.1; NC_009465.1.
DR   AlphaFoldDB; A5CY09; -.
DR   SMR; A5CY09; -.
DR   STRING; 412965.COSY_0005; -.
DR   PRIDE; A5CY09; -.
DR   EnsemblBacteria; BAF61144; BAF61144; COSY_0005.
DR   KEGG; vok:COSY_0005; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000247; 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; 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   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..815
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009461"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           571..575
FT                   /note="'KMSKS' region"
FT   BINDING         574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   815 AA;  95149 MW;  98F196937EC5C85E CRC64;
     MNIKYDVQKI EKQAQKYWKE KKSFEVIEDY SKEKYYCLSM FPYPSGRLHM GHVRNYSIGD
     VISRFQRMQG KNVMQPIGWD GFGLPAENAA LKNKESPAKW TYKNINYMKT QLNQLGFGYD
     WAREITTCHP KYYRWEQWLF IKLFKKNLIY KKKAIVNWDP VDQTVLANEQ VINGRGWRSN
     ALIEKKEISQ WFIRITNYAE ELLNDLDKLY GWPDPVKIMQ KNWIGKSIGL EITFSRRNSD
     PLIIYTTRPD TLMGVTYLAI SFEHPLALES GKNNYQVQSF IEKCKTIQTS EILNEIMDKK
     GIDSGFKCIH PITNNEVPIW ITNFVLMSYG TGAIMSVPAH DKRDFKFAKK YGIFIKQVIN
     KNESIDKGPI INKGKLFNSE EFSGMDFNQA YESIAKTLIE KNLGNKKINY RLRDWGISRQ
     RYWGCPIPIV NCKYCGSVTV KVKDLPVILP EKVKFYDVSS PIKKMPNFYQ TICPKCGSKA
     HRETDTFDTF FESSWYFARH TCNNNNNAML DKRVNYWLEV DQYIGGVEHS ILHLLYARFF
     NKLLRDEGLI KYDEPFKNLL TQGMVLKNGV KMSKSKGNTV DPTKMIKKYG ADTVRLFILF
     AAPPMQDLEW NNSGLEGAHR FIKKVYRLVS IYINDSKDYI VNHLNINFLN KTQKHIRRKI
     HQNLVKITDD INRRYTFNTA ISTLMESVDI INKFTKTDTQ SIALRSESIN IILLTLSPIT
     PHICHYLWLK LGNKKAIINE PWPKVDLKAL IESEVQIIIQ VDGKLRDKMM MMINTDKEIL
     ESEVLSNKNI IKFTKNKNII KIIIIHNKLI NIVTK
 
 
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