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SYL_OCEIH
ID   SYL_OCEIH               Reviewed;         804 AA.
AC   Q8EP12;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=OB2307;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14263.1; -; Genomic_DNA.
DR   RefSeq; WP_011066700.1; NC_004193.1.
DR   AlphaFoldDB; Q8EP12; -.
DR   SMR; Q8EP12; -.
DR   STRING; 221109.22777992; -.
DR   EnsemblBacteria; BAC14263; BAC14263; BAC14263.
DR   KEGG; oih:OB2307; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q8EP12; -.
DR   Proteomes; UP000000822; 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; Reference proteome.
FT   CHAIN           1..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152057"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  91702 MW;  F0FFC32DBC4513FC CRC64;
     MSFQHRQIEK KWQDYWEDNK TFKTDTFSNK EKFYALDMFP YPSGQGLHVG HPEGYTATDI
     LARMKRMQGY EVMHPMGWDA FGLPAEQYAI DTGNSPAEFT NQNINTFKRQ IKELGFSYDW
     DREINTTDPN YYKWTQWIFK KLYENDLAYM DEVAVNWCPA LGTVLANEEV IDGKSERGGH
     PVIRKPMKQW MLKITAYADR LLEDLNELDW PDSLKEMQRN WIGRSEGAEV TFSIKGNEGT
     FTVFTTRPDT LFGATYAVVA PEHPLVKEIT TLSQKEAVQN YLDEIQTKSD LERTDLAKDK
     TGVFTGAYAI NPVNGEEMPI WVADYVLMSY GTGAIMAVPA HDERDYEFAN TFGLPIKEVV
     AGGNIDDEAY TGDGEHVNSE FLNGLGKEEA ITKMIDWLEA NGSGEKKITY RLRDWLFARQ
     RYWGEPIPII HWEDGTMTAV PDEDLPLTLP QVAEIKPSGT GESPLANNTD WVNVVDPETG
     LKGRRETNTM PQWAGSCWYF LRYIDPNNTE RLADPKALEE WLPIDIYIGG AEHAVLHLLY
     ARFWHKFLFD IGVVSTKEPF QKLYNQGMIL GEGNEKMSKS KGNVVNPDDI IDSHGADTLR
     LYEMFMGPLD ASVAWSTNGL DGSRRFLDRV WRLYVGDDGS LTDKIIDDES TELDKIYHET
     VKKVTDDFEH MHFNTGISQM MVFINECYKA NKIPKIYAEG FVKLLSPVAP HLSEEIWQKL
     GHSESISKAT WPAYDESKLV EDEVEVVLQI MGKVRSKIQV PVDISKDDLE KAALDDESMQ
     KWLEGKTIRK VIVVPGKLVN IVAN
 
 
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