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SYL_ALKMQ
ID   SYL_ALKMQ               Reviewed;         824 AA.
AC   A6TQK3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-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=Amet_2314;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR48471.1; -; Genomic_DNA.
DR   RefSeq; WP_012063446.1; NC_009633.1.
DR   AlphaFoldDB; A6TQK3; -.
DR   SMR; A6TQK3; -.
DR   STRING; 293826.Amet_2314; -.
DR   EnsemblBacteria; ABR48471; ABR48471; Amet_2314.
DR   KEGG; amt:Amet_2314; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001572; 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; 2.
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..824
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091285"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   824 AA;  95056 MW;  7CAF3459E6CB80F7 CRC64;
     MAIYDFGNIE KKWQERWQEN KAFSIIERDR PKYYVLEMFP YPSGKIHMGH VRNYSIGDVV
     ARFKRMKGYN VLHPMGWDSF GLPAENAAIK HGIHPDHWTK ENVKEMKEQL DALGLSYDWD
     REVSTCTPEY YKWTQWLFLQ FYHKGLAYKK ESQVNWCPSC ETVLANEQVV NGGCDRCDSS
     VGKKNLNQWY FKITDYAEAL LEDIKLLDGW PEKVKTMQQN WIGKSHGAEI DFPIENTSKE
     LKVFTTRPDT IYGATYMVLA PEHPYVMELV KETEYEEAVV AFRNKLQHMS DIERTSTEIE
     KEGIFIGKYC INPVSNEKIP IYIANYVLAD YGTGAIMAVP AHDQRDLDFA RKYDITVTPV
     IRPIDESDGF DIEKEAYTDS GIMINSEKFN GLDSEKAYED IAKHIETLNA GKRTINYRLR
     DWLLSRQRYW GTPIPIIYCD DCGIVPVREE ELPVKLPVDV TFSGKGSSPL ETSEGFLNTN
     CPSCGKMAKR ETDTMDTFVD SSWYFLRYTD ANNEQLPFSK EAANYWVPVD QYIGGVEHAI
     LHLLYSRFFT KVMKDLGLTD QPEPFKKLLT QGMVLKDGAK MSKSKGNVVS PEEIIQKYGA
     DTARLFVLFA APPERDLEWS DQGVEGSYRF LNRVWRLAEE FIDNNLFMST SLGEALTKRD
     KDLKYTIHYT IKKVTSDVED RFNFNTAISA VMELINELYK YKETDPSKLN GDLFREGIET
     SILLLAPFAP HFTEELWEKL GKAESVHMTN WPEYDHEAII KDEVEIVMQV NGKVKDRMMV
     PTNVSKEELE SLAMKNEKII QIIEGKQIIK IIAVPKKLVN IVIK
 
 
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