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SYL_SINMW
ID   SYL_SINMW               Reviewed;         876 AA.
AC   A6UEE2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Smed_3198;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000738; ABR62022.1; -; Genomic_DNA.
DR   RefSeq; WP_012067403.1; NC_009636.1.
DR   RefSeq; YP_001328857.1; NC_009636.1.
DR   AlphaFoldDB; A6UEE2; -.
DR   SMR; A6UEE2; -.
DR   STRING; 366394.Smed_3198; -.
DR   EnsemblBacteria; ABR62022; ABR62022; Smed_3198.
DR   GeneID; 61610780; -.
DR   KEGG; smd:Smed_3198; -.
DR   PATRIC; fig|366394.8.peg.6436; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001108; 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   Gene3D; 3.90.740.10; -; 1.
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; 2.
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..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009434"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   876 AA;  98092 MW;  4AF876E12CEFBBBC CRC64;
     MATERYNPRD AEPRWQQQWE AGKIFETKND DPREKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARYKRAR GFNVLHPMGW DAFGMPAENA AMERGVHPAS WTYQNIASMK AQLKVMGLSL
     DWSREFATCD PEYYQRQQHL FLDFLEKGLV YRKQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFRITDFS QDLLDSLDTL DEWPEKVRLM QKNWIGRSEG LSVRWELDPA
     TVPGEEKELT VYTTRPDTLF GASFLAISAD HPLARDAAAK SAEIEAFCEE CRRAGTSLAA
     LETAEKMGID TGIRARHPFD PDWELPVYVA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYG
     LPVVPVVMPK DADPQTFTIG DEAYVGDGVM INSRFLDGLS TEEAFETIAT RLEKDLLNGT
     PRAERKVNFR LRDWGISRQR YWGCPIPVIH CDDCGVVPVP KTDLPVTLPP DVTFDKPGNP
     LDRHPTWRHV ACPQCGKDAR RETDTMDTFV DSSWYFTRFT APWEDGPTDP KAANHWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMKATGHVA LDEPFKGLFT QGMVVHETYS RGEGAQREWI
     TPAEIRIEEA DGQRRAVHIE TSEEIAIGSI EKMSKSKKNV VDPDDIIASY GADTARFFVL
     SDSPPDRDVI WSEAGVEGAH RFVQRVWRLL SEAAEGLSAA EAAPAREGEG LAVSQAAHRT
     LKAVEADYDK LAFNKAVARI YELVNTLAAP LAQIAAGKAD QALTAAVKDA AGILISLIAP
     MMPHLAEECW RAIGGKGLIA ERPWPKFDAT LVVENEITLP VQINGKKRAD LTIARDADQS
     AIESAVLALD VVKTALNGSN PKKIIVVPQR IVNVVV
 
 
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