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SYL_SYNS3
ID   SYL_SYNS3               Reviewed;         867 AA.
AC   Q0IAE0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=sync_1375;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI47465.1; -; Genomic_DNA.
DR   RefSeq; WP_011619300.1; NC_008319.1.
DR   AlphaFoldDB; Q0IAE0; -.
DR   SMR; Q0IAE0; -.
DR   STRING; 64471.sync_1375; -.
DR   EnsemblBacteria; ABI47465; ABI47465; sync_1375.
DR   KEGG; syg:sync_1375; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001961; 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; 3.
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; Reference proteome.
FT   CHAIN           1..867
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334828"
FT   REGION          308..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   867 AA;  96742 MW;  88FE65741507DAF4 CRC64;
     MTAFSSPSSN AASSATDRYQ PLALEERWQA LWKEQRLYET QDPKPGQRAF YALSMFPYPS
     GTLHMGHVRN YVITDVIARV QRMRGDAVLH PMGWDAFGLP AENAAIERKI EPGVWTDSNI
     AQMRGQLGRL GLSIDWDREV ATCHSDYYRW TQWLFLELHA GGLAYQKDAT VNWDPVDQTV
     LANEQVDADG RSWRSGALVE KRDLRQWFLR ITDYADALLD DLDQLQGWPE RVRTMQANWI
     GRSIGAEIDF QVEAHPGTSI TVFTTRPDTL FGVSYLVLAP DHALVDQLTT SEERISVTAF
     RDLMAELSQD ERTSDDQPKR GVPTGAVAIN PANGKSIPIW IADYVLADYG TGAVMGVPAH
     DVRDFSFARQ HELPVQRVIE VSGTNEHVND GEAWAGPGTL IHSAGFSGLS NDEAKTAITN
     HGAENGWARA KRQYRLRDWL ISRQRYWGCP IPIIHCDDCG AVPVPRDQLP VELPTGIDLK
     GAGGSPLARA EDWVSVTCPK CGKPARRETD TMDTFMCSSW YYLRFADPHN RDLPFNATSV
     NRWLPVKQYV GGIEHAILHL LYARFFTKAL NDRDLLQTKE PFERLLTQGM VQGTTYRNPR
     TGRYISPAAV KDESNPLDPD DGGPLEVLFE KMSKSKHNGV DPAAVIDRYG ADTARMFILF
     KAPPEKDLEW DDADVEGQFR FLQRLWRLVD SEVNHDGVSP ATGESDSDIR RAVHQAIKAV
     SEDLSDDFQF NTAISELMKL SNSLSSGLAQ ASPGVRQEAM SALVRLLAPF APHLAEEFWQ
     RLGGEDSVHC QPWPDHDPEA LVLASIEVVI QVKGKVRGSM SVAADCSKEE LERLALASDV
     AQRWLEGKPP RRVIVVPGKL VNLVPSS
 
 
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