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SYY_LACDA
ID   SYY_LACDA               Reviewed;         421 AA.
AC   Q1GBW9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=Ldb0256;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC   11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC       step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC       then transferred to the acceptor end of tRNA(Tyr). {ECO:0000255|HAMAP-
CC       Rule:MF_02006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02006};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
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DR   EMBL; CR954253; CAI97096.1; -; Genomic_DNA.
DR   RefSeq; WP_011543583.1; NZ_JQAV01000030.1.
DR   AlphaFoldDB; Q1GBW9; -.
DR   SMR; Q1GBW9; -.
DR   STRING; 390333.Ldb0256; -.
DR   PRIDE; Q1GBW9; -.
DR   EnsemblBacteria; CAI97096; CAI97096; Ldb0256.
DR   KEGG; ldb:Ldb0256; -.
DR   PATRIC; fig|390333.7.peg.231; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_3_9; -.
DR   OMA; YHSSVQA; -.
DR   BioCyc; LDEL390333:LDB_RS01070-MON; -.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00165; S4; 1.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   Pfam; PF01479; S4; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..421
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_1000088595"
FT   DOMAIN          353..419
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOTIF           43..52
FT                   /note="'HIGH' region"
FT   MOTIF           231..235
FT                   /note="'KMSKS' region"
FT   BINDING         38
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         169
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         173
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   421 AA;  47550 MW;  5A40A76564B2FB2C CRC64;
     MANFDILEDL KWRGAINQET DEEGLRDYLA KHDDLALYCG TDPTGDSLHI GHLIPFMILK
     RFQLAGYKPV IVIGGGTGSI GDPSGRSTER VLQSEETIKH NEEALTAQMV KLFGTENFRI
     VNNRDWLGKM NLLEFLRDYG KLFQVNNMLN KEVVASRLKN GISFTEFSYQ ILQAIDFYIL
     NRDHCVQMQI GGADQWGNIT AGIDLIHRLE GADRPAFGLT IPLMLKADGT KFGKSAGGAV
     WLDPEKTSPY EFYQFWINQD DRDVIKYLKY FTFLKHEEID ALEEKVKTEP WKREAQKRLA
     EEVTKFVHGE EGLKEAQTVT EALFSGNVKD LTTKQVEIAL AKAPSAESGA EKKNLVDFLV
     DTKIESSKRQ AREDVNNGAI YVNGDRIQDT DFEVDPAAAF DGKFVIIRKG KKKYTLVHIK
     G
 
 
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