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SYY1_ENTFA
ID   SYY1_ENTFA              Reviewed;         418 AA.
AC   P0DM33; Q838D7; Q8KXD3;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Tyrosine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE   AltName: Full=Tyrosyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE            Short=TyrRS 1 {ECO:0000255|HAMAP-Rule:MF_02006};
GN   Name=tyrS1 {ECO:0000255|HAMAP-Rule:MF_02006}; Synonyms=tyrS-1;
GN   OrderedLocusNames=EF_0633;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80458.1; -; Genomic_DNA.
DR   RefSeq; NP_814387.1; NC_004668.1.
DR   RefSeq; WP_002355444.1; NZ_KE136527.1.
DR   AlphaFoldDB; P0DM33; -.
DR   SMR; P0DM33; -.
DR   STRING; 226185.EF_0633; -.
DR   EnsemblBacteria; AAO80458; AAO80458; EF_0633.
DR   GeneID; 60892922; -.
DR   KEGG; efa:EF0633; -.
DR   PATRIC; fig|226185.45.peg.2576; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_3_9; -.
DR   OMA; CINARYH; -.
DR   Proteomes; UP000001415; 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..418
FT                   /note="Tyrosine--tRNA ligase 1"
FT                   /id="PRO_0000234708"
FT   DOMAIN          350..416
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOTIF           39..48
FT                   /note="'HIGH' region"
FT   MOTIF           228..232
FT                   /note="'KMSKS' region"
FT   BINDING         34
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         166
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         170
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   418 AA;  47261 MW;  3136B3CBB783F9F8 CRC64;
     MNIIDELAWR DAINQQTNEE GLRELTENTS ISLYCGVDPT GDSMHIGHLI PFMMMKRFQL
     AGHHPYILIG GGTGTIGDPS GRTTERVLQT MEAVQHNVDS LSNQMKKLFG KDAEVTMVNN
     YDWLSELSLL DFLRDYGKNF NVNTMLAKDI VASRLESGIS FTEFTYQILQ SIDFYTLHKK
     HNIQLQIGGA DQWGNITAGL DLIRKKEGPE AKVFGLTIPL MLKADGTKFG KTAGGAIWLD
     PKKTSPFEFY QFWLNQDDRD VIKYLKFFTF LDKEEIDALA EKVEKEPGKR EAQRRLAEEV
     TRFVHDDAAL EEAQKISEAL FSGNIKDLTI EEIEQGLEHV PTVEITKDAK NIVDWLVDTE
     IEPSKRQARE DVSGGAISIN GDRVTDLDFA VDPTQHFDGK FVVVRKGKKN YFLAKVMD
 
 
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