位置:首页 > 蛋白库 > SYY1_BACSU
SYY1_BACSU
ID   SYY1_BACSU              Reviewed;         422 AA.
AC   P22326;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   03-AUG-2022, entry version 145.
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}; OrderedLocusNames=BSU29670;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1735721; DOI=10.1128/jb.174.4.1299-1306.1992;
RA   Henkin T.M., Glass B.L., Grundy F.J.;
RT   "Analysis of the Bacillus subtilis tyrS gene: conservation of a regulatory
RT   sequence in multiple tRNA synthetase genes.";
RL   J. Bacteriol. 174:1299-1306(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-422.
RC   STRAIN=168;
RX   PubMed=1699930; DOI=10.1128/jb.172.11.6372-6379.1990;
RA   Grundy F.J., Henkin T.M.;
RT   "Cloning and analysis of the Bacillus subtilis rpsD gene, encoding
RT   ribosomal protein S4.";
RL   J. Bacteriol. 172:6372-6379(1990).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M77668; AAA22878.1; -; Genomic_DNA.
DR   EMBL; M59358; AAA22718.1; -; Genomic_DNA.
DR   EMBL; AF008220; AAC00303.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14945.1; -; Genomic_DNA.
DR   EMBL; L17309; AAA68288.1; -; Genomic_DNA.
DR   PIR; A42648; A42648.
DR   RefSeq; NP_390845.1; NC_000964.3.
DR   RefSeq; WP_003229300.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P22326; -.
DR   SMR; P22326; -.
DR   STRING; 224308.BSU29670; -.
DR   jPOST; P22326; -.
DR   PaxDb; P22326; -.
DR   PRIDE; P22326; -.
DR   EnsemblBacteria; CAB14945; CAB14945; BSU_29670.
DR   GeneID; 938185; -.
DR   KEGG; bsu:BSU29670; -.
DR   PATRIC; fig|224308.179.peg.3225; -.
DR   eggNOG; COG0162; Bacteria.
DR   InParanoid; P22326; -.
DR   OMA; YMMAKDS; -.
DR   PhylomeDB; P22326; -.
DR   BioCyc; BSUB:BSU29670-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00165; S4; 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   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50889; S4; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..422
FT                   /note="Tyrosine--tRNA ligase 1"
FT                   /id="PRO_0000055643"
FT   DOMAIN          355..421
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOTIF           40..49
FT                   /note="'HIGH' region"
FT   MOTIF           232..236
FT                   /note="'KMSKS' region"
FT   BINDING         35
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         174
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   422 AA;  47737 MW;  141E573981303643 CRC64;
     MTNLLEDLSF RGLIQQMTDE EGLNKQLNEE KIRLYSGFDP TADSLHIGHL LPILTLRRFQ
     LAGHHPIALV GGATGLIGDP SGKKAERTLN TADIVSEWSQ KIKNQLSRFL DFEAAENPAV
     IANNFDWIGK MNVIDFLRDV GKNFGINYML AKDTVSSRIE SGISYTEFSY MILQSYDFLN
     LYRDKNCKLQ IGGSDQWGNI TAGLELIRKS EEEGAKAFGL TIPLVTKADG TKFGKTEGGA
     IWLDKEKTSP YEFYQFWINT DDRDVVKYLK YFTFLSKEEI EAYAEKTETA PEKREAQKRL
     AEEVTSLVHG REALEQAINI SQALFSGNIK ELSAQDVKVG FKDVPSMEVD STQELSLVDV
     LVQSKLSPSK RQAREDIQNG AVYINGERQT EINYTLSGED RIENQFTVLR RGKKKYFLVT
     YK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024