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Database: UniProt
Entry: Q9Z8I2
LinkDB: Q9Z8I2
Original site: Q9Z8I2 
ID   SYY_CHLPN               Reviewed;         412 AA.
AC   Q9Z8I2; Q9JSF6; Q9K284;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   05-DEC-2018, entry version 127.
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};
GN   OrderedLocusNames=CPn_0361, CP_0397, CpB0370;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138
RT   from Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
CC       two-step reaction: tyrosine is first activated by ATP to form Tyr-
CC       AMP and then transferred to the acceptor end of tRNA(Tyr).
CC       {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) +
CC         L-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
CC       family. TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD18505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP98301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA98569.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE001363; AAD18505.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE002161; AAF38242.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98569.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE009440; AAP98301.1; ALT_INIT; Genomic_DNA.
DR   PIR; D72088; D72088.
DR   PIR; G81581; G81581.
DR   PIR; G86535; G86535.
DR   RefSeq; NP_224561.1; NC_000922.1.
DR   ProteinModelPortal; Q9Z8I2; -.
DR   SMR; Q9Z8I2; -.
DR   STRING; 182082.CpB0370; -.
DR   PRIDE; Q9Z8I2; -.
DR   EnsemblBacteria; AAD18505; AAD18505; CPn_0361.
DR   EnsemblBacteria; AAF38242; AAF38242; CP_0397.
DR   EnsemblBacteria; AAP98301; AAP98301; CpB0370.
DR   EnsemblBacteria; BAA98569; BAA98569; BAA98569.
DR   GeneID; 895054; -.
DR   KEGG; cpa:CP_0397; -.
DR   KEGG; cpj:tyrS; -.
DR   KEGG; cpn:CPn0361; -.
DR   KEGG; cpt:CpB0370; -.
DR   PATRIC; fig|115713.3.peg.399; -.
DR   eggNOG; ENOG4105DA0; Bacteria.
DR   eggNOG; COG0162; LUCA.
DR   HOGENOM; HOG000242790; -.
DR   KO; K01866; -.
DR   OrthoDB; POG091H00WT; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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; 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; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN         1    412       Tyrosine--tRNA ligase.
FT                                /FTId=PRO_0000055650.
FT   DOMAIN      345    412       S4 RNA-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_02006}.
FT   MOTIF        36     45       "HIGH" region.
FT   MOTIF       222    226       "KMSKS" region.
FT   BINDING      31     31       Tyrosine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02006}.
FT   BINDING     162    162       Tyrosine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02006}.
FT   BINDING     166    166       Tyrosine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02006}.
FT   BINDING     225    225       ATP. {ECO:0000255|HAMAP-Rule:MF_02006}.
FT   CONFLICT    128    128       R -> G (in Ref. 1; AAD18505).
FT                                {ECO:0000305}.
FT   CONFLICT    349    349       D -> G (in Ref. 3; BAA98569).
FT                                {ECO:0000305}.
SQ   SEQUENCE   412 AA;  45915 MW;  D2022DFE5D8B212F CRC64;
     MQSWLQSLQE RNILENFTAG LESVEGPIAA YLGFDPTAPA LHIGHWIGIC FLKRLAALGI
     TPIALVGGAT GMVGDPSGKQ SERSLLQTSE VFDNSQKITA CLQRYLPGVT LVNNADWLQE
     ISLIDFLRDI GKHFRLGQML VKDTIKQRVH SDEGISYTEF SYLILQSYDF YHLFKNYGTI
     LQCGGSDQWG NITSGIDFIR RKGLGQAYGL TYPLLTNAQG KKIGKTESGT VWLDSDLTSP
     FELYQYLLRL PDDTIPKIAR TLTLLSNEEI QDIDRRVQTD PVAVKEFVAQ DILSAIHGDL
     GLEEALSVTR SMHPGNLSSL SEKDFHELFA GGMGASLDKS EVLGKRWLDL FLVLGLCKSK
     GEIRRLIEQK GVYINNVPIA NEHSVCEEQD ICYGHYVLLA QGKKRKLVLY LN
//
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