ID   SYY2_PSEAE              Reviewed;         399 AA.
AC   Q9I5Q3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Tyrosine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_02007};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007};
DE   AltName: Full=Tyrosyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_02007};
DE            Short=TyrRS 2 {ECO:0000255|HAMAP-Rule:MF_02007};
GN   Name=tyrS2 {ECO:0000255|HAMAP-Rule:MF_02007}; OrderedLocusNames=PA0668;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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_02007}.
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_02007};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}.
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DR   EMBL; AE004091; AAG04057.1; -; Genomic_DNA.
DR   PIR; C83563; C83563.
DR   RefSeq; NP_249359.1; NC_002516.2.
DR   RefSeq; WP_003113167.1; NZ_QZGE01000010.1.
DR   AlphaFoldDB; Q9I5Q3; -.
DR   SMR; Q9I5Q3; -.
DR   STRING; 287.DR97_3621; -.
DR   PaxDb; Q9I5Q3; -.
DR   PRIDE; Q9I5Q3; -.
DR   EnsemblBacteria; AAG04057; AAG04057; PA0668.
DR   GeneID; 880817; -.
DR   KEGG; pae:PA0668; -.
DR   PATRIC; fig|208964.12.peg.699; -.
DR   PseudoCAP; PA0668; -.
DR   HOGENOM; CLU_024003_5_0_6; -.
DR   InParanoid; Q9I5Q3; -.
DR   OMA; YMMAKDS; -.
DR   PhylomeDB; Q9I5Q3; -.
DR   BioCyc; PAER208964:G1FZ6-673-MON; -.
DR   Proteomes; UP000002438; 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; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02007; Tyr_tRNA_synth_type2; 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; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   PANTHER; PTHR11766:SF1; PTHR11766:SF1; 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..399
FT                   /note="Tyrosine--tRNA ligase 2"
FT                   /id="PRO_0000236750"
FT   DOMAIN          336..396
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT   MOTIF           42..51
FT                   /note="'HIGH' region"
FT   MOTIF           226..230
FT                   /note="'KMSKS' region"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   399 AA;  44130 MW;  14CF0EB768EE833D CRC64;
     MKSVEEQLAL IQRGADEILV EAELVAKLKR GQPLRIKAGF DPTAPDLHLG HTVLINKLRQ
     FQDLGHQVIF LIGDFTGMIG DPSGKSVTRP PLTREQVLEN AETYKSQVFK ILDPAKTEVA
     FNSTWMDQLT PADFIRLASQ YTVARMLERD DFSKRYASNQ PIAIHEFLYP LVQGYDSVAL
     KADVELGGTD QKFNLLMGRE LQRAYGQEAQ VILTMPLLEG LDGVKKMSKS LGNYIGIQEA
     PGVMYSKLVS IPDTLMWRYF ELLSFRSLDE IDSFRKDVEA GANPRDIKIK LAEEIVARFH
     GEEAAASAHK SAGNRLKEGE LPEDLPEIEL SSPEDMPVAS VLNKAGLVKN AAAARDLLGA
     GSVKVDGQVV DRTFMLALGE TRVFQAGKKA FARITLKAE