ID   SYY2_VIBVU              Reviewed;         395 AA.
AC   Q8DBX3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=VV1_1683;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION TO 373-380.
RC   STRAIN=CMCP6;
RX   PubMed=21245845; DOI=10.1038/msb.2010.115;
RA   Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y.,
RA   Rhee J.H., Lee S.Y.;
RT   "Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug
RT   targeting and discovery.";
RL   Mol. Syst. Biol. 7:460-460(2011).
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; AE016795; AAO10099.2; -; Genomic_DNA.
DR   RefSeq; WP_011079602.1; NC_004459.3.
DR   AlphaFoldDB; Q8DBX3; -.
DR   SMR; Q8DBX3; -.
DR   EnsemblBacteria; AAO10099; AAO10099; VV1_1683.
DR   KEGG; vvu:VV1_1683; -.
DR   HOGENOM; CLU_024003_5_0_6; -.
DR   Proteomes; UP000002275; Chromosome 1.
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_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; 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; 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; RNA-binding.
FT   CHAIN           1..395
FT                   /note="Tyrosine--tRNA ligase 2"
FT                   /id="PRO_0000236778"
FT   DOMAIN          334..395
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   395 AA;  43834 MW;  EA950AA7B3541907 CRC64;
     MASIEAALAE IKRGVEELIP EEELIAKLKE GRPLRIKLGA DPTAPDIHLG HTVILNKLRA
     FQDLGHDVTF LIGDFTGMVG DPTGKNSTRP PLTREDVLRN AETYKQQVFK ILDPAKTKIQ
     FNSEWLSELG AEGMIRLAAN QTVARMLERD DFKKRYAGGQ PIAIHEFMYP LLQGYDSVAM
     ETDVELGGTD QKFNLLMGRE LQKANGQKPQ VVLMMPLLVG LDGEKKMSKS ANNYIGVSEA
     PSEMFGKIMS ISDDLMWSYY ELLSFRPLEE LAQFKADVAA GKNPRDIKVL LAKEIIARFH
     SEADADAAEQ EFVNRFAKNQ IPDEMPEFTF AAGTPMANLL KEAELCSSTS EAMRMVKQGA
     AKMDGEKVED AKAEPAVGTY VFQVGKRKFA RITIA