ID   SYY2_PSET1              Reviewed;         399 AA.
AC   Q3ILJ9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   02-SEP-2026, entry version 105.
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};
GN   OrderedLocusNames=PSHAa0545;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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=tRNA(Tyr) + L-tyrosine + ATP = L-tyrosyl-tRNA(Tyr) + AMP +
CC         diphosphate + H(+); 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; CR954246; CAI85633.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3ILJ9; -.
DR   SMR; Q3ILJ9; -.
DR   STRING; 326442.PSHAa0545; -.
DR   KEGG; pha:PSHAa0545; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_5_0_6; -.
DR   BioCyc; PHAL326442:PSHA_RS02655-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
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   FunFam; 1.10.240.10:FF:000006; Tyrosine--tRNA ligase; 1.
DR   FunFam; 3.10.290.10:FF:000022; Tyrosine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000061; Tyrosine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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; IPR054608; SYY-like_C.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF22421; SYY_C-terminal; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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_0000236749"
FT   DOMAIN          336..398
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT   MOTIF           41..50
FT                   /note="'HIGH' region"
FT   MOTIF           225..229
FT                   /note="'KMSKS' region"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   399 AA;  44283 MW;  A2EDA9154F632B6D CRC64;
     MDLQTALAEI KRGTEEILIE DELVEKLKSG KKLKIKAGFD PTAPDLHLGH TVLINKMKTF
     QDLGHEVVFL IGDFTGMIGD PTGKNVTRKP LTREDVLANA ETYKEQVFKI LDPAKTTVAF
     NSTWMENLGA AGMIKLAARQ TVARMLERDD FKKRYASGQS IAIHEFLYPL VQGWDSVALE
     ADVELGGTDQ RFNLLMGREL QKDEGQKPQT VIMTPLLEGT DGVQKMSKSL GNYIGITDAP
     NDMFGKIMSI SDVLMWRYYD LLSGLSIAGI NAQKERVEQG TNPRDIKIEL AKELIARFHS
     EADAQAAHDD FIQRFQKKAL PDEIPELTVT IEQDSILIAN LLKEANLVAS TSEAMRMIKQ
     GAVKLNGEDK ITDTKLEIAK GSTAIYQVGK RKFANITVA
//