(data stored in ACNUC7421 zone)

SWISSPROT: SYY2_PSEHT

ID   SYY2_PSEHT              Reviewed;         399 AA.
AC   Q3ILJ9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 75.
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 haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   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.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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_02007}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
CC       diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000255|HAMAP-
CC       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
CC       family. TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}.
DR   EMBL; CR954246; CAI85633.1; -; Genomic_DNA.
DR   RefSeq; WP_011327246.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILJ9; -.
DR   SMR; Q3ILJ9; -.
DR   STRING; 326442.PSHAa0545; -.
DR   EnsemblBacteria; CAI85633; CAI85633; PSHAa0545.
DR   GeneID; 32566434; -.
DR   KEGG; pha:PSHAa0545; -.
DR   eggNOG; ENOG4105DA0; Bacteria.
DR   eggNOG; COG0162; LUCA.
DR   HOGENOM; HOG000242791; -.
DR   KO; K01866; -.
DR   OMA; DLMWRYY; -.
DR   OrthoDB; POG091H02CB; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
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; 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:SF5; PTHR11766:SF5; 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   3: Inferred from homology;
DR   PRODOM; Q3ILJ9.
DR   SWISS-2DPAGE; Q3ILJ9.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN         1    399       Tyrosine--tRNA ligase 2.
FT                                /FTId=PRO_0000236749.
FT   DOMAIN      336    398       S4 RNA-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_02007}.
FT   MOTIF        41     50       "HIGH" region.
FT   MOTIF       225    229       "KMSKS" region.
FT   BINDING     228    228       ATP. {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
//

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