(data stored in ACNUC7421 zone)

SWISSPROT: C1ASY8_RHOOB

ID   C1ASY8_RHOOB            Unreviewed;       425 AA.
AC   C1ASY8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02006};
DE            EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02006};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006};
DE            Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02006};
GN   Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02006,
GN   ECO:0000313|EMBL:BAH48920.1};
GN   OrderedLocusNames=ROP_06730 {ECO:0000313|EMBL:BAH48920.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48920.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48920.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48920.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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:0000256|HAMAP-Rule:MF_02006, ECO:0000256|SAAS:SAAS00009852}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
CC       diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000256|HAMAP-
CC       Rule:MF_02006, ECO:0000256|SAAS:SAAS00777173}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02006,
CC       ECO:0000256|SAAS:SAAS00009815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006,
CC       ECO:0000256|SAAS:SAAS00009833}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. TyrS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02006,
CC       ECO:0000256|SAAS:SAAS00538763}.
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DR   EMBL; AP011115; BAH48920.1; -; Genomic_DNA.
DR   RefSeq; WP_012687923.1; NC_012522.1.
DR   STRING; 632772.ROP_06730; -.
DR   EnsemblBacteria; BAH48920; BAH48920; ROP_06730.
DR   KEGG; rop:ROP_06730; -.
DR   PATRIC; fig|632772.20.peg.734; -.
DR   eggNOG; ENOG4105DA0; Bacteria.
DR   eggNOG; COG0162; LUCA.
DR   HOGENOM; HOG000242790; -.
DR   KO; K01866; -.
DR   OMA; DLMWRYY; -.
DR   OrthoDB; POG091H00WT; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; 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; IPR024107; Tyr-tRNA-ligase_bac_1.
DR   PANTHER; PTHR11766; PTHR11766; 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; C1ASY8.
DR   SWISS-2DPAGE; C1ASY8.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777199,
KW   ECO:0000313|EMBL:BAH48920.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777290};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|SAAS:SAAS00009761};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777344,
KW   ECO:0000313|EMBL:BAH48920.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777134};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777336};
KW   RNA-binding {ECO:0000256|SAAS:SAAS00009776}.
FT   DOMAIN      356    422       S4 RNA-binding. {ECO:0000259|PROSITE:
FT                                PS50889}.
FT   MOTIF        41     50       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02006}.
FT   MOTIF       231    235       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02006}.
FT   BINDING      36     36       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02006}.
FT   BINDING     171    171       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02006}.
FT   BINDING     175    175       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02006}.
FT   BINDING     234    234       ATP. {ECO:0000256|HAMAP-Rule:MF_02006}.
SQ   SEQUENCE   425 AA;  46336 MW;  86BBE9D9B3D8C6D8 CRC64;
     MTENIIDELT WRGLIAQSTD LDALRRDLDA GPVTLYAGFD PTGPSLHAGH LVPLLALKRF
     QRAGNRPIVL AGGATGLIGD PRDVGERTMN SADTVAEWAD RIRGQLERFV DFDDSPSGAV
     IENNMNWTGK LSAIDFLRDV GKHFSVNVML ARDTVKRRLE TDGMSYTEFS YMLLQANDYL
     HLRRSHGCSL QVGGSDQWGN IIAGVELNRR VDAASVHGLT VPLVTSADGK KFGKSTGGGS
     LWLDPEMTSP YAWYQYFVNT GDADVIKYLR WFTFLSAEEL AELETATAER PHAREAQRRL
     AAEMTTLVHG EANTRAVELA SQALFGRAEL QDLDEPTLGA ALREASVAEL APGEPSSIVD
     LLVLSGLCES KGAARRAVKE GGASVNNQKI SSEDWTPESG DLLHGTWLVV RRGKRNFAGV
     KVLSN
//

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