(data stored in SCRATCH zone)

SWISSPROT: B4STG2_STRM5

ID   B4STG2_STRM5            Unreviewed;       403 AA.
AC   B4STG2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 81.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007};
DE            EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007};
DE            Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007};
GN   Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007};
GN   OrderedLocusNames=Smal_0300 {ECO:0000313|EMBL:ACF50005.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50005.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50005.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50005.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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_02007, ECO:0000256|SAAS:SAAS00724248}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) +
CC         L-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:0000256|HAMAP-Rule:MF_02007,
CC         ECO:0000256|SAAS:SAAS01125827};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007,
CC       ECO:0000256|SAAS:SAAS00724244}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007,
CC       ECO:0000256|SAAS:SAAS00724257}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007,
CC       ECO:0000256|SAAS:SAAS00724250}.
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DR   EMBL; CP001111; ACF50005.1; -; Genomic_DNA.
DR   RefSeq; WP_006388280.1; NC_011071.1.
DR   STRING; 391008.Smal_0300; -.
DR   EnsemblBacteria; ACF50005; ACF50005; Smal_0300.
DR   KEGG; smt:Smal_0300; -.
DR   eggNOG; ENOG4105DA0; Bacteria.
DR   eggNOG; COG0162; LUCA.
DR   HOGENOM; HOG000242791; -.
DR   KO; K01866; -.
DR   OMA; VNYMMAK; -.
DR   OrthoDB; 402899at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01520-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
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;
DR   PRODOM; B4STG2.
DR   SWISS-2DPAGE; B4STG2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777199,
KW   ECO:0000313|EMBL:ACF50005.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777290};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|SAAS:SAAS00724231};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777344,
KW   ECO:0000313|EMBL:ACF50005.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777134};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777336};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182,
KW   ECO:0000256|SAAS:SAAS00893931}.
FT   DOMAIN      339    400       S4 RNA-binding. {ECO:0000259|PROSITE:
FT                                PS50889}.
FT   MOTIF        42     51       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02007}.
FT   MOTIF       226    230       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02007}.
FT   BINDING     229    229       ATP. {ECO:0000256|HAMAP-Rule:MF_02007}.
SQ   SEQUENCE   403 AA;  44348 MW;  E2180B1D05452A32 CRC64;
     MSSIEEALAL IGRGADEILK LEDLRARLQE GRPLRIKAGF DPTAPDLHLG HTVLLNKMRQ
     FQDLGHQVIF LIGDFTGMIG DPSGKSLTRK PLSKDDVLAN ARTYEEQVFK VLDRSRTEVR
     FNSEWFGKMG AADMIRLAGQ HTVARMLERD DFAKRYAAQQ SIAIHEFLYP LVQGYDSVAL
     EADVELGGTD QKFNLLMGRG LQEHHGQKPQ VVLTMPLLEG LDGVNKMSKS LGNYIGISEP
     AIDIVTKTMK VDDTLMWRWI ELLSFDISQA EAVQLREQVA NGGLNPRVVK LRLARELATR
     FHDAAAAEQA VAGWEAAVTG QGDITQLPLQ DVAIPAEGLR IAALLTAAGL TPSNSEANRK
     LKERAVKVDG EVVEDGQQVL QPGFEGLLQV GKRTFARVRL VAA
//

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