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SYT_RHOOB
ID   SYT_RHOOB               Reviewed;         685 AA.
AC   C1B4B5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE            EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE   AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE            Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN   Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; OrderedLocusNames=ROP_68570;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
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 erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC       step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC       and then transferred to the acceptor end of tRNA(Thr). Also edits
CC       incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-
CC       Rule:MF_00184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC         threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC         Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR   EMBL; AP011115; BAH55104.1; -; Genomic_DNA.
DR   RefSeq; WP_015890534.1; NC_012522.1.
DR   AlphaFoldDB; C1B4B5; -.
DR   SMR; C1B4B5; -.
DR   STRING; 632772.ROP_68570; -.
DR   PRIDE; C1B4B5; -.
DR   EnsemblBacteria; BAH55104; BAH55104; ROP_68570.
DR   KEGG; rop:ROP_68570; -.
DR   PATRIC; fig|632772.20.peg.7147; -.
DR   HOGENOM; CLU_008554_0_1_11; -.
DR   OMA; FYYDFAY; -.
DR   OrthoDB; 900765at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00771; ThrRS_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR033728; ThrRS_core.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11451; PTHR11451; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR01047; TRNASYNTHTHR.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..685
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_1000199564"
FT   DOMAIN          1..65
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   REGION          262..568
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         545
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   685 AA;  76415 MW;  06EC49A08482FE7A CRC64;
     MSTPASAAPA ALVRVPAGTT AGTAVREAGY PSKGPDVVVV VRDAEGGLRD LSWVPDADVD
     VEPVAANTDD GRSVIRHSAA HVLAQAVQQE FPEAKLGIGP PIKDGFYYDF AVERPFTPED
     LANLEKRMKK IVKGSQRFSR RVVDSLEEAR AELANEPFKL ELIDDKSGID DPEIMEVGGN
     ELTIYDNLDP RTGEKVWGDL CRGPHIPTTK HIPAFKLTRS SAAYWRGNQD NADLQRIYGT
     AWESAEAQEQ HLELLAEAER RDHRKLGSEL DLFSFPDELG SGLPVFHPRG GIIRTEMEDY
     SRKRHVEEGY EFVNTPHITK GHLYEVSGHL DWYRDGMFPA MHIDEELNED GTVRKPGQDY
     YLKPMNCPMH NLIFRSRGRS YRELPLRLFE FGSVYRYEKS GVVHGLTRVR GMTQDDAHIY
     CTREQMRDEL ATTLQFVLGL LKDYGLDDFY LELSTKNPDK FVGDDAVWEE ATATLAEVAE
     SSGLNLVPDP GGAAFYGPKI SVQVQDALGR TWQMSTIQLD FNLPERFDLE YTASDGTKKR
     PVMIHRALFG SIERFFGVLT EHYAGAFPAW LAPVQVVGIP VAETFADHLF DVVKRLKAAG
     VRAEVDASDD RMQKKIFNNT AQKVPFMLLA GARDVEAGAV SFRFRDGTQV NGVPVDDAVR
     IVTDWIGRRE NASPTAELLQ SGREG
 
 
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