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SYT_METBU
ID   SYT_METBU               Reviewed;         635 AA.
AC   Q12WD4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Mbur_1324;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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   -!- DOMAIN: The N-terminal domain is an archaea-specific tRNA-editing
CC       domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis
CC       of tRNA editing is performed by the charged tRNA itself.
CC       {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; CP000300; ABE52242.1; -; Genomic_DNA.
DR   RefSeq; WP_011499387.1; NC_007955.1.
DR   AlphaFoldDB; Q12WD4; -.
DR   SMR; Q12WD4; -.
DR   STRING; 259564.Mbur_1324; -.
DR   EnsemblBacteria; ABE52242; ABE52242; Mbur_1324.
DR   GeneID; 3998613; -.
DR   KEGG; mbu:Mbur_1324; -.
DR   HOGENOM; CLU_029833_0_0_2; -.
DR   OMA; DAHIFML; -.
DR   OrthoDB; 11656at2157; -.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   Gene3D; 3.50.80.10; -; 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; IPR023509; DTD-like_sf.
DR   InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR   InterPro; IPR015011; Threonyl-tRNA_syn_edit_dom_arc.
DR   PANTHER; PTHR11451; PTHR11451; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF08915; tRNA-Thr_ED; 1.
DR   PRINTS; PR01047; TRNASYNTHTHR.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..635
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_1000020427"
FT   REGION          1..144
FT                   /note="Editing domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   REGION          215..514
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         483
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   635 AA;  72718 MW;  6D3032119A937759 CRC64;
     MQLLLIHSDY IEYEVKKSTP VAEEIEESFK QGRLEDALTA FMAVESFDEA NPQEIIDRAV
     SEIENVAGQV KAENIMLYPY AHLSSDLSSP KVAVSVLKGI ENALEGKYNV MRAPFGWYKA
     FRISCKGHPL SELSRTIRLE GAVPCGKVVS LDAEKKEVVS EALKAEDSAK SYWRILTPDG
     ELHDAETFDL TGHDNLQKFV DYEISKNRNI EKAPPHVELM RRLEIADYEP GSDSGNMRYY
     PKGRLMKSLI ENFVLEESSK IGAMEVETPL MYDMNHPTLK KYLDRFPARQ YSIESDKRHM
     FLRFAACFGQ FLMNHDMTIS YKNLPLKMIE MTRYSFRKEQ RGELVGLRRL RAFTMPDMHT
     LCPDMEAAIS QFGEQYSMCI DILRKIGIDV SDFEVAIRFT REFYDDNREF ITELAKKVDK
     PVLVEMWDTR FFYFVLKFEF NFVDAIAKAS ALSTVQIDVE NAERYDINYV DANGKINRPT
     ILHCSPSGAI ERCIYALLEK AAMDAEEGKV PNLPVWLSPT QVRVIPIAER HMDFAQEVAD
     SLLCRADIDD REETVGKKIR DAGREWIPYV AVIGDSEVES GKVTVTIRAE SEPKKPMKVE
     MTAEELSERV FNEIGDMPYR SLPLAKLLSM RPKFI
 
 
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