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SYT_METHJ
ID   SYT_METHJ               Reviewed;         610 AA.
AC   Q2FPK3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=Mhun_1007;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD40757.1; -; Genomic_DNA.
DR   RefSeq; WP_011448036.1; NC_007796.1.
DR   AlphaFoldDB; Q2FPK3; -.
DR   SMR; Q2FPK3; -.
DR   STRING; 323259.Mhun_1007; -.
DR   EnsemblBacteria; ABD40757; ABD40757; Mhun_1007.
DR   GeneID; 3924567; -.
DR   KEGG; mhu:Mhun_1007; -.
DR   eggNOG; arCOG00401; Archaea.
DR   HOGENOM; CLU_029833_0_0_2; -.
DR   OMA; IATFQID; -.
DR   OrthoDB; 11656at2157; -.
DR   Proteomes; UP000001941; 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..610
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_1000020429"
FT   REGION          1..144
FT                   /note="Editing domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   REGION          194..486
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   610 AA;  68832 MW;  0014BB3B6B8C17E1 CRC64;
     MRLLLIHSDF IEYEAKKKTK FAEDPCNPAD RLDDALVAFC AVESPDADDI DDVICQTVTA
     IGEMAGKVEC NRVMVYPYAH LSSDLAAPDL AVAALKAIEE SLEKAGYEVK RAPFGWYKSF
     SLSCKGHPLS ELSRSITPSE DAVKPEKKHI EHKFFVLTPE GTIHDVQEYM DDSPFAALIK
     KEIGTAVPVG GEPVHVDLMR SKEFVDYEPV SDVGHLRWLP RGKLVRDLLA DYALSLVLDY
     GASPVETPVM YDLADKAIFE HADKFGERQY RFKSGNRNMM LRFAACFGMF TTMRSMHISP
     NHLPMKMYEL STYSFRHEQK GEVIGLKRLR AFTMPDMHSL CKDLENALTC FEEQLAIGWK
     TGRDFGTQLV AVFRCTEEFY SEYEGWIKKI VKDSGVPILI ETLSDRVHYW IAKIDLAAID
     GQNRPIENPT VQIDVESSKR FGIKYHLADG TEVYPPILHC SPTGSVERVF CAILENTVNQ
     KVAHLPTWLT PTQVRIIPVT DNHLGYAKDI AEKLTKARIR ADIDDRDDSL NKKIRAAGMD
     WVSYVIVVGD SEMNSGNLTV TVRSESEPNK PQKITCTAEK LIEMIGKETS GKPFRPLYTP
     RMLSLKPRYI
 
 
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