SYT_PYRFU
ID SYT_PYRFU Reviewed; 625 AA.
AC Q8U176;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=PF1351;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION IN EDITING, DOMAIN, AND MUTAGENESIS OF 120-TYR--GLU-134.
RX PubMed=26113036; DOI=10.1038/ncomms8552;
RA Ahmad S., Muthukumar S., Kuncha S.K., Routh S.B., Yerabham A.S.,
RA Hussain T., Kamarthapu V., Kruparani S.P., Sankaranarayanan R.;
RT "Specificity and catalysis hardwired at the RNA-protein interface in a
RT translational proofreading enzyme.";
RL Nat. Commun. 6:7552-7552(2015).
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) (By similarity).
CC Also edits incorrectly charged L-seryl-tRNA(Thr) (PubMed:26113036).
CC {ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:26113036}.
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 (about residues 1-143) is an archaea-
CC specific tRNA-editing domain (PubMed:26113036). Catalysis of tRNA
CC editing is performed by the charged tRNA itself (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:26113036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; AE009950; AAL81475.1; -; Genomic_DNA.
DR RefSeq; WP_011012497.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U176; -.
DR SMR; Q8U176; -.
DR STRING; 186497.PF1351; -.
DR PRIDE; Q8U176; -.
DR EnsemblBacteria; AAL81475; AAL81475; PF1351.
DR GeneID; 41713154; -.
DR KEGG; pfu:PF1351; -.
DR PATRIC; fig|186497.12.peg.1413; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_029833_0_0_2; -.
DR OMA; DAHIFML; -.
DR OrthoDB; 11656at2157; -.
DR PhylomeDB; Q8U176; -.
DR BRENDA; 6.1.1.3; 5243.
DR Proteomes; UP000001013; 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 CDD; cd00771; ThrRS_core; 1.
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 InterPro; IPR033728; ThrRS_core.
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 1: Evidence at protein level;
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..625
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101109"
FT REGION 1..147
FT /note="Editing domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000305|PubMed:26113036"
FT REGION 206..505
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT MUTAGEN 120..134
FT /note="YKAFRISCKGHPLAE->AKAFRISCKGHPLAA: Isolated domain
FT has nearly wild-type deacylation of mischarged L-seryl-
FT tRNA(Thr), no activity on L-threonyl-tRNA(Thr)."
FT /evidence="ECO:0000269|PubMed:26113036"
SQ SEQUENCE 625 AA; 73208 MW; 53C9044674B0742A CRC64;
MRMLLIHSDY IEYEVKDKAI KNPEPISEEE KKGRMDEVLV AFISVEKVDE KNPDEVVEKA
INEIIEVAKQ VKAENLFVYP FAHLSSELAK PSVAQEVLRR IYEGLKERGY NVGKAPFGYY
KAFRISCKGH PLAELSRTIV PEEAKVEEVP EALKKEETEL VSYWYILTPE GELVEVDKFD
FTGHENLRKF ANYEIAKSRI ADKEPPHVRL MLEHELVDYE PGSDPGNLRY YPKGRLIKSL
LEQYVSEKVI EYGAMEVETP IMYDFEHPAL EKYLNRFPAR QYIVLSGDKR YFLRFAACFG
QFMISKDATI SYRNLPLRMY ELTRYSFRRE KRGELSGLRR LRAFTMPDMH TLAKDIEQAK
DEFKKQFKLS MEVLGGVGLT PDDYEVAIRF TEDFWNEHKD FIIELVKLIG KPVLIEMWKQ
RFFYFILKFE FNFVDNLDKA AALSTVQIDV ENAERFGITY YDENGEEKYP LILHCSPSGA
IERVMYAILE KQAKLMQEGK KPMFPLWLSP IQVRVIPVSK EYLDYALYVA GKIEGARIRV
DVDDEDERLS KKIRRAEKEW IPYIVVVGEK EKETGTITVR RREDGKQYET RIEELIKEIK
QKTEGFPYKP RPLPLLLSQR PKFRG
