ID SYTC_SULAC Reviewed; 549 AA.
AC Q4J9C4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Threonine--tRNA ligase catalytic subunit;
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase catalytic subunit;
DE Short=ThrRS-cat;
GN Name=thrS-cat {ECO:0000305};
GN Synonyms=thrS {ECO:0000255|HAMAP-Rule:MF_00184};
GN OrderedLocusNames=Saci_1261;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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 activates
CC L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly
CC charged amino acid; unlike most archaea the editing function is found
CC in a freestanding protein. {ECO:0000250|UniProtKB:Q97VW8}.
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 (By similarity). Probably interacts with its editing
CC subunit (By similarity). {ECO:0000250|UniProtKB:Q97VW8,
CC ECO:0000250|UniProtKB:Q9YDW0}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY80606.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000077; AAY80606.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015385586.1; NZ_CP046615.1.
DR AlphaFoldDB; Q4J9C4; -.
DR SMR; Q4J9C4; -.
DR STRING; 330779.Saci_1261; -.
DR GeneID; 78441607; -.
DR KEGG; sai:Saci_1261; -.
DR PATRIC; fig|330779.12.peg.1222; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_008554_2_2_2; -.
DR Proteomes; UP000001018; 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; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 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..549
FT /note="Threonine--tRNA ligase catalytic subunit"
FT /id="PRO_0000101112"
FT REGION 142..437
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 549 AA; 64036 MW; 93504056531F9BD9 CRC64;
MESYKEVWLK AGLIYALNLL SSGNLKPVEI GLGERYFYVD IDSPDILTLD EAKDFAKYNQ
YDYQLVEDNR GSITVVYNGH QIKLNGGKPN QNVHPKYFQI LSISVHHPSP EKQYVRVLGV
GFEKEEQLKD YLNWLEKVSE YDHRIIGDRL DLFSFPEEAP PGVVLFHPNG QIIRKEMMRF
MEEINDSMGY KEVYTSHVYR SLLWKISGHY DYYKDKMLLF EIDNDEELGI KPMNCPAHIL
IYKSKVRSYK DLPIRFSEFG HVYRWEKKGE LYGLLRVRGF TQDDGHIFLR EDQIKDEIKL
LMKKTLDVLA IFGFKGDDVR VNLSTRPDES IGTDEQWNKA TDALISALNE LNIKYEVKEK
EGAFYGPKID FDIRDSLSRW WQLSTIQVDF NLPERFKLEY VDKDGSKKRP VMVHRAIYGS
IDRFMAILLE HFRGKLPTWL SPIQVRVLPI TDEIEDYGNS LMAKLRENKI RVDMDSGEET
LSKRIKKAYD DGVPYLIIVG RKEKDEGKVT VRARGNIEIR GINVEKFVQA LVEEIRNKDL
NQSAVSKLK
//
