ID   SYTE_SACS2              Reviewed;         386 AA.
AC   Q980D1;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Threonine--tRNA ligase editing subunit;
DE   AltName: Full=Ser-tRNA(Thr) hydrolase {ECO:0000305};
DE   AltName: Full=Threonyl-tRNA synthetase editing subunit {ECO:0000303|PubMed:15240874};
DE            Short=ThrS-ed {ECO:0000303|PubMed:15240874};
GN   Name=thrS-ed {ECO:0000303|PubMed:15240874}; OrderedLocusNames=SSO0384;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION IN EDITING, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=15240874; DOI=10.1073/pnas.0403926101;
RA   Korencic D., Ahel I., Schelert J., Sacher M., Ruan B., Stathopoulos C.,
RA   Blum P., Ibba M., Soell D.;
RT   "A freestanding proofreading domain is required for protein synthesis
RT   quality control in Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:10260-10265(2004).
CC   -!- FUNCTION: Freestanding tRNA editing subunit of threonine--tRNA ligase,
CC       the catalytic subunit is AC Q97VW8. Deacylates (edits) mischarged L-
CC       seryl-tRNA(Thr) in trans, removing L-serine, has no aminoacylation
CC       activity. In vitro when both subunits are present, or if the 2 subunits
CC       are fused, L-seryl-tRNA(Thr) is no longer produced. Has no activity on
CC       correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr)
CC       (PubMed:15240874). Editing is probably catalyzed by the 2'-OH of A76 of
CC       tRNA(Thr) (By similarity). {ECO:0000250|UniProtKB:Q9YFY3,
CC       ECO:0000269|PubMed:15240874}.
CC   -!- SUBUNIT: Probably interacts with its catalytic subunit (AC Q97VW8); a
CC       subunit fusion (in the order edit-catalytic) is fully functional.
CC       {ECO:0000305|PubMed:15240874}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Not essential, however growth is severely
CC       inhibited in the presence of 0.5 mM L-serine, but not in the presence
CC       of 0.5 mM L-ser plus 0.5 mM L-threonine. {ECO:0000269|PubMed:15240874}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Archaea-specific ThrRS editing domain subfamily. {ECO:0000305}.
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DR   EMBL; AE006641; AAK40712.1; -; Genomic_DNA.
DR   PIR; A90182; A90182.
DR   RefSeq; WP_009988816.1; NC_002754.1.
DR   AlphaFoldDB; Q980D1; -.
DR   SMR; Q980D1; -.
DR   STRING; 273057.SSO0384; -.
DR   EnsemblBacteria; AAK40712; AAK40712; SSO0384.
DR   GeneID; 44129358; -.
DR   KEGG; sso:SSO0384; -.
DR   PATRIC; fig|273057.12.peg.378; -.
DR   eggNOG; arCOG00401; Archaea.
DR   HOGENOM; CLU_712936_0_0_2; -.
DR   InParanoid; Q980D1; -.
DR   OMA; IIYPYAH; -.
DR   PhylomeDB; Q980D1; -.
DR   BRENDA; 6.1.1.3; 6163.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.800; -; 1.
DR   Gene3D; 3.50.80.10; -; 1.
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; PF08915; tRNA-Thr_ED; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..386
FT                   /note="Threonine--tRNA ligase editing subunit"
FT                   /id="PRO_0000441620"
SQ   SEQUENCE   386 AA;  44954 MW;  8707FCE32EF29128 CRC64;
     MIILFIHASD FSFNVKERAI KEPEEAKLKS IELKNTLVCF TTVEKGDDEE ILSKAIDDIL
     DVYSKVKADS VVIYPYAHLS SNLANPDTAI KILESLENLL KDKVKVYRAP FGWYKAFSIS
     CYGHPLSELS RRIRKTEELE KSEELKYCEK FGFPSSSESA FMRRATIGYL RNLFQPLFES
     ENNENVRDGE MSILYQNVES GRILPCINEN PRIVVVYGGV RELNFPKEIN DSKNRIRVWW
     VNESKIYVDV GRLIYYFILE SVKQQPPTLP DWLNPIQVRL LPVKKDFLDF SIQVAERLRK
     EGIRVNIDDL DDSLGNKIRR AGTDWIPFVI VIGEREVKTN TLTVKIRARN EQKSMTVEEL
     VKEIKDEVKE RQNLPLYYTL YRHKNN