SYTC_AERPE
ID SYTC_AERPE Reviewed; 471 AA.
AC Q9YDW0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
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 1;
DE Short=ThrRS 1 {ECO:0000303|PubMed:19761773};
DE AltName: Full=Threonyl-tRNA synthetase catalytic subunit;
DE Short=ThrRS-cat;
GN Name=thrS-cat {ECO:0000303|PubMed:19761773}; Synonyms=thrS1;
GN OrderedLocusNames=APE_0809.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2] {ECO:0007744|PDB:3A31, ECO:0007744|PDB:3A32}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC, PROBABLE
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=19761773; DOI=10.1016/j.jmb.2009.09.018;
RA Shimizu S., Juan E.C., Sato Y., Miyashita Y., Hoque M.M., Suzuki K.,
RA Sagara T., Tsunoda M., Sekiguchi T., Dock-Bregeon A.C., Moras D.,
RA Takenaka A.;
RT "Two complementary enzymes for threonylation of tRNA in crenarchaeota:
RT crystal structure of Aeropyrum pernix threonyl-tRNA synthetase lacking a
RT cis-editing domain.";
RL J. Mol. Biol. 394:286-296(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) (Probable). This
CC protein is probably not able to deacylate mischarged L-seryl-tRNA(Thr)
CC as it lacks the appropriate domain (PubMed:19761773).
CC {ECO:0000305|PubMed:19761773}.
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 ECO:0000269|PubMed:19761773};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184,
CC ECO:0000269|PubMed:19761773};
CC -!- SUBUNIT: Homodimer (PubMed:19761773). Probably interacts with its
CC editing subunit (By similarity). {ECO:0000250|UniProtKB:Q97VW8,
CC ECO:0000269|PubMed:19761773}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184,
CC ECO:0000305}.
CC -!- MISCELLANEOUS: There are two ThrRS in this archaeon. The first one
CC (APE_0809.1, this entry) is most similar to bacterial ThrRS but it
CC lacks the N-terminal editing domain. The second one (APE_0117.1, AC
CC Q9YFY3) is most similar to archaeal ThrRS but lacks the central
CC catalytic domain; it probably does not aminoacylate tRNA(Thr).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; BA000002; BAA79787.2; -; Genomic_DNA.
DR PIR; C72673; C72673.
DR PDB; 3A31; X-ray; 2.50 A; A=1-471.
DR PDB; 3A32; X-ray; 2.30 A; A=1-471.
DR PDBsum; 3A31; -.
DR PDBsum; 3A32; -.
DR AlphaFoldDB; Q9YDW0; -.
DR SMR; Q9YDW0; -.
DR STRING; 272557.APE_0809.1; -.
DR PRIDE; Q9YDW0; -.
DR EnsemblBacteria; BAA79787; BAA79787; APE_0809.1.
DR KEGG; ape:APE_0809.1; -.
DR PATRIC; fig|272557.25.peg.582; -.
DR eggNOG; arCOG00401; Archaea.
DR EvolutionaryTrace; Q9YDW0; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR033728; ThrRS_core.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..471
FT /note="Threonine--tRNA ligase catalytic subunit"
FT /id="PRO_0000101117"
FT REGION 8..333
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000305|PubMed:19761773"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000269|PubMed:19761773, ECO:0007744|PDB:3A32"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000269|PubMed:19761773, ECO:0007744|PDB:3A32"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000269|PubMed:19761773, ECO:0007744|PDB:3A32"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 158..170
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 222..243
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 260..271
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 273..286
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 306..316
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 353..369
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:3A32"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:3A32"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 435..457
FT /evidence="ECO:0007829|PDB:3A32"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:3A32"
SQ SEQUENCE 471 AA; 53122 MW; 8AA642538F4DDD7A CRC64;
MASGQDKTHI DYAYELDITV KPDSRVPVFN REFATFTGAG VPLFSLGGGP IRYALAEVLA
KFHARRGYYV VETPIIASTE LFKVSGHIEF YRNNMYLFDI EGHEFAVKPM NCPYHILLFL
NEVAKHRSKL PLPFKVFEFG RVHRYEPSGS IYGLLRVRGF TQDDAHIIVP GGRVIDVVYD
VFEEMKLVLE RLFKLGVSSE TFKVRLSMSD KSLIGKEFMG SKEEWEGAEE ALREAASRIN
EKYGIDIVEL EGEAAFYGPK LDFIMMVEES GVSKEWQMGT IQFDFNLPRR FRLYDVVREE
FGIEEVYIIH RALLGSIERF LGVYLEHRRG RMPFTLAPIQ FAVIAVKTGG EVDREIEDLA
SSIAKGLLDK GFRVAVKGSS KTGLSSDVRH IESTAKPAVN VFIGAKEVRE KVLDVRVFDL
ESMKRRRLAI AYGDAADAVE NLAAVAEELE SPVRSLSGQA PRIPADFSFM L
