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Threonine--tRNA ligase catalytic subunit (EC 6.1.1.3) (Threonyl-tRNA synthetase 1) (ThrRS 1) (Threonyl-tRNA synthetase catalytic subunit) (ThrRS-cat)

 SYTC_AERPE              Reviewed;         471 AA.
Q9YDW0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
23-MAY-2018, entry version 110.
RecName: Full=Threonine--tRNA ligase catalytic subunit;
EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
AltName: Full=Threonyl-tRNA synthetase 1;
Short=ThrRS 1 {ECO:0000303|PubMed:19761773};
AltName: Full=Threonyl-tRNA synthetase catalytic subunit;
Short=ThrRS-cat;
Name=thrS-cat {ECO:0000303|PubMed:19761773}; Synonyms=thrS1;
OrderedLocusNames=APE_0809.1;
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC
100138 / K1).
Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
Desulfurococcaceae; Aeropyrum.
NCBI_TaxID=272557;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
PubMed=10382966; DOI=10.1093/dnares/6.2.83;
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y.,
Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H.,
Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H.,
Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y.,
Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y.,
Nomura N., Sako Y., Kikuchi H.;
"Complete genome sequence of an aerobic hyper-thermophilic
crenarchaeon, Aeropyrum pernix K1.";
DNA Res. 6:83-101(1999).
[2] {ECO:0000244|PDB:3A31, ECO:0000244|PDB:3A32}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC, PROBABLE
FUNCTION, COFACTOR, AND SUBUNIT.
PubMed=19761773; DOI=10.1016/j.jmb.2009.09.018;
Shimizu S., Juan E.C., Sato Y., Miyashita Y., Hoque M.M., Suzuki K.,
Sagara T., Tsunoda M., Sekiguchi T., Dock-Bregeon A.C., Moras D.,
Takenaka A.;
"Two complementary enzymes for threonylation of tRNA in crenarchaeota:
crystal structure of Aeropyrum pernix threonyl-tRNA synthetase lacking
a cis-editing domain.";
J. Mol. Biol. 394:286-296(2009).
-!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a
two-step reaction: L-threonine is first activated by ATP to form
Thr-AMP and then transferred to the acceptor end of tRNA(Thr)
(Probable). This protein is probably not able to deacylate
mischarged L-seryl-tRNA(Thr) as it lacks the appropriate domain
(PubMed:19761773). {ECO:0000305|PubMed:19761773}.
-!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP +
diphosphate + L-threonyl-tRNA(Thr). {ECO:0000255|HAMAP-
Rule:MF_00184}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00184,
ECO:0000269|PubMed:19761773};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_00184, ECO:0000269|PubMed:19761773};
-!- SUBUNIT: Homodimer (PubMed:19761773). Probably interacts with its
editing subunit (By similarity). {ECO:0000250|UniProtKB:Q97VW8,
ECO:0000269|PubMed:19761773}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184,
ECO:0000305}.
-!- MISCELLANEOUS: There are two ThrRS in this archaeon. The first one
(APE_0809.1, this entry) is most similar to bacterial ThrRS but it
lacks the N-terminal editing domain. The second one (APE_0117.1,
AC Q9YFY3) is most similar to archaeal ThrRS but lacks the central
catalytic domain; it probably does not aminoacylate tRNA(Thr).
{ECO:0000305}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000255|HAMAP-Rule:MF_00184}.
-----------------------------------------------------------------------
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EMBL; BA000002; BAA79787.2; -; Genomic_DNA.
PIR; C72673; C72673.
PDB; 3A31; X-ray; 2.50 A; A=1-471.
PDB; 3A32; X-ray; 2.30 A; A=1-471.
PDBsum; 3A31; -.
PDBsum; 3A32; -.
ProteinModelPortal; Q9YDW0; -.
SMR; Q9YDW0; -.
STRING; 272557.APE_0809.1; -.
PRIDE; Q9YDW0; -.
EnsemblBacteria; BAA79787; BAA79787; APE_0809.1.
KEGG; ape:APE_0809.1; -.
PATRIC; fig|272557.25.peg.582; -.
eggNOG; arCOG00401; Archaea.
eggNOG; COG0441; LUCA.
HOGENOM; HOG000009830; -.
KO; K01868; -.
OrthoDB; POG093Z01GO; -.
EvolutionaryTrace; Q9YDW0; -.
Proteomes; UP000002518; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
CDD; cd00771; ThrRS_core; 1.
Gene3D; 3.40.50.800; -; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR002320; Thr-tRNA-ligase_IIa.
InterPro; IPR033728; ThrRS_core.
PANTHER; PTHR11451; PTHR11451; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
PRINTS; PR01047; TRNASYNTHTHR.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
1: Evidence at protein level;
3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Cytoplasm; Ligase; Metal-binding;
Nucleotide-binding; Protein biosynthesis; Reference proteome;
RNA-binding; tRNA-binding; Zinc.
CHAIN 1 471 Threonine--tRNA ligase catalytic subunit.
/FTId=PRO_0000101117.
REGION 8 333 Catalytic. {ECO:0000255|HAMAP-
Rule:MF_00184,
ECO:0000305|PubMed:19761773}.
METAL 112 112 Zinc. {ECO:0000244|PDB:3A32,
ECO:0000255|HAMAP-Rule:MF_00184,
ECO:0000269|PubMed:19761773}.
METAL 166 166 Zinc; via tele nitrogen.
{ECO:0000244|PDB:3A32, ECO:0000255|HAMAP-
Rule:MF_00184,
ECO:0000269|PubMed:19761773}.
METAL 310 310 Zinc; via pros nitrogen.
{ECO:0000244|PDB:3A32, ECO:0000255|HAMAP-
Rule:MF_00184,
ECO:0000269|PubMed:19761773}.
HELIX 9 15 {ECO:0000244|PDB:3A32}.
TURN 27 29 {ECO:0000244|PDB:3A32}.
HELIX 34 37 {ECO:0000244|PDB:3A32}.
HELIX 48 65 {ECO:0000244|PDB:3A32}.
STRAND 75 78 {ECO:0000244|PDB:3A32}.
HELIX 80 84 {ECO:0000244|PDB:3A32}.
HELIX 91 94 {ECO:0000244|PDB:3A32}.
STRAND 95 100 {ECO:0000244|PDB:3A32}.
STRAND 103 107 {ECO:0000244|PDB:3A32}.
HELIX 112 126 {ECO:0000244|PDB:3A32}.
HELIX 127 129 {ECO:0000244|PDB:3A32}.
STRAND 132 143 {ECO:0000244|PDB:3A32}.
HELIX 148 150 {ECO:0000244|PDB:3A32}.
TURN 153 155 {ECO:0000244|PDB:3A32}.
STRAND 158 170 {ECO:0000244|PDB:3A32}.
HELIX 171 173 {ECO:0000244|PDB:3A32}.
HELIX 174 191 {ECO:0000244|PDB:3A32}.
TURN 199 201 {ECO:0000244|PDB:3A32}.
STRAND 202 207 {ECO:0000244|PDB:3A32}.
HELIX 211 213 {ECO:0000244|PDB:3A32}.
TURN 215 217 {ECO:0000244|PDB:3A32}.
HELIX 222 243 {ECO:0000244|PDB:3A32}.
STRAND 246 250 {ECO:0000244|PDB:3A32}.
STRAND 260 271 {ECO:0000244|PDB:3A32}.
STRAND 273 286 {ECO:0000244|PDB:3A32}.
HELIX 287 290 {ECO:0000244|PDB:3A32}.
HELIX 293 301 {ECO:0000244|PDB:3A32}.
STRAND 306 316 {ECO:0000244|PDB:3A32}.
HELIX 317 327 {ECO:0000244|PDB:3A32}.
TURN 328 330 {ECO:0000244|PDB:3A32}.
HELIX 334 336 {ECO:0000244|PDB:3A32}.
STRAND 340 347 {ECO:0000244|PDB:3A32}.
HELIX 353 369 {ECO:0000244|PDB:3A32}.
STRAND 373 380 {ECO:0000244|PDB:3A32}.
TURN 381 383 {ECO:0000244|PDB:3A32}.
HELIX 384 393 {ECO:0000244|PDB:3A32}.
STRAND 398 403 {ECO:0000244|PDB:3A32}.
HELIX 405 410 {ECO:0000244|PDB:3A32}.
STRAND 412 419 {ECO:0000244|PDB:3A32}.
TURN 420 423 {ECO:0000244|PDB:3A32}.
STRAND 424 431 {ECO:0000244|PDB:3A32}.
HELIX 435 457 {ECO:0000244|PDB:3A32}.
HELIX 468 470 {ECO:0000244|PDB:3A32}.
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


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