SYTC1_DICDI
ID SYTC1_DICDI Reviewed; 710 AA.
AC Q54J66;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Probable threonine--tRNA ligase 1, cytoplasmic;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
GN Name=thrS1; ORFNames=DDB_G0288267;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000109; EAL63315.1; -; Genomic_DNA.
DR RefSeq; XP_636821.1; XM_631729.1.
DR AlphaFoldDB; Q54J66; -.
DR SMR; Q54J66; -.
DR STRING; 44689.DDB0231248; -.
DR PaxDb; Q54J66; -.
DR EnsemblProtists; EAL63315; EAL63315; DDB_G0288267.
DR GeneID; 8626539; -.
DR KEGG; ddi:DDB_G0288267; -.
DR dictyBase; DDB_G0288267; thrS1.
DR eggNOG; KOG1637; Eukaryota.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; Q54J66; -.
DR OMA; FYYDFAY; -.
DR PhylomeDB; Q54J66; -.
DR PRO; PR:Q54J66; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:dictyBase.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..710
FT /note="Probable threonine--tRNA ligase 1, cytoplasmic"
FT /id="PRO_0000333831"
FT DOMAIN 72..137
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 81187 MW; 1D6E143FE62908A2 CRC64;
MSDSQENKPV ETPTEVKPVA EKKPAAEKKE KKPAVKKVGV METLQTPDYV KERIEIWESL
KAKHLESLKD MKEEPINVTL PDGKVVAGIK NKTTPYDIAK GISRGLADSI VSSKVNGEQI
WDISRPLEAD CNLQLCKFDS EEGKKTFWHS SAHILGQAME RIYGGQLCIG PATSEGFYYD
MAMGDKIVSA EDYKLINEVA QKIVQEKQPF ERLAVPRDIA LTMFKFNKYK TEIISKIPQE
DTVSLYRCGT LVDLCRGPHV PNTSYIKSFA VTKNSSAYWL GKAENDDLQR VYGISFPDKK
QMEEYENFMR EAALRDHRNV GKAQELFFFH PYSPGSAFFL PHGTRIYNKL VEFIREEYHR
RGFTEVISPS IFSQKLWEQS GHWQKYSENM FVLPVDKDNF SLKPMNCPGH CLMFGSRQRS
YRELPLRFAD FGVLHRNELA GALTGLTRVR KFQQDDAHIF CTTEMIEDEI NSCLGFMQYV
YGIFGFEFGL ELSTRPDNFL GEIAQWDIAE ASLEKALNKF GKPWKLNPKD GAFYGPKIDI
HITDCLKRSH QCATIQLDFQ LPIRFDLEYQ SDDAAELKKR PVIIHRAILG SVERMMAILI
EHTGGKWPLW VSPRQAIVVT VNKTHNEYGQ KVCKEISDAG FYCDIDDSDK TISKKVREAQ
LAQYNYILVV GQEEINGNTV NVRTRDNVVR GSLTVNDLIS EFKQLVKEFK
