ID A0A1E4RXA0_CYBJN Unreviewed; 741 AA.
AC A0A1E4RXA0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=threonine--tRNA ligase {ECO:0000256|ARBA:ARBA00013163};
DE EC=6.1.1.3 {ECO:0000256|ARBA:ARBA00013163};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031900};
GN ORFNames=CYBJADRAFT_153959 {ECO:0000313|EMBL:ODV71907.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV71907.1, ECO:0000313|Proteomes:UP000094389};
RN [1] {ECO:0000313|EMBL:ODV71907.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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:0000256|ARBA:ARBA00000070};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; KV453937; ODV71907.1; -; Genomic_DNA.
DR RefSeq; XP_020068946.1; XM_020213426.1.
DR AlphaFoldDB; A0A1E4RXA0; -.
DR STRING; 983966.A0A1E4RXA0; -.
DR GeneID; 30987822; -.
DR OMA; WYADGMY; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000094389; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd01667; TGS_ThrRS; 1.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 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; 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; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF46; THREONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 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; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:ODV71907.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000094389}.
FT DOMAIN 89..151
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 321..629
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 84697 MW; B99070D8A3F7AD0B CRC64;
MSQEIAEKVD KLSIGSEDKK QAPKAQGAGG APSGGAPKKE KKNKKDKNAG AVSSAIYLDP
QPEFIDERIQ LFEKLKGEYD TFVASQPRSA IKITLKDGSV KEGVAWETSP FEIAKEIGKS
FLERQCISKV NGELWDLERP LEGDAQLEFF DFETEEGRRV FWHSSAHVLG EACECNLGAH
ICLGPPTDDG FFYEFSVKGG EVAVSQADFP NLEAVAKNAV KQKQKFERLV MSKEDLLKMF
AYSKYKTYLV QTKVPDGGST TVYRCGPLID LCVGPHIPNT GRIKNFKLLK NSSCYFLGDA
TNDSLQRIYG ISFPEKKQME EHLKFLQEAA NRDHRKIGRE QELFYFNEMS PGSCFWLPHG
TRIYNTLVDL LRTEYRKRGY DEVITPNMYN AKLWETSGHW ANYQENMFTF DVEKEKFGLK
PMNCPGHCLM FKSRERSYRE LPWRVADFGV IHRNEFSGAL SGLTRVRRFQ QDDAHIFCTH
DQIEDEIHSI FDFLRYVYGV FGFEFKMELS TRPEKYVGEI ETWNNAEAKL ESALNKWGGK
WEVNPGDGAF YGPKIDIMIS DALKRWHQCA TIQLDFQLPD RFALEYRTKD VASEDTKDTD
RPVMIHRAIL GSVERMTAIL TEHFAGKWPF WLSPRQVLVV PVGVKFFDYA QEVGAKLKAE
GFYADVDLTG NTLQKKIRTG QLQKYNFIFI VGDQEEQSKS VNVRNRDITD LQTKNDAVPL
ETVIPQLKEL KESKRCDNAL I
//
