ID A0A364KRQ5_9EURO Unreviewed; 541 AA.
AC A0A364KRQ5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BHQ10_002241 {ECO:0000313|EMBL:RAO66229.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO66229.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO66229.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO66229.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAO66229.1}.
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DR EMBL; MIKG01000003; RAO66229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364KRQ5; -.
DR STRING; 1196081.A0A364KRQ5; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000249363; 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; cd00771; ThrRS_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF50; THREONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW 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:UP000249363}.
FT DOMAIN 98..386
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 39..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 60925 MW; 3F46F6E01A3FEC0A CRC64;
MRPTSFLCRR QHLRINILRP RARILPDAAS IRHCSCHASP LTPKRPASSA PSSLNRPKST
DASNIHSNTP AADHRILGTA QELFTSSPYS PGSPLFLPNG THIINKLIDF LRAQYRQYGF
REVLTPNIYK KSLWEISGHW QNYKDDMYEV RGRGATGVTE GELGEDEQYG LKPMNCPGHC
LLFKSQNHSF RDLPVRYADF SPLHRNEISG SLSGLTRVRR FHQDDGHIFC RPQQIGKEID
LALAFVNMVM KTFGLPKYNL VLSTRPEKDF IGSLELWDSA EDQLRQALDK SGLPWELNEG
DGAFYGPKID IQLQDSDGKY HQLSTIQLDL NLPQRFELEY QVAEGEPDYD PNTPGKATPV
LIHRAIFGSL ERFLALLIEQ YAGRWPFWLS PRQGIILTVQ NDEPVLRLAE EAAAKLSGYD
TIVPRLHSED ADLQQPAPLT PDPTFLIDID SSSRSLSKKI QRAKSMKYNL IFVVGSKNLA
DQTIDVDISG QLQGSTEDNA SKFQSVLTEV VGASSQGNSR ALKMKIDDVR DLLLEMERKF
V
//
