ID A0A094ECJ1_9PEZI Unreviewed; 779 AA.
AC A0A094ECJ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=V496_00263 {ECO:0000313|EMBL:KFY69405.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY69405.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY69405.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY69405.1}.
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DR EMBL; JPJY01000042; KFY69405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094ECJ1; -.
DR STRING; 1420909.A0A094ECJ1; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000029302; 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 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:UP000029302}.
FT DOMAIN 78..143
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 348..655
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 16..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88792 MW; 4E80C7ADE6E36017 CRC64;
MADTVKDAVD AVKDGVKNLA VNKKQQQKPK KEKKSGDDGG ASGPLELSPE PDFISHRIKI
FEKLKAEYEV ELAAKPREPI TITMKDGSIK EGTSWETTPS EIAKAISNSL LKRTVIARLN
GDNNQLWDLE RPLEESCSLE LLPFEDEEGR KVFWHSSAHI LGEASERRFG CNLCFGPPID
DGFYYEMALP EGAAVQQSDW KPIETLFSKI VKEKQQFERL VISKEDLLEM FKGNPYKQHV
IKEKVTEPKT TVYRNGPLID LCRGPHVPNT GRIETFAIMK NSASYFLGDP KRDSLQRIYG
VSFPDKKMMA EHKKFLEEAA KRDHRKIGRE QELFFFHEMS PGSAMWLPHG ARIYNTIQAF
LRDEYWKRGY EEVITPNMYN SELWKTSGHW QNYKDDMFTF DVEKEQFGLK PMNCPGHCLL
FSHRERSHRE LPWRVADFGV LHRNEASGAL TGLTRVRRFQ QDDAHIFCRE DQIVDEIEGL
FDFLRTMYGL LGFTFKMKLS TRNPEKFMGE LAEWDRAEAS LKSALDNFAT SPGGTPWEYN
HGDAAFYGPK IDIKISDSMR RDWQCATIQL DFQLPKNFGL EYMTSEGAIK PKDDASKGEN
LTATADTAEK EVSKKDKAKA LTPGCARPVM IHRAMAGSIE RFVAVLIEHF GGKWPFWLSP
RQILIIPVGV GFYEYAKEVQ GTFHKLKFFV DVDLSGNTLQ KKIRTGQLAQ YNFIFVVGDQ
EMKNGEVNIR NRDDTSSQDR GKPVSVQEAK EKLIALRDER GSSNPFAAND SKVAEVPKA
//
