ID A0A2P5HFL3_9PEZI Unreviewed; 776 AA.
AC A0A2P5HFL3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DHEL01_v212574 {ECO:0000313|EMBL:POS69033.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS69033.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS69033.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS69033.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) 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:POS69033.1}.
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DR EMBL; MAVT02002764; POS69033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5HFL3; -.
DR STRING; 158607.A0A2P5HFL3; -.
DR InParanoid; A0A2P5HFL3; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000094444; 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:POS69033.1}; 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:UP000094444}.
FT DOMAIN 66..131
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 303..649
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 88054 MW; 11791398FED37FA4 CRC64;
MADAAAPPPP AAAKQKAPKK EKKAAAGEDS GPLEMQPPPS FLQDRLDLFD RLKARQDEQA
AKQPREPIKI TMPDGKVIDG TSWETTPGEI AKGISNSLYK RTVVARLDKS DDKLWDLDRP
LEASCDLELL DFDHPVGKTV FWHSSAHVLG EACERRFGCS LCIGPPIDAG FYYEMALPDG
AAVQNSDWKP LETIVGKIAK EKQKFERLVM TKEELLEMFK YNKYKQHIIK DKIPDGTSTT
VYRNGPLIDL CRGPHVPDTG RIEAFSILKN SASYFLGNQE NDSLQRVYGV SFPDKKKMAE
HKKLLEEAAK RDHRKIGKDQ ELFFFDGVSP GSAFWLPHGA RIFNKIVEFL KEQYWKRDYD
EVITPNMYNA DLWKQSGHWA HYKDDMFINK VDKEDFGLKP MNCPAHCIMF DNRERSHREL
PLRLADFGVL HRNEASGALS GLTRVRRFQQ DDAHIFCRED QIKQEMDDCF DFLREFYGLL
GMSFKLKLST RPEGYMGEIA TWDRAEAALK EALDDFTQKI GSSWELNPGD GAFYGPKIDI
KVVDSLGREW QCATTQLDFV QPENFSLEYM TAEGVKDTAK AKEDKDKEAS KPAPAAAAAE
DNTDKVAKRA TKKPLSPGCA RPVIIHRAMA GSVERFAAIL CEHYGGKWPM WLSPRQIMVI
PVGKGFYGYA EEVRKLFKTR MRMYVDVDTS GETLPKKIRR AQLAQYNFVF VVGDEEMRNR
QVNIRYRDDT DTQSRGTPVG LDEAADKIGK LRDERGMYNP FPAAAKELPV QIKEGE
//
