ID F0U7D6_AJEC8 Unreviewed; 733 AA.
AC F0U7D6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=HCEG_01765 {ECO:0000313|EMBL:EGC42403.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) 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}.
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DR EMBL; DS990636; EGC42403.1; -; Genomic_DNA.
DR AlphaFoldDB; F0U7D6; -.
DR STRING; 544711.F0U7D6; -.
DR VEuPathDB; FungiDB:I7I53_06450; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR OMA; WYADGMY; -.
DR Proteomes; UP000008142; 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 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; 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:EGC42403.1}; 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:UP000008142}.
FT DOMAIN 60..127
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 332..622
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 83524 MW; 0A877526621977CF CRC64;
MDAHPSNPNA PPPQKAAKTK PKKPEPTEEA PLPDFIIERN KLFEELKQKH DEELKHKSRF
GINITIDIGD SNPSTIIGKA WETTPGSFLR DIPKEISSTV VIAKLDGKEL WDLDRPLERD
CRVTFLPFDS IEGREVFWHS SAHVLGEACE CYYGCLLSHG PPTPQGFFYD MALEPGHVVK
ESDWPALDTK AARIFKEKQP FDRLEVSKSD LKKMFAYSKY KLHYINNLVE GESSTVYRCG
TLVDLCRGPH IQNTGKIKIM KIMQNSAAYF LGDQSNDALQ RIRGVAFPDK KQMQEHLKFL
EEAEKRNHLR IGKDQDLFFF DEVSPGCPFL LPNGTKIFNA LQALLRSEYR KRGYQEVQSP
NMYDVGIWRQ SGHWQHYKDD MFKLDIEKRT WALKPMNCPG HAIMFGHRER SYRELPLRIA
DFGVLHRNEA SGALHGLTRI MQEIDGLFDF LRAIYGLFGF SFKLKLSTRP EKYMGKLETW
NYAEDQLRAA MTKFKGNDWE VDEGDGAFYG PKIDVTIQDA LKREFQCATI QLDYQMPVNF
KLEYMTGETG AKAKPEEKSA GAPAAKTADK PAGDAAKPDV PPTNSDEPGP GRARPVVIHR
AIIGSFERFF GIIIEHFGGK WPFWLSPRQI LIVPVMPAVN DYVEELQRIL KGDKLNVDID
ISGNTMQKKI RTGQIAQYNF IFVVGAQEKS TRTVNIRNRD DPSSQAKGSL VPLEEARAKL
RALRKERRLV NEL
//
