ID A0A1R0GLM8_9FUNG Unreviewed; 707 AA.
AC A0A1R0GLM8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=AYI68_g8166 {ECO:0000313|EMBL:OLY77803.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY77803.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY77803.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY77803.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(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}.
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:OLY77803.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSSL01007654; OLY77803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R0GLM8; -.
DR STRING; 133383.A0A1R0GLM8; -.
DR Proteomes; UP000187455; 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 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 SUPFAM; SSF55186; ThrRS/AlaRS common domain; 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, ECO:0000313|EMBL:OLY77803.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000187455};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..707
FT /note="threonine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012660999"
FT DOMAIN 263..553
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 707 AA; 80910 MW; 113E0782B5F45269 CRC64;
MWRSSAFILS AALANVLSND LFVYKNKVLD HSFSEDGTLF AGGFYTEFYA FHQGRGDLVS
KTLKFDGSGN DLNDQIIKSI ERVCKLPQNV RMFLKREQLN LVWKEYTKIC KRNDPITNLT
VDYELAIKIM QGNPFAQYLI SQAAKKGAKE FNLYRVGDYI GYPEGPVFSS SDVLVNKVEL
NQGSSHFTLE EEDLELYSNK FNYMEPTLNR ITGMTLFNKD SIDKYLANQA SMTKNDHRVI
GKDQDLFMMH TLSPGSPFFL IHGTRIVNRI LNLIRNKYSE YGFDEVITPQ IYLKSLWETS
GHWENYKKDM FGVVDAYTQN SNIIGESDNG PGCCSNSHDS GDIAAGLKPM NCPGHCLIFS
SKVRSYRDLP LRLADLSPLH RNEPVGSLSG LTRVRRFHQD DGHIFCSHQD IQEEIYKQLK
MLDEVYSIFK FNEYSLCLST RPLDHYIGSE TQWNEAENML KSALRKAGRE WTENKGDGAF
YGPKIDIHVK DALGRNHQTA TIQLDFQLPK RFKLKFVGKD GSREEPVIIH RAILGSVERM
MAILSEHYRG RWPFWMSPRQ AMVVPILPKE SKDVPEEVNL ANQEFVIEYA KKVHRSLLGG
NFSKSEHGGE SIISVRDSER DKSVEFIESR MKNYRFYVDL DSSLGSTKLG RVVKDARLSR
YNYLLAVGVE EAKQGLVNVR SFNSKEIGVV TLTRLQELFM EMSDNFD
//
