VIRJ_HYPVG
ID VIRJ_HYPVG Reviewed; 646 AA.
AC G9N4A3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Glutamine--tRNA ligase protein virJ {ECO:0000303|PubMed:31790246};
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P00962};
DE AltName: Full=Trichoxide biosynthesis protein virJ {ECO:0000303|PubMed:31790246};
DE AltName: Full=Virensol biosynthesis cluster protein J {ECO:0000303|PubMed:31790246};
GN Name=virJ {ECO:0000303|PubMed:31790246}; ORFNames=TRIVIDRAFT_81025;
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586;
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
RN [2]
RP FUNCTION.
RX PubMed=31790246; DOI=10.1021/jacs.9b09669;
RA Liu L., Tang M.C., Tang Y.;
RT "Fungal highly reducing polyketide synthases biosynthesize salicylaldehydes
RT that are precursors to epoxycyclohexenol natural products.";
RL J. Am. Chem. Soc. 141:19538-19541(2019).
CC -!- FUNCTION: Glutamine--tRNA ligase; part of the gene cluster that
CC mediates the biosynthesis of virensols and trichoxide, fungal natural
CC products that contain or are derived from a salicylaldehyde core
CC (PubMed:31790246). VirJ does not seem to play any role in virensols and
CC trichoxide biosynthesis (PubMed:31790246).
CC {ECO:0000269|PubMed:31790246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000250|UniProtKB:P00962};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; ABDF02000086; EHK18429.1; -; Genomic_DNA.
DR RefSeq; XP_013952629.1; XM_014097154.1.
DR AlphaFoldDB; G9N4A3; -.
DR SMR; G9N4A3; -.
DR STRING; 413071.G9N4A3; -.
DR EnsemblFungi; EHK18429; EHK18429; TRIVIDRAFT_81025.
DR GeneID; 25798224; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_81025; -.
DR eggNOG; KOG1148; Eukaryota.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; G9N4A3; -.
DR OMA; FAWRIMG; -.
DR OrthoDB; 809861at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..646
FT /note="Glutamine--tRNA ligase protein virJ"
FT /id="PRO_0000449288"
FT REGION 25..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..108
FT /note="'HIGH' region"
FT /evidence="ECO:0000250|UniProtKB:P13188"
FT MOTIF 351..355
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250|UniProtKB:P13188"
FT BINDING 99..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 105..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 147
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 296
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 344..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 352..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
SQ SEQUENCE 646 AA; 73489 MW; 1BDA6736A994F91E CRC64;
MADAVAEAVA KLVLDDETGE MVTKNELKKR IQKRARKAAA AANRSNAQQE KGNKPAANKP
AAKPEERVID PDAMFKQGFL GDVFKLRPEE SVVTRFPPEP NGYLHLGHAK AIAVNFGFAK
YHGGRTQQQL DGQINYIPTD VADSRFDDTN PDAEKGEYFV AIEDTIRWLG FTPSEITYAS
DNYQRMYDLA EELIKMEKAY VCHCDDVETK KQRGGEDGLF PRYRCEHAKQ DVETNLKKFR
GMRDGEYAPR SAWLRMKQDI ENNPNPQMWD LAAYRIPKDQ EPHFRTGTKW RIYPTYDFAH
CLCDSFEGIT HSLCTTEFIM SRESYEWLNK LLVEFQPMQR EYGRLNLSGT IMSKRGLRTL
IENNVVRGWD DPRLYTIKGI RRRGIPPGAL LSFIYELGVT TSITQVSIKR FEQSIRVYLE
KTVPRLMLVL DPVPVVIEDG EEQDLDIPFS PKDPKLGSHT IRLTKTVYID RSDFREVDSK
DYFRLAPGKT VGLLNVPYPI KAVSFTKDET TGAIKEIKAV YDKEGKKPKT YIQWVPEGSL
PAEVRIHEAL FKSDSPGSAP GGLLSDVNPN SETIWPNALI ETGFHEVKRR APWPEAEGEK
TGEFHPETVR FQAMRVAYFA LDSDSTDEKI VLNRIVPLKE DSGKSS
