ID G9MZ03_HYPVG Unreviewed; 806 AA.
AC G9MZ03;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=TRIVIDRAFT_90082 {ECO:0000313|EMBL:EHK20332.1};
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 {ECO:0000313|EMBL:EHK20332.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK20332.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000225};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
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:EHK20332.1}.
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DR EMBL; ABDF02000080; EHK20332.1; -; Genomic_DNA.
DR RefSeq; XP_013954528.1; XM_014099053.1.
DR AlphaFoldDB; G9MZ03; -.
DR STRING; 413071.G9MZ03; -.
DR EnsemblFungi; EHK20332; EHK20332; TRIVIDRAFT_90082.
DR GeneID; 25798914; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_90082; -.
DR eggNOG; KOG0556; Eukaryota.
DR HOGENOM; CLU_004553_0_1_1; -.
DR InParanoid; G9MZ03; -.
DR OMA; KYSLDFP; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR024320; LPG_synthase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF2; ASPARTATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09924; LPG_synthase_C; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 177..485
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 91236 MW; A2908805004E537F CRC64;
MNEGGGRRSA QGSPRSSMDN STTSFDSVRS SGSDWPTHPY ELNTIAELDT LPIGTEVNFR
GRIHTQRQLS KALDFLLLRD QTYSIQGVLS RENMEMVQWV QKLPAESLLQ INGVLKAPPE
PVRSATVSNV EIDIHGLWLV NPAQSAPFSV YRPPEAMRNR MSSRILDLRH PANQALFRIR
SMVARQFRDT LEKEGFLEIQ TPKLQPAATE SGASVFKVNY FGRKAFLAQS PQLAKQMSVS
ADFGRVYEIG PVFRAENSNT HRHLTEYTGL DIEMAIEHDY HEVIAVLDIF LKNVFKTVYE
MPEVEVLKKR WPSSEFKYLD ETLILDFRDG LQMLRDDGRE APEEDLSTSD EIRLGELVRE
KYNTDYYVLD RFPTNARPFY THKDPEDPRW TRSFDIFIRG QEICSGGQRI HDAAELRANM
AAAGIAEEGM EEYMAGFDLG APPHAGAGLG LERIVTWMLE LGDVRNASLF YRDPKSLPDR
KPGLPHPEAD TTKPYAALHT PPVEKLIANY GDASNTSWLD ERFEIWRHKS GAAIGFVKQE
KFAMITGDPL CDKSQYKDVI SSYVKYVVTE LRLVPMWMLV SYDVQKILAH DLGWRTLSCT
EEQRVDTARH QSPAGGPKAR RVEREGVKIH EVKADEDFIS RANPAIEAWK ANRKGKQVHL
TEVRPWVDPE HRRYFAAEKD GKVHAMVVLA KLSPRHGWQV KWALDFPGAV NGAIEVLIEH
ALSCVTGQVT FGVGVSEKLT PGEHLHGIRA KFLATTYRSI VESLGLRRKA GFRSKFGALG
EEVYICYPKH GVGLRDLQQV IKFFQD
//
