ID S8AGW1_DACHA Unreviewed; 923 AA.
AC S8AGW1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
GN ORFNames=H072_3870 {ECO:0000313|EMBL:EPS42129.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS42129.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS42129.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42129.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:EPS42129.1}.
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DR EMBL; AQGS01000129; EPS42129.1; -; Genomic_DNA.
DR RefSeq; XP_011109830.1; XM_011111528.1.
DR AlphaFoldDB; S8AGW1; -.
DR STRING; 1284197.S8AGW1; -.
DR eggNOG; KOG2411; Eukaryota.
DR HOGENOM; CLU_014330_2_1_1; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT DOMAIN 281..743
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 761..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 104882 MW; D34D9F669D3DEC8E CRC64;
MTVQFRSCVR CRLDLARAAG PLLSRHPIAR TRRKPAGLSS QWQSIRTYIA DDPMADDIAD
RRGISNKEYR AFRRELVLKA KERRHLLSRI RARVVWWKGR SKVQDPIRSY WEEFKQQRIG
HAIGLPVKKF YQPWSLPAEP SNRKAIPELT KRDLGRTILI RAWLIKTTVI SKYLVFCKLG
HDGKKIQATV NDYTEFGDLE FLKSLKPHTP VEVEGVLAYK LGANPTYKPG PTPFHERVEI
LMQRVTPIGN PPADPIIEDT VYDADKRYLT LRTNQKSLET LQLRSTVSLL CRNHLVEEGF
TEVETPLLFK STPEGAREFL VPTRTPNMMY ALPQSPQQYK QILMASGVLK YFQVAKCFRD
EDLRADRQPE FTQLDLEMGF SSGSDVQRMV ERLLKRIWYE ILGVRLPAFP YLRYHDAIRL
YGSDKPDLRY DMKINDITEV MEEFLPSPEQ NIAHHPFKYE LISVPDIIIS NRQFKTVFGT
MTDPGTVLSQ YMKGPERSVS MSYFTADFKK EKFRENILFF APYLDQHEGA VDNFISKLES
LGYLKPNSIV ILAKRKKEFN PGGGTPIGEA RKALAANLVK EEIIPPLKGW KFCWVTRFPL
FTKMDPADGE PGQSASSGYK ATHHPFTAPM MHHLTKLYQK PWNVLGQHYD IVLNGVELGG
GSTRIHNAAL QKIILEEILG VPPSKMKTFN HLLEMLDSGC PPHAGLALGF DRLIATLAGT
SSIRDVIAFP KNNNGADVMV GSPSLVKPSQ LKPYGVEMIN PPEITEDDVE EAEEEERRKE
DKPFYDVPEE EEYDEVVEEN ASDVAPFHIS PSSISVPRGL LNSLEEDSIK SSERTKAQNK
WSDLLDIASK QFRQERAKAA AANASSGPRT GEAGTSEQEV KQPDNQTSES NQTTMSNEKG
WKQISATRVS DLKKMLQETK ERT
//
