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Database: UniProt
Entry: S8BLQ7_DACHA
LinkDB: S8BLQ7_DACHA
Original site: S8BLQ7_DACHA 
ID   S8BLQ7_DACHA            Unreviewed;       557 AA.
AC   S8BLQ7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN   ORFNames=H072_5831 {ECO:0000313|EMBL:EPS40338.1};
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:EPS40338.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS40338.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS40338.1,
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       Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006703}.
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:EPS40338.1}.
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DR   EMBL; AQGS01000406; EPS40338.1; -; Genomic_DNA.
DR   RefSeq; XP_011111644.1; XM_011113342.1.
DR   AlphaFoldDB; S8BLQ7; -.
DR   STRING; 1284197.S8BLQ7; -.
DR   eggNOG; KOG2784; Eukaryota.
DR   HOGENOM; CLU_025086_2_0_1; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 4619at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   Gene3D; 1.10.10.2320; -; 1.
DR   Gene3D; 1.10.10.2330; -; 1.
DR   Gene3D; 3.30.1370.240; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   NCBIfam; TIGR00468; pheS; 1.
DR   PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT   DOMAIN          313..557
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  62863 MW;  5ABBD8549737E9C7 CRC64;
     MDNIHIDLTI RLLARGARTS VGFCSPTSNR NRPAPSNIQR SKPGRRFESK KFRLLLPSNT
     SKHIQNLLLS RTPGTPTPVA DPAMAELQTE VLQKLDASST ATLTSEDAFP AVPFATLKAA
     LDSLQSKEMI VYETRDSEYN ILTAEGEQIR TSGSHEAKVF HVVHALGELK IADLAKQEEF
     ANDPNGAKVG QMRAFKEGWI KKHPEDKSKI ITGVDEIVDL TQKDLETISQ TGSLPDATTI
     ADLRKRKLIS PQKKIAFTIR KGPKFALEIL KEYTDLDSDM LQSGKWQEVT FKPYNLKALG
     APAMSGALHP LGKVRHEFRQ IFFEMGFTEM PTSQFVESGF WNFDALYVPQ QHPARDMQDT
     FFISDPPMAD MPRNEKGELL TEYWDNIKQV HENGKFGSLG YRYPWQPEES LKLVLRTHTT
     ATSAAMLYKL AQDPKPARYF SIDRVFRNET VDATHLAEFH QVEGVIADFD LTLGDLIGFM
     NEFFGKMGVK QLRFKPAYNP YTEPSMEIFS WHEGLGKWVE IGNSGMFRPE MLESMGLPKG
     MKVHGWGLSL ERPTMIK
//
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