ID B8P378_POSPM Unreviewed; 508 AA.
AC B8P378;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN ORFNames=POSPLDRAFT_88321 {ECO:0000313|EMBL:EED84736.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED84736.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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DR EMBL; EQ966246; EED84736.1; -; Genomic_DNA.
DR RefSeq; XP_002470133.1; XM_002470088.1.
DR AlphaFoldDB; B8P378; -.
DR STRING; 561896.B8P378; -.
DR KEGG; ppl:POSPLDRAFT_88321; -.
DR HOGENOM; CLU_025086_2_0_1; -.
DR InParanoid; B8P378; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 4619at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 1.10.10.2330; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR040725; PheRS_DBD3.
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; 2.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 351..441
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 55720 MW; B105B96B3CDD544D CRC64;
MAEAIQQLVL DTLDKSGIIQ DTRTLVLPGQ ADAAADHESQ IVILGALNSL ASRDMIAYTT
QETTSHVLTP EGAQIALEGS HEARVWAALP PKGQGAAITS KQLEAVVGSE TAKIGQGRAF
KNKWIAKEGD GLVKVAESVQ DATQLEMREV DSTGTLKAGE KALAELRKRK LIVQSGSWKT
STYKKYNFEA EGLPPNGGAF HPLLKVREEI RNIFLEMGFA EMPTSSFVES GFWCFDALFV
PQQHPAREVQ DTFYLSGKRN PSTSLPPPAS YYSRVSKVHE HGGYGSMGYR APWSDAETRK
LLLRTHTTAS SASMLYKLAA KCRGEDTDDS VNEQAAHPGA SAKDGDDGFR PAKLFSIDRV
FRNETMDATH LAEFHQVEGV VADRGLTLAD LIGFMRVFFK KMGIENLRFK PAYNPYTEPS
LEIFAFHPQL GKWVEVGNSG MFRPEMLEPM GFPKDVHAYN DSVRGAIDPS LSAAHVACLR
RYGISNIRTL VGHKVSIEGV ETSPAVRF
//
