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Database: UniProt
Entry: C0NUD1_AJECG
LinkDB: C0NUD1_AJECG
Original site: C0NUD1_AJECG 
ID   C0NUD1_AJECG            Unreviewed;       600 AA.
AC   C0NUD1;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=HCBG_06962 {ECO:0000313|EMBL:EEH05011.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05011.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR   EMBL; GG663372; EEH05011.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NUD1; -.
DR   STRING; 447093.C0NUD1; -.
DR   VEuPathDB; FungiDB:I7I50_12179; -.
DR   HOGENOM; CLU_020279_2_0_1; -.
DR   InParanoid; C0NUD1; -.
DR   OrthoDB; 5473299at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   Gene3D; 3.30.56.10; -; 2.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR040659; PhetRS_B1.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   NCBIfam; TIGR00471; pheT_arch; 1.
DR   PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF18262; PhetRS_B1; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR   PROSITE; PS51483; B5; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001631}.
FT   DOMAIN          297..375
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   600 AA;  67833 MW;  647C490FD8967E02 CRC64;
     MPTIAVDKAA LFKELGRKYS TEEFDQLCFE FGLELDEDTE NLERPFVNGK QEPPQLKIEV
     PANRYDLLCI EGIALMLNIF RERTLSPEYR LVAPSNGELE TIIVKEETMK IRPYISGAIL
     RNIHFDQARY ESFIALQDKL HQNLARQRTL VAIGTHDLDK LKGPFTYEAL PPKDISFVPL
     NQTRKMNGQE MMEFYEKDKH IGKYLHIIRD SPVYPVIYDS NRVVCSLPPI INGDHSKITL
     NTKNVFLEYT ATDKTKVEIV NNIMVTMFSQ YTSEPFTVEP VRIVSAHNNE TRQTPDLSPR
     PTQASISYIN QCCGLSLSAA EICNLLKRMS YFAEPSKTSP DLVDVRVPVT RADVLHQADI
     MEDVAIAYGF NELPRYFPNI SGTIAQPLPV NKLTDIIRTE AAMAGWSEVM PLILCSHDEN
     FAWLNRKDDG NTAVKLANPK TVEFQVVRTS LLPGLLKTIG ENKHHAIPMK IFEVSDVAFK
     DVSRERKSTN ERHFAAAWYG KTSGFEIVHG LLDRIMAMLK TAFTIGEEGL DNPAMGNASY
     WIEELDDPTY FTGHAASVHV RISGKDHVIG SFGILHPTVL GKFDLKYPVS TLEINIETFL
//
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