ID A0A179UQ23_BLAGS Unreviewed; 521 AA.
AC A0A179UQ23;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BDBG_04759 {ECO:0000313|EMBL:OAT09217.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT09217.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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DR EMBL; GG657456; OAT09217.1; -; Genomic_DNA.
DR RefSeq; XP_002624895.1; XM_002624849.1.
DR AlphaFoldDB; A0A179UQ23; -.
DR STRING; 559298.A0A179UQ23; -.
DR GeneID; 8504540; -.
DR KEGG; bgh:BDBG_04759; -.
DR VEuPathDB; FungiDB:BDBG_04759; -.
DR OrthoDB; 4619at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:UP000002038}.
FT DOMAIN 223..514
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 283..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 58544 MW; B4C67EAA8A8021E5 CRC64;
MASDLTAQIL DLLSSTDDPI LSSDAFPAAP SIALKSALDR LRSRDMIIYE TIEQEQAVLL
PEAEGIVANG SHEAKVFEAV RAALDGLKIK DLPDIVGKEA AKVGAGNSFK KGWIKKDKDV
LRSATDSIED TTREQLLTIQ KTKTYSDPKV LADLRKRKLL TMQKVLSFTI SKGPKYAREL
VKEETDLTAD MLANGSWKTA KFKPYNFNAK GAITPSGALH PLNKVRQEFR QIFFEMGFEE
MPTNRFVETG FWNFDALFVP QQHPARDLQD TFYISDPVCA DKPREDDPSD VHVANAGKTT
GRSSDADNSK ALDYEQYWNN IRAVHQSGKY GSIGYRYPWD PEESLRLVLR THTTSVSTYM
LHKLAANPRP ARYFSIDRVF RNEAVDATHL AEFHQVEGVI ADFGLALGGL IGFMEVFFAK
MGIHGLRFKP AYNPYTEPSM EIFGYHDGLG KWVEIGNSGM FRPEMLEPMG LPKDMRVYGW
GLSLERPTMI KYGVSNIREL LGHKVDLNFI ETNPAVRLEK D
//