ID A0A1Y2M3G5_EPING Unreviewed; 593 AA.
AC A0A1Y2M3G5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=B5807_04367 {ECO:0000313|EMBL:OSS50664.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS50664.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS50664.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS50664.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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; KZ107841; OSS50664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2M3G5; -.
DR STRING; 105696.A0A1Y2M3G5; -.
DR InParanoid; A0A1Y2M3G5; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 5473299at2759; -.
DR Proteomes; UP000193240; 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:UP000193240}.
FT DOMAIN 292..370
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 593 AA; 67201 MW; 00410CEC56D28A8C CRC64;
MPTIAVDKAA LFKELGRDYT TEEFDELCFE FGIELDEDTS QSTKPEDQAQ PPQLKIEIPA
NRYDMLCFEG IALNLKVFLE KEKLPKWQVT PPKDGQLQEL HIKPETAQIR ELCSGVILRG
ITFTQARYDS FIALQDKLHQ NLARQRTLVS IGTHDLDTVK GPFTYEALKP EEIEFIPLNQ
TKKMNAKELM EFYEKDKHLG RFLHIIRDSP VYPVIYDANR TVLSLPPIIN GNHSKITLDT
KNVLIEITAT DKTKVEIVNH MLIAMFAGYA ESIEPIKIVS DHNNESRISP DLSPREWKAE
VDYLNNVTGL DLSPEEISKL LSKMGHDVTP SKTDKNILDV SVPITRADIL HQADIMEDYS
IAYGFNKLPR VYPNKTAAVS APLPINKLAD IVRLESASAG WTEVMPLILC SHEENFEWLN
RVDDGKTAIK LANPKTAEYQ LVRTSLLPGL LKTINSNKHH SVPMKIFEVS DVGFKDETQE
RKSRNERHFA AAIMGKTSGF EQVHGLMDRL MLMLRSKFTT REDGLKNTAL EGYWIEEVED
KTFLPGHAAS IKINLSGKNH TIGVFGILHP SVLHKFELPY PVSTVEFNLE VFL
//
