ID E3RML2_PYRTT Unreviewed; 509 AA.
AC E3RML2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 13-SEP-2023, entry version 55.
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 {ECO:0000256|ARBA:ARBA00031194};
GN ORFNames=PTT_09695 {ECO:0000313|EMBL:EFQ93054.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ93054.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ93054.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000395};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; GL534010; EFQ93054.1; -; Genomic_DNA.
DR RefSeq; XP_003298867.1; XM_003298819.1.
DR AlphaFoldDB; E3RML2; -.
DR STRING; 861557.E3RML2; -.
DR EnsemblFungi; EFQ93054; EFQ93054; PTT_09695.
DR KEGG; pte:PTT_09695; -.
DR eggNOG; KOG2783; Eukaryota.
DR HOGENOM; CLU_022696_0_1_1; -.
DR OrthoDB; 1095527at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0070156; P:mitochondrial phenylalanyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00469; pheS_mito; 1.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 2.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 89..375
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 377..509
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 57403 MW; C2A5C36AF532D1C6 CRC64;
MTGTSSCKDA DTDVLDGNLP SIELEYIVKG TESGGIVEVV ATYSSVPRDI KIEGRSYQTD
EWMNTPSTIL AAIPRRLHLQ PDHPLTITRK LIESRFPGYK THNDLFPIVT TRQNFDSLGF
PLDHVGRSRT DTYYLNKDTV LRTHTSAHQA DTFRSNESEG YLISADVYRR DAVDRSHYPV
FHQMEGARTW DREQAKRESK DLAQIIWEDV EKIPKHDIAV EDPNPPFHTE RNPLQTGHSP
EEVEAIAAHL KRSLEDMVVT IFNAAKSASD TTTDTPDEPL KVRWVEAYFP FTSPSWELEV
FWQGDWLEVL GCGVVSQPIL NNASVPNRVG WAFGIGLERI AMLLYSIPDI RLFWSSDERF
LSQFSEQKPI RRFVPFSKYP ACFKDVSFWL KSSSSAAGGG GAAAQAPGTV SSNPSGANNA
IPPASPTPPP QSSSFHENDV MEIAREVGGD LIEDVRLTDQ FVHPKTARRS MCYRINYRNL
ERTLTNEETN ELHERLRALL VERLGVELR
//
