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Database: UniProt
Entry: E2L929_MONPE
LinkDB: E2L929_MONPE
Original site: E2L929_MONPE 
ID   E2L929_MONPE            Unreviewed;       211 AA.
AC   E2L929;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE   Flags: Fragment;
GN   ORFNames=MPER_02484 {ECO:0000313|EMBL:EEB98072.1};
OS   Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS   disease fungus) (Marasmius perniciosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB98072.1, ECO:0000313|Proteomes:UP000000741};
RN   [1] {ECO:0000313|EMBL:EEB98072.1, ECO:0000313|Proteomes:UP000000741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX   PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA   Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA   Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA   Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA   Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA   Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA   Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT   "A genome survey of Moniliophthora perniciosa gives new insights into
RT   Witches' broom disease of cacao.";
RL   BMC Genomics 9:548-548(2008).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEB98072.1}.
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DR   EMBL; ABRE01004891; EEB98072.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2L929; -.
DR   STRING; 554373.E2L929; -.
DR   KEGG; mpr:MPER_02484; -.
DR   HOGENOM; CLU_022696_1_1_1; -.
DR   InParanoid; E2L929; -.
DR   OrthoDB; 1095527at2759; -.
DR   Proteomes; UP000000741; Unassembled WGS sequence.
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:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 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:UP000000741}.
FT   DOMAIN          31..211
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEB98072.1"
FT   NON_TER         211
FT                   /evidence="ECO:0000313|EMBL:EEB98072.1"
SQ   SEQUENCE   211 AA;  24185 MW;  DE5B4C6D8981CE4D CRC64;
     TPYKNFDELS FPADHPGRSV TDSYYINKNL MLRTHTSAHE VEVFKQKETK WLLTADMEGA
     RLFDASAQGM KEVEEDSERI ARHLEQSNII IEDVPHISPT NPVQECHDPV YAEAVTRNLK
     LSLNSLILRL FGGHTHEEPL KVRWIEAYFP FTSPSFEVEV FFRGKWLEIL GCGVIRQATL
     DKSGVHDKIG WAFGLGFERI AMVLYSIQTF D
//
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