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Database: UniProt
Entry: A0A1L7WJ13_9HELO
LinkDB: A0A1L7WJ13_9HELO
Original site: A0A1L7WJ13_9HELO 
ID   A0A1L7WJ13_9HELO        Unreviewed;       485 AA.
AC   A0A1L7WJ13;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
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=PAC_02646 {ECO:0000313|EMBL:CZR52769.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR52769.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR52769.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR52769.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJOG01000003; CZR52769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WJ13; -.
DR   STRING; 576137.A0A1L7WJ13; -.
DR   OrthoDB; 1095527at2759; -.
DR   Proteomes; UP000184330; 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:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
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   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CZR52769.1};
KW   Ligase {ECO:0000313|EMBL:CZR52769.1};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          98..380
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   DOMAIN          382..485
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
FT   REGION          217..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  55184 MW;  937378427DB101B9 CRC64;
     MRPLTSTKRF SSGTEALALF IGLSNAIPRR WGACVPCRYN SNTSTSPETI TIEGKSYQKD
     SWHNLPPNIT SSISRRLHVQ KDHPISITRS IIESRFPSPT YAHHNTLFPI VSTYQNFDSL
     GFPLDHPGRS KTDTYYINAS TVLRTHTSAH QADTFRANAS EGFLISADVY RRDAIDRSHY
     PVFHQMEGAR MWDRSKVLNG DIAKAVWADM EKLSKHGMKV EDPNPPTHEE RNPLQSEHSL
     QEAEAIAAHL KRSLELVVVE IFTRAKQAAL KADPSFIDEP LRVRWIEAYF PFTSPSWELE
     VFWQGDWLEV LGCGVVKQDL FKNADVPDQL GWAFGIGLER IAMLLFEIPD IRLFWSKDPR
     FLDQFKGVSE DLDKLRKFVP FSKYPACYKD VAFWLKSSSS AAGGGGMEME FHENDVMEIV
     RDAAGDIVED VSMTDSFVHP KTGRKSLCYR VNYRSLERTL TNEEANEVHE RVRGALVEKL
     GVELR
//
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