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Database: UniProt
Entry: A0A061H5S9_9BASI
LinkDB: A0A061H5S9_9BASI
Original site: A0A061H5S9_9BASI 
ID   A0A061H5S9_9BASI        Unreviewed;       505 AA.
AC   A0A061H5S9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   13-SEP-2023, entry version 34.
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=PFL1_06396 {ECO:0000313|EMBL:EPQ25941.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25941.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ25941.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25941.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
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; KE361648; EPQ25941.1; -; Genomic_DNA.
DR   RefSeq; XP_007882130.1; XM_007883939.1.
DR   AlphaFoldDB; A0A061H5S9; -.
DR   GeneID; 19320474; -.
DR   KEGG; pfp:PFL1_06396; -.
DR   eggNOG; KOG2783; Eukaryota.
DR   HOGENOM; CLU_022696_0_1_1; -.
DR   OrthoDB; 1095527at2759; -.
DR   Proteomes; UP000053664; 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   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:UP000053664};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          57..343
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   DOMAIN          395..505
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
FT   REGION          347..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  56003 MW;  12051EC2E2B71407 CRC64;
     MSTSLTRSQQ GQRPSSLSVL GQTYASDDYT NLPSSILSRL APSPTLPYQP HHPLCLLRAQ
     IEEQLGAAYT PIRAPSPVVS THLNFEELGF PVDHPGRSPT DTYYLNRTTC LRTHTSAHEV
     ETFRNRHDRW LLTADVYRRD EIDASHYPIF HQMEGAAIFP TSAYAPGGQV ELECQEMEAR
     LARANLEIED TVDLDEAGGF QPTHDARSAQ LACRHLKATL NGLVLDLFGE RHAQEPSSSN
     GGGGGDPLRV RWIAATFPFT SPSFEVEVWF RGKWLEILGC GVVMENTLTK AGVNAVGGGG
     EKKMGWAFGL GLERIAMVLY SIPDIRLFWS QDRRFLDQFI VDPASDRGKR QEGFRDTIDG
     GGGGGKDETG VSAAGGAQSP TRTPRRKLVT FKPYSKYPPC YKDVSFWLPS SSSSACSQGS
     TATTITGGTR FHENDFYEIV RDTVADLAED VVKIDEFTHP KTGRASLCYR INYRSMDRSL
     ENEQVNALHA KVVQRLVDEM HLEIR
//
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