ID S3CYG1_GLAL2 Unreviewed; 467 AA.
AC S3CYG1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=GLAREA_03612 {ECO:0000313|EMBL:EPE30645.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE30645.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE30645.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(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; KE145363; EPE30645.1; -; Genomic_DNA.
DR RefSeq; XP_008082056.1; XM_008083865.1.
DR AlphaFoldDB; S3CYG1; -.
DR STRING; 1116229.S3CYG1; -.
DR GeneID; 19462667; -.
DR KEGG; glz:GLAREA_03612; -.
DR eggNOG; KOG2783; Eukaryota.
DR HOGENOM; CLU_022696_0_1_1; -.
DR OMA; PISHYPQ; -.
DR OrthoDB; 1095527at2759; -.
DR Proteomes; UP000016922; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 145..358
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 360..467
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 467 AA; 52808 MW; ADF6168576E78065 CRC64;
MVLRGDLRAA ANAGITRQAS ASAFPGKITL GGKEYQKDNW FNVPDSIANS LTRELHNTPD
HPISITRSIV ESKFPSPTFK HYNKFFPVVS THENFDSLGF PADHPGRSKT DTYYVNEKTV
LRTHTSAHEL AIFGANESVG YTCSADVYRR DAIDKTHYPI FHQMEGARMW DRRKAPGGNI
VQAVWDDISN LPTHDMIVED PNPPTHPERN PLQHGHSHDE AEAIAAHLKR SLELMVVEIF
SRAKTAAIAA DPNYHDEPLK VRWIEAYFPW TSPSWELEIF WQGDWLEVLG CGVVKQELLE
NAGVPSQLGW AFGIGLERIA MLLFEIPDIR LFWSQDARFL DQFKGVSSDL TSLKRYVPFS
KYPACYKDVA FWLQPSSSST TSAAGGLAPV QSFHENDVME IVREIGGDVV EDVRKTDEFT
HPKTGRKSLC YRINYRSLER TLTNEEANEF HEQVRAALAR RLGVVLR
//
