ID A0A1V6TW18_9EURO Unreviewed; 512 AA.
AC A0A1V6TW18;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN ORFNames=PENFLA_c003G06929 {ECO:0000313|EMBL:OQE30567.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE30567.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006703}.
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:OQE30567.1}.
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DR EMBL; MLQL01000003; OQE30567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TW18; -.
DR STRING; 254877.A0A1V6TW18; -.
DR OrthoDB; 4619at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.10.10.2320; -; 1.
DR Gene3D; 1.10.10.2330; -; 1.
DR Gene3D; 3.30.1370.240; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR040725; PheRS_DBD3.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF18553; PheRS_DBD3; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT DOMAIN 223..505
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 276..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 57641 MW; FBAAC11AC6B394DC CRC64;
MASDLTNQIL DALSASDAPI LSSEAFPSTP SLNVKSALDR LESRQMVQYE TLEKEIVTLT
AEGQEIAANG SHEAKVFAVV LAAMDGLKIS DLPGIVGKEN AKVGQGNAFK RGWIKKDKDL
LRASADSIVD ETQQQLLAVQ KTKTLDDKKV VADLKRRKLI GLAKELAFKI TKGPKYAREF
VKEQTDLTPE MIANGSWKTA HLKPYNFNAK GAPTPSGTLH PLNKVRQEFR NIFFDMGFEE
MPTNRFVETG FWNFDALFVP QQHPARDLQD TFYISDPAVA DPPREDPPNE PNPPAQLKAD
NPLDYKKYWD NVREVHEHGK FGSIGYRYPW SADESLRLVL RTHTTSISTY MLHKLAANPR
PARFFSIDRV FRNESVDATH LAEFHQVEGV IADFGLTLGG LIGFMEVFFA KMGIHKLRFK
PAYNPYTEPS MEIFGYHDGL GKWVEIGNSG MFRPEMLESM GLPKDLRVYG WGLSLERPTM
IKYGVSNIRE LLGHKVDLHF IETNPAVRLE KD
//
