ID W6QVA4_PENRF Unreviewed; 512 AA.
AC W6QVA4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-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 alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN Name=FRS2 {ECO:0000313|EMBL:CDM33492.1};
GN ORFNames=PROQFM164_S03g000216 {ECO:0000313|EMBL:CDM33492.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM33492.1};
RN [1] {ECO:0000313|EMBL:CDM33492.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM33492.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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}.
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DR EMBL; HG792017; CDM33492.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QVA4; -.
DR STRING; 1365484.W6QVA4; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 4619at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CDM33492.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:CDM33492.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 223..505
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 512 AA; 57829 MW; FCAA1908A9964125 CRC64;
MASDLTNQIL DALSASDAPI LSSEAFPSTP SLNVKSALDR LDSRQMVEYE TLDKEIVTLT
AEGQEIATNG SHEAKVFAVV LAALDGLKIS DLPGIVGKEN AKVGQGNAFK RGWIKKDKDL
LRASTDSIVD ETQQQLLEVQ KTKNLDDKKA LADLKRRKLV GLAKEISFKF TKGPKYAREF
VKEQTDLTPE MIASGSWKTA HLKPYNFNAK GAPTPCGTLH PLNKVRQEFR NIFFEMGFEE
MPTNRFVETG FWNFDALFVP QQHPARDLQD TFYISDPAVA DAPREDPPND PHRPAQLKSE
KPLDYKKYWD NVREVHEHGK FGSIGYRYPW SADESLRLVL RTHTTSISTY MLHKLAANPR
PARFFSIDRV FRNESVDATH LAEFHQVEGV IADFGLTLGG LIGFMEVFFA KMGIHKLRFK
PAYNPYTEPS MEIFGYHDGL GKWVEIGNSG MFRPEMLESM GLPKDLRVYG WGLSLERPTM
IKYAVSNIRE LLGHKVDLDF IQTNPAVRLE KD
//