ID A0A2A2J2T5_9BILA Unreviewed; 593 AA.
AC A0A2A2J2T5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=WR25_25439 {ECO:0000313|EMBL:PAV55971.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV55971.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV55971.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV55971.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(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:PAV55971.1}.
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DR EMBL; LIAE01010733; PAV55971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2J2T5; -.
DR STRING; 2018661.A0A2A2J2T5; -.
DR Proteomes; UP000218231; 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; 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; IPR040724; PheRS_DBD1.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF18552; PheRS_DBD1; 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:UP000218231}.
FT DOMAIN 325..575
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 593 AA; 67454 MW; 72A1C498327A10CC CRC64;
MANTCSRSTR NVDFEPEQKM ESIKELINKA GERARWNLCQ VLFRVAELPF PWMVDSSPDA
LNKLLADFPY IQSFEVTTRD FQVHPQILPA DLKNRPHLAR WHRNIAELKN SLNSESKMVA
STTEQVAQGG VENLPQMILE TIDKSKEPLD SLQYAAQLKI DHQRVVGAIK SLQAHEGLIE
VDEVSQKRLD LTAEGKEIAE GGSHEFKLFE HIGKDGAAQA ELNIRKKDSV VDECCKQLND
LSLGGNVDDK IKAELKKRKL VAEVVIKGFR VRKGSNFSVT ISKAEIDLTP DMITTGSWKT
ATFKKYNFDA MGVQPSCGHL HPLMKVRAEF RQIFFSMGFS EMQTNRYVES SFWNFDALFQ
PQQHPARDAH DTFFVSDPAA ATQFPQDYLE RVKTVHSKGG YGSSGYNYDW KLEEAQKNVL
RTHTTAVSAR QLYKLAQEGF KPARMFSIDR VFRNETLDAT HLAEFHQVEG VIAERNLSLG
HLIGVFTEFF KRMGIENLRF KPTYNPYTEP SMEIFAYHNG LKKWVEIGNS GMFRPEMLLP
MGLPEDVNVA GYGLSLERPT MIRYGINNIR DLFGPKVDLQ MIYDGPICRL DKD
//
