ID Q5DAZ9_SCHJA Unreviewed; 497 AA.
AC Q5DAZ9;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:AAW27007.1};
RN [1] {ECO:0000313|EMBL:AAW27007.1}
RP NUCLEOTIDE SEQUENCE.
RA Han Z.;
RT "The full-length cDNA sequences of Schistosoma japonicum genes.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAW27007.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16617374; DOI=10.1371/journal.ppat.0020029;
RA Liu F., Lu J., Hu W., Wang S.Y., Cui S.J., Chi M., Yan Q., Wang X.R.,
RA Song H.D., Xu X.N., Wang J.J., Zhang X.L., Zhang X., Wang Z.Q., Xue C.L.,
RA Brindley P.J., McManus D.P., Yang P.Y., Feng Z., Chen Z., Han Z.G.;
RT "New perspectives on host-parasite interplay by comparative transcriptomic
RT and proteomic analyses of Schistosoma japonicum.";
RL PLoS Pathog. 2:268-281(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY815275; AAW27007.1; -; mRNA.
DR AlphaFoldDB; Q5DAZ9; -.
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; IPR040724; PheRS_DBD1.
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; PF18552; PheRS_DBD1; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 346..479
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 497 AA; 56719 MW; 7F776100F543EFE7 CRC64;
MDIQNTILHT LDNKDYFKSD KLAEELGVDH QVVVGGIKRL ENYSGIIDCE NVVDVILQLT
EEGDEMLNNG SHEYKVYCAI PESGIPQSDI LRTFSSAKIG ISKALSLKWI SLIKNEDGVP
YLHRLIPEVK DDVQQLLLEV KESKRPLSDN EKSQLKKRKL ITELRRTSYM VRKGPSFSTN
IRSEETDLSS DLLSSGEWQT AQFKAYNFNA LGATLPSGHL HPLLRVRSEF CRILCDMGFS
EMPTNNYVEC SFWNFDSLFQ PQQHPARDAH DTFFLSDPET SIINNTIETS YIDKVSTVHS
QGAFGSRGYQ SPWLVKEAEK NLLRTHTTAV SARMLYALSK KNPFTPAKYY SIDRVFRNEN
LDATHLAEFH QVEGLVADFG LSLGHLKAVI RTFFLNWDFT KLRFKPGYNP FREPSMEIFS
YHPGFNKGVE IGISGLFRPE MLRPMGLPEG LSVIAWGLSL ERPTMIRYGY KNIRDLIGPK
IDLNMIYKAP LCRMYKC
//