ID A0A095ALI2_SCHHA Unreviewed; 523 AA.
AC A0A095ALI2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 32.
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};
DE Flags: Fragment;
GN ORFNames=MS3_03219 {ECO:0000313|EMBL:KGB34986.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB34986.1};
RN [1] {ECO:0000313|EMBL:KGB34986.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
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; KL250648; KGB34986.1; -; Genomic_DNA.
DR RefSeq; XP_012794752.1; XM_012939298.1.
DR AlphaFoldDB; A0A095ALI2; -.
DR STRING; 6185.A0A095ALI2; -.
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 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 Ligase {ECO:0000313|EMBL:KGB34986.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 195..417
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 414..523
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGB34986.1"
SQ SEQUENCE 523 AA; 61070 MW; F6C614E9C89290FE CRC64;
FQRIFNYRVT VHINHILKIW ERLMRLNLCS CYFRLFRSSC VQPHRLLSTK QSLQPTAENP
TSSWVSIGGH STVKDSWYNL TPHMIELTKR SLHNQQHHPL NLIKQRIVDF MFKRHVRHVC
NNNQGGTPLF SLYDHLSPVV TVRKNFDSLF IPPDHPSRLR TDTYYLNETT VLRSHTSAHQ
LDLINSGLNA FLVAGDVYRR DDIDSLHYPV FHQLEGVRLF TSDELFRNAT DPFQCFRLFE
DIPSSSPYSE PDVHPFKVFP SYMLPPDRQI SHTTETKMLL EFELKTLLQE MAKFLFGPDI
QLRWVSAYFP FTHPSWELEI KTNSGYSNYD DDSDSEKPEE WTEMLGCGIM RQELLERSGI
PNKVGYAFGL GLERWAMQLY EIPDIRLFWS KDEGFLNQFI TDDIHAPIKY KPVSIFPPCV
LDLSFWLNNS QSISSSLSSN SDGLDRIKIV ERDIFDIVRS EAGDLIEQIR LVDSYNDLKT
GQQSLCYRFI YRDQHKTLTV DDVRPLHENI AQVLAEKLNL SIR
//
