SYFM_DICDI
ID SYFM_DICDI Reviewed; 454 AA.
AC Q86A68; Q556D2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phenylalanine--tRNA ligase, mitochondrial;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase;
DE Short=PheRS;
DE Flags: Precursor;
GN Name=mpheS; ORFNames=DDB_G0274371;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Is responsible for the charging of tRNA(Phe) with
CC phenylalanine in mitochondrial translation. {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000012; EAL70078.1; -; Genomic_DNA.
DR RefSeq; XP_643878.1; XM_638786.1.
DR AlphaFoldDB; Q86A68; -.
DR SMR; Q86A68; -.
DR STRING; 44689.DDB0231330; -.
DR PaxDb; Q86A68; -.
DR PRIDE; Q86A68; -.
DR EnsemblProtists; EAL70078; EAL70078; DDB_G0274371.
DR GeneID; 8619304; -.
DR KEGG; ddi:DDB_G0274371; -.
DR dictyBase; DDB_G0274371; mpheS.
DR eggNOG; KOG2783; Eukaryota.
DR HOGENOM; CLU_022696_0_1_1; -.
DR InParanoid; Q86A68; -.
DR OMA; SKSDTYY; -.
DR PhylomeDB; Q86A68; -.
DR PRO; PR:Q86A68; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 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 PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 2.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..454
FT /note="Phenylalanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000327805"
FT DOMAIN 361..454
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170..172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 53179 MW; 55572EDEA2CF8E0D CRC64;
MIKILRNINN NIVNRYDGLN KSYLNINFYC STTNNSSGKI DYTKLIPENG NISKSITEKI
GKNLHCKRDH PLNIIKKKIQ YHFQNKLSDE EHKFQFFDSF EPKVSVKENF DELLFPVDHV
GRSPNDTYYF SKDQLLRTHT SAHQSQLLRE QEKAFLVTGD VYRRDTIDAV HYPVFHQMEG
VKVFKDKVNL AIDGKPFDET IDYYEDNNYK QLQSVKDVEK DLKQSLESMI RSVIGQDLQV
RWIDAYFPFT SPSFEMEIYF QGQWLEVLGC GVVHPSIMNN CGLSNDRAWA FGIGLERLAM
ILFNIPDIRL FWTEDNRFHN QFKGVDKSIS TSSSSSSSSS SSSSSTLSDI DIKGVQFQQF
SKYPSCFKDV SFWLEDEENF HENKFYEFVR ESCGDLVERV DLVDNFTNKK LNKTSHCYRI
YYRSMDRNLT NEEIDILQFN LREKLENHLS VKLR
