SYFA_DICDI
ID SYFA_DICDI Reviewed; 487 AA.
AC Q54KS8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=phesA; Synonyms=pheS; ORFNames=DDB_G0287141;
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=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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000098; EAL63845.1; -; Genomic_DNA.
DR RefSeq; XP_637352.1; XM_632260.1.
DR AlphaFoldDB; Q54KS8; -.
DR SMR; Q54KS8; -.
DR STRING; 44689.DDB0231328; -.
DR PaxDb; Q54KS8; -.
DR EnsemblProtists; EAL63845; EAL63845; DDB_G0287141.
DR GeneID; 8625974; -.
DR KEGG; ddi:DDB_G0287141; -.
DR dictyBase; DDB_G0287141; phesA.
DR eggNOG; KOG2784; Eukaryota.
DR HOGENOM; CLU_025086_2_2_1; -.
DR InParanoid; Q54KS8; -.
DR OMA; QIEGWVM; -.
DR PhylomeDB; Q54KS8; -.
DR PRO; PR:Q54KS8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:dictyBase.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:dictyBase.
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; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR040725; PheRS_DBD3.
DR Pfam; PF18553; PheRS_DBD3; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..487
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000327538"
FT BINDING 319
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 361..363
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 401
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 403
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000250|UniProtKB:A5K9S0"
FT BINDING 427
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
SQ SEQUENCE 487 AA; 56174 MW; 5A1FDBD76CF00D95 CRC64;
MNKEIFNSKL FEKLDKDNLI ENSREWSNEI DSTWNYNDVV GILKSWESLN TISLEYIDSI
VNCLTETGKD ILINGSPEAK LYNILTEQGM SPADANKQFG ATAFGSAKNK GWIEVKAGKI
FKKVESINDI VKSDLSIPDL SKLDSKTLEQ YKKSRFIEEK KLSYYRVTKG EQYNKRSKEL
SDLTIEMLKD DSWEKESFKV NINAMGVVPE QGYRHPLNKV KNEFKQIFLD MGFEEMPTFN
FVENGFWNFD ALFQPQQHPA RELQDTFFIK DPKTSHDFSD EYCERVKQVH SVGGYGSLGW
IYDWKLEEAE KNILRTHTTA VSARMLYKLA QNGFKPKKYF SIDRVFRNET LDATHLAEFH
QVEGVIADVD ISLGHLIGVI SEFFKRLGID NVRFKPAFNP YTEPSMEIFG YHPILKRWVE
LGNSGIFRPE LLLPMGIPEN VRVAAWGLSL ERPTMIKYGL DNIRAIFGNS INVNFIKNNP
ICMFESK
