SYFA_RAT
ID SYFA_RAT Reviewed; 508 AA.
AC Q505J8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20 {ECO:0000250|UniProtKB:Q9Y285};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=Farsa; Synonyms=Farsla;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-12 AND 43-59, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=3880707; DOI=10.1016/0014-4827(85)90264-2;
RA Mirande M., Le Corre D., Louvard D., Reggio H., Pailliez J.P., Waller J.P.;
RT "Association of an aminoacyl-tRNA synthetase complex and of phenylalanyl-
RT tRNA synthetase with the cytoskeletal framework fraction from mammalian
RT cells.";
RL Exp. Cell Res. 156:91-102(1985).
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:0000250|UniProtKB:Q9Y285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19414;
CC Evidence={ECO:0000250|UniProtKB:Q9Y285};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and
CC FARSB. {ECO:0000250|UniProtKB:Q9Y285}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3880707}.
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; BC094515; AAH94515.1; -; mRNA.
DR RefSeq; NP_001019408.1; NM_001024237.1.
DR AlphaFoldDB; Q505J8; -.
DR SMR; Q505J8; -.
DR BioGRID; 252747; 1.
DR IntAct; Q505J8; 1.
DR MINT; Q505J8; -.
DR STRING; 10116.ENSRNOP00000004370; -.
DR iPTMnet; Q505J8; -.
DR PhosphoSitePlus; Q505J8; -.
DR jPOST; Q505J8; -.
DR PaxDb; Q505J8; -.
DR PRIDE; Q505J8; -.
DR Ensembl; ENSRNOT00000004370; ENSRNOP00000004370; ENSRNOG00000003149.
DR GeneID; 288917; -.
DR KEGG; rno:288917; -.
DR CTD; 2193; -.
DR RGD; 1310314; Farsa.
DR eggNOG; KOG2784; Eukaryota.
DR GeneTree; ENSGT00390000006387; -.
DR HOGENOM; CLU_025086_2_2_1; -.
DR InParanoid; Q505J8; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 733355at2759; -.
DR PhylomeDB; Q505J8; -.
DR TreeFam; TF300647; -.
DR PRO; PR:Q505J8; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000003149; Expressed in thymus and 20 other tissues.
DR Genevisible; Q505J8; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; ISS:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
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; IPR040724; PheRS_DBD1.
DR InterPro; IPR040586; PheRS_DBD2.
DR InterPro; IPR040725; PheRS_DBD3.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF18552; PheRS_DBD1; 1.
DR Pfam; PF18554; PheRS_DBD2; 1.
DR Pfam; PF18553; PheRS_DBD3; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT CHAIN 2..508
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000280449"
FT BINDING 329
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 372..374
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 412
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 414
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 438
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C7"
FT MOD_RES 311
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
SQ SEQUENCE 508 AA; 57720 MW; 78CE0B72EC5BF377 CRC64;
MADNPVLEQL LRRLEVADGG LDSAELATQL GVEHQAVVGA VKSLQALGEV IEAELRSTKC
WELTTEGEEI AREGSHEARV FRSIPLEGLV QSELMQLPSG KVGFSKAMSN KWIRVDKSAA
DGPRVFRVVD SIEDEVQRRL QQVQAGQAEK LAEKERNELR KRKLLTEVIL KTYWVSKGKG
FSTSVSKQEA ELSPEMISSG SWRDRPFKPY NFSARGVLPD SGHLHPLLKV RSQFRQIFLE
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
SQGGYGSQGY KYTWKLEEAR KNLLRTHTTA ASARALYRLA QKKPFTPAKY FSIDRVFRNE
TLDATHLAEF HQIEGVIADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH
KVNLQMVYDS PVCRLDIEPR SSKTQEAA
