SYFA_DANRE
ID SYFA_DANRE Reviewed; 497 AA.
AC Q1JPX3; Q6NYF9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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; ORFNames=zgc:136506, zgc:158185;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 alpha and
CC beta subunits. {ECO:0000250|UniProtKB:Q9Y285}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}.
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; BC066611; AAH66611.1; -; mRNA.
DR EMBL; BC116564; AAI16565.1; -; mRNA.
DR RefSeq; NP_001038760.2; NM_001045295.2.
DR AlphaFoldDB; Q1JPX3; -.
DR SMR; Q1JPX3; -.
DR STRING; 7955.ENSDARP00000034945; -.
DR PaxDb; Q1JPX3; -.
DR Ensembl; ENSDART00000164767; ENSDARP00000132548; ENSDARG00000098825.
DR GeneID; 692329; -.
DR KEGG; dre:692329; -.
DR CTD; 2193; -.
DR ZFIN; ZDB-GENE-050512-2; farsa.
DR eggNOG; KOG2784; Eukaryota.
DR GeneTree; ENSGT00390000006387; -.
DR HOGENOM; CLU_025086_2_2_1; -.
DR InParanoid; Q1JPX3; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 733355at2759; -.
DR PhylomeDB; Q1JPX3; -.
DR TreeFam; TF300647; -.
DR PRO; PR:Q1JPX3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000098825; Expressed in bone element and 29 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS: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:0048856; P:anatomical structure development; IEA:UniProt.
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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..497
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000280451"
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 CONFLICT 106
FT /note="K -> E (in Ref. 1; AAI16565)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> E (in Ref. 1; AAI16565)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="N -> S (in Ref. 1; AAH66611)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="Q -> R (in Ref. 1; AAI16565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 56364 MW; 2621B545376CA73D CRC64;
MADTGLLEAL LQRVEQLDGG VDSQDVSAAL GVDHQLVVGA VKSLQALGEV ISAEQKSSKH
WELTGEGREI AEQGSHEARV FNAIPAEGLP QNQLMKMASG KVGFSKAMSN KWIRLDKAHE
GGPRVFRTVE SIEDTVRDKL QLVQNGQSAK LEEKEKNELK KRKLLAEVTV KSYWITKGNS
FSTTITKQET ELTPEMIASG NWKEKKFKPY NFEAMGVAPD CGHLHPLMKV RTQFRQIFLE
MGFTEMPTNN FIESSFWNFD SLFQPQQHPA RDQHDTFFIS DPALAHEFPR DYLERVKKVH
SEGGYGSQGY KYDWKIEEAQ KNLLRTHTTA VSARMLYKLA QQEKFTPVKY FSIDRVFRNE
TLDATHLAEF HQIEGVVADY GLTLGNLMGV LHQFFTKLGI TKLRFKPAYN PYTEPSMEVF
SYHEGLKKWV EVGNSGVFRP EMLLPMGLPE GVSVIAWGLS LERPTMIKYG INNIRELVGH
KVNLQMVYDS PICRLDS
