ID A0A091GWQ6_9AVES Unreviewed; 401 AA.
AC A0A091GWQ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=N303_07655 {ECO:0000313|EMBL:KFO78547.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO78547.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO78547.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO78547.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: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; KL447914; KFO78547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GWQ6; -.
DR STRING; 55661.A0A091GWQ6; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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 CDD; cd00496; PheRS_alpha_core; 1.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 47..296
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 308..400
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO78547.1"
FT NON_TER 401
FT /evidence="ECO:0000313|EMBL:KFO78547.1"
SQ SEQUENCE 401 AA; 47139 MW; 062B1CF65806AA90 CRC64;
VELLGKAYPQ DDYSNVTEKI LSKVGKNLHN KKHHPLWLIK EQVKDHFYKQ YLGRRGTPLF
SVYDGLSPVV TVQQNFDSLL IPQNHASRRK EDNYYLNRDH MLRAHTSAHQ WDLIHSGLDA
FLAVGDVYRR DTIDNTHYPV FHQMEGVRLF SCHELFSNIK DGEGLQLFEQ GHRTAHKQEC
HTMEAVRLVE FNLKQVLTKL MTHIFGDGLQ VRWVDCYFPF THPSFEMEIN FQGEWMEVLG
CGVMEQQLVN SAGAQDKIGW AFGLGLERLA MILYNIPDIR LFWSEDERFL KQFIVPHIWQ
KIEFQPLSRY PPLINDISFW LPFETYSKND FYDLARNIGG DLIEKVVLVD EFTHPKTKKV
SHCYRIIYRH PERTLTQNEV HRIHQAIEES AIRELGVEGR F
//
