SYFM_RAT
ID SYFM_RAT Reviewed; 472 AA.
AC Q6AYQ3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phenylalanine--tRNA ligase, mitochondrial;
DE EC=6.1.1.20 {ECO:0000250|UniProtKB:O95363};
DE AltName: Full=Phenylalanyl-tRNA synthetase;
DE Short=PheRS;
DE Flags: Precursor;
GN Name=Fars2; Synonyms=Fars1;
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=Kidney;
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26553276; DOI=10.1002/humu.22930;
RA Yang Y., Liu W., Fang Z., Shi J., Che F., He C., Yao L., Wang E., Wu Y.;
RT "A newly identified missense mutation in FARS2 causes autosomal-recessive
RT spastic paraplegia.";
RL Hum. Mutat. 37:165-169(2016).
CC -!- FUNCTION: Is responsible for the charging of tRNA(Phe) with
CC phenylalanine in mitochondrial translation. To a lesser extent, also
CC catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to
CC tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA
CC to the ribosome and incorporation of ROS-damaged amino acid into
CC proteins. {ECO:0000269|PubMed:26553276}.
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:O95363};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. Mitochondrion
CC {ECO:0000269|PubMed:26553276}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the Purkinje cell of
CC cerebellum. {ECO:0000269|PubMed:26553276}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC078956; AAH78956.1; -; mRNA.
DR RefSeq; NP_001013157.1; NM_001013139.1.
DR AlphaFoldDB; Q6AYQ3; -.
DR SMR; Q6AYQ3; -.
DR STRING; 10116.ENSRNOP00000021660; -.
DR ChEMBL; CHEMBL3757; -.
DR PaxDb; Q6AYQ3; -.
DR PRIDE; Q6AYQ3; -.
DR Ensembl; ENSRNOT00000021660; ENSRNOP00000021660; ENSRNOG00000016135.
DR GeneID; 306879; -.
DR KEGG; rno:306879; -.
DR UCSC; RGD:1309416; rat.
DR CTD; 10667; -.
DR RGD; 1309416; Fars2.
DR eggNOG; KOG2783; Eukaryota.
DR GeneTree; ENSGT00940000158071; -.
DR HOGENOM; CLU_022696_1_0_1; -.
DR InParanoid; Q6AYQ3; -.
DR OMA; SKSDTYY; -.
DR OrthoDB; 1115196at2759; -.
DR PhylomeDB; Q6AYQ3; -.
DR TreeFam; TF105798; -.
DR PRO; PR:Q6AYQ3; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016135; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; Q6AYQ3; baseline and differential.
DR Genevisible; Q6AYQ3; RN.
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; IDA: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; 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 TIGRFAMs; TIGR00469; pheS_mito; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; 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 ?..472
FT /note="Phenylalanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035815"
FT DOMAIN 379..471
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT BINDING 157..160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193..195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95363"
SQ SEQUENCE 472 AA; 55165 MW; F0C90187062FBA20 CRC64;
MVCLAFIRAA HEHLYLVRKV SHVCRCHQHR AWGSRPAASQ FAVQGAPGRV LELLGKSYPQ
DDHTNLTQKV LSKVGRNLHN QKFHPLWLIK ERVKEHFYQQ YMGRSRTPLF SVYDQLSPVV
TTWQNFDSLL IPADHPSRKK GDNYYLNRGH MLRAHTSAHQ WDLLHAGLNA FLVVGDVYRR
DQIDSQHYPV FHQLEGVRLF SKHELFAGVK DGESLQLFEE SSRSAHKQET HTMEAVKLVE
FDLKQVLTRL VTHLFGDGLE VRWVDCYFPF THPSFEMEIN FRGEWLEVLG CGVMEQQLVN
SAGAQDRIGW AFGLGLERLA MVLYDIPDIR LFWSEDERFL KQFRLSDINQ SVKFQRWFFQ
EERATGIQRK MGRQLCPFSK YPAVFNDISF WLPSENYTEN DFYDIVRTVG GDLVEKVDLI
DKFEHPKTHR TSHCYRITYR HMERTLSQRE VSSVHQAVQE AAVQLLGVEG RF
