SYFM_DROME
ID SYFM_DROME Reviewed; 453 AA.
AC O16129; Q9V6V8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable phenylalanine--tRNA ligase, mitochondrial;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase;
DE Short=PheRS;
DE Flags: Precursor;
GN Name=PheRS-m {ECO:0000312|FlyBase:FBgn0275436};
GN Synonyms=Aats-phe, Aats-phe-m {ECO:0000312|FlyBase:FBgn0275436}, Pts;
GN ORFNames=CG13348 {ECO:0000312|FlyBase:FBgn0275436};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9662479; DOI=10.1046/j.1365-2583.1998.00070.x;
RA Gray Y.H.M., Sved J.A., Preston C.R., Engels W.R.;
RT "Structure and associated mutational effects of the cysteine proteinase
RT (CP1) gene of Drosophila melanogaster.";
RL Insect Mol. Biol. 7:291-293(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Is responsible for the charging of tRNA(Phe) with
CC phenylalanine in mitochondrial translation. {ECO:0000250}.
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:P15625};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF012089; AAB65750.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF58310.1; -; Genomic_DNA.
DR EMBL; AY058580; AAL13809.1; -; mRNA.
DR RefSeq; NP_477283.1; NM_057935.5.
DR AlphaFoldDB; O16129; -.
DR SMR; O16129; -.
DR BioGRID; 62301; 4.
DR IntAct; O16129; 1.
DR STRING; 7227.FBpp0086720; -.
DR PaxDb; O16129; -.
DR PRIDE; O16129; -.
DR DNASU; 36547; -.
DR EnsemblMetazoa; FBtr0087594; FBpp0086720; FBgn0275436.
DR GeneID; 36547; -.
DR KEGG; dme:Dmel_CG13348; -.
DR CTD; 36547; -.
DR FlyBase; FBgn0275436; PheRS-m.
DR VEuPathDB; VectorBase:FBgn0275436; -.
DR eggNOG; KOG2783; Eukaryota.
DR GeneTree; ENSGT00940000158071; -.
DR HOGENOM; CLU_022696_1_0_1; -.
DR InParanoid; O16129; -.
DR OMA; SKSDTYY; -.
DR OrthoDB; 1115196at2759; -.
DR PhylomeDB; O16129; -.
DR SignaLink; O16129; -.
DR BioGRID-ORCS; 36547; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36547; -.
DR PRO; PR:O16129; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0275436; Expressed in thoracico-abdominal ganglion (Drosophila) and 30 other tissues.
DR Genevisible; O16129; DM.
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; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IMP:FlyBase.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IMP:FlyBase.
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 Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..453
FT /note="Probable phenylalanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035816"
FT DOMAIN 356..453
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT BINDING 142..145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171..173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178..180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 217..232
FT /note="SSKFMDQTKQPCHTLE -> HPSSWTKPNSPATRR (in Ref. 1;
FT AAB65750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 51996 MW; 4540742E54D1AE24 CRC64;
MLLTLRVQGA RHWLKSTRCL ASSAAPAKSP SSPPQLEVSG STYATDGWTN VTPKILSYVG
ANKHLQTDHP LSIIRQRIVN YFYGAYRNQR GNPLFSVYDQ MNPVVTVQQN FDNLLIPADH
VSRQKSDCYY INQQHLLRAH TTAHQVELIS GGLDNFLVVG EVYRRDEIDS THYPVFHQAD
AVRLVTKDKL FERNPGLELF EETWSGTLAD PKLILPSSKF MDQTKQPCHT LEAVKLMEHE
MKHVLVGLTK DLFGPRIKYR WVDTYFPFTQ PSWELEIYFK DNWLEVLGCG IMRHEILQRS
GVHQSIGYAF GVGLERLAMV LFDIPDIRLF WSNDSGFLSQ FSEKDLHNLP KYKPISHYPQ
CTNDLSFWLP QDIEVDAGFS PNDFYDLVRS VAGDMVEQIS LVDKFKHPKT GKSSVCFRIV
YRHMERTLTQ AEVNEIHKQI ASASVDSFNV QIR
