ID   SYFM_SCHPO              Reviewed;         429 AA.
AC   O74952;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Phenylalanine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase;
DE   Flags: Precursor;
GN   Name=mfs1; ORFNames=SPCC736.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA19267.1; -; Genomic_DNA.
DR   PIR; T41560; T41560.
DR   RefSeq; NP_587774.1; NM_001022767.2.
DR   AlphaFoldDB; O74952; -.
DR   SMR; O74952; -.
DR   STRING; 4896.SPCC736.03c.1; -.
DR   MaxQB; O74952; -.
DR   PaxDb; O74952; -.
DR   EnsemblFungi; SPCC736.03c.1; SPCC736.03c.1:pep; SPCC736.03c.
DR   GeneID; 2538914; -.
DR   KEGG; spo:SPCC736.03c; -.
DR   PomBase; SPCC736.03c; -.
DR   VEuPathDB; FungiDB:SPCC736.03c; -.
DR   eggNOG; KOG2783; Eukaryota.
DR   HOGENOM; CLU_022696_0_1_1; -.
DR   OMA; SKSDTYY; -.
DR   PhylomeDB; O74952; -.
DR   PRO; PR:O74952; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:PomBase.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:PomBase.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
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   3: Inferred from homology;
KW   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           ?..429
FT                   /note="Phenylalanine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000316581"
FT   DOMAIN          339..429
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT   BINDING         115..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  50188 MW;  D3919AA462884AE4 CRC64;
     MFPHRVSHLS KLFSRRFPNW KRKVQTDSWS NVPEHIHSKI GRNLFQKEGH PICSLRQLLE
     QQFQKFEMNN VQKESPIVSV ETNFDSLGFP KTHVSRSKSD TYYMNNKTCL RTHTSAHQPE
     EFSRLAKEGF KKNGFLITAD VYRRDEVDSS HYPIFHQMEG ALVWNRNDTA KMKNDLKKVA
     LSPSLKSMVD DETTALETHN DMQDIYSLEE TKFVSQHLKD TLTTVIHDLV SLAPSISSGA
     EQVRYRWTYD SFPFTKPSFQ LEIDWKGKWL EILGCGVVQD RLLKGAGLNN YIGWAFGIGL
     ERLAMILYGI PDIRLFWSLD ERFSKQFLPN KISTFKPFSK YPACFKDIAF WINNDFNPND
     FYEIIRDVCQ DMVESVNLID QYTAKSGKTS LCYRVNYRSM ERSLRNEEID KLQEKLRNRV
     ANSLRVELR