ID   Q5KJG7_CRYNJ            Unreviewed;       351 AA.
AC   Q5KJG7; Q55WT0;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 2.
DT   24-JAN-2024, entry version 133.
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};
GN   OrderedLocusNames=CNC06600 {ECO:0000313|EMBL:AAW42606.2};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW42606.2, ECO:0000313|Proteomes:UP000002149};
RN   [1] {ECO:0000313|EMBL:AAW42606.2, ECO:0000313|Proteomes:UP000002149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017343; AAW42606.2; -; Genomic_DNA.
DR   RefSeq; XP_569913.1; XM_569913.1.
DR   AlphaFoldDB; Q5KJG7; -.
DR   STRING; 214684.Q5KJG7; -.
DR   PaxDb; 214684-Q5KJG7; -.
DR   EnsemblFungi; AAW42606; AAW42606; CNC06600.
DR   GeneID; 3256558; -.
DR   KEGG; cne:CNC06600; -.
DR   VEuPathDB; FungiDB:CNC06600; -.
DR   eggNOG; KOG2783; Eukaryota.
DR   HOGENOM; CLU_022696_0_1_1; -.
DR   InParanoid; Q5KJG7; -.
DR   OrthoDB; 1095527at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
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; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0070156; P:mitochondrial phenylalanyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
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:UP000002149};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          25..227
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   DOMAIN          229..351
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
SQ   SEQUENCE   351 AA;  39809 MW;  FF5FA7B5DC1B67FF CRC64;
     MLRTHTSAHE VESYRRGLDR WLLSADVYRR DEIDGSHYPV FHQMEGTHVW PVSELHTLPA
     LNAQLEASLA ACPILIEDTT RISPSNPYQP THDPVHAAEI TKHLKHSLNG LIFRLFGHVA
     AQRQGGGAPK EPLRVRWIEA YFPFTSPSYE VEVWWEGEWL ELLGCGVVMQ KTLDEAGVPD
     KAGWAFGLGL ERLSMVLFSI PDIRLFWTTD QRFHSQFSQD QITTFVPYSR YPECYKDMSF
     WLPVGSVGVA GSEGETKTGS GSAAAGVSAA GGKGRVFHEN DYFEIVREVA GDLVETVSLI
     DEFTHPKTNR QSRCYRLNYR HMDRSLSNEE VNVLQQEVQK RVVEEMGIEM R
//