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Database: UniProt
Entry: A0CJC7_PARTE
LinkDB: A0CJC7_PARTE
Original site: A0CJC7_PARTE 
ID   A0CJC7_PARTE            Unreviewed;       576 AA.
AC   A0CJC7;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=GSPATT00000605001 {ECO:0000313|EMBL:CAK70894.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK70894.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK70894.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK70894.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR   EMBL; CT868096; CAK70894.1; -; Genomic_DNA.
DR   RefSeq; XP_001438291.1; XM_001438254.1.
DR   AlphaFoldDB; A0CJC7; -.
DR   STRING; 5888.A0CJC7; -.
DR   EnsemblProtists; CAK70894; CAK70894; GSPATT00000605001.
DR   GeneID; 5024077; -.
DR   KEGG; ptm:GSPATT00000605001; -.
DR   eggNOG; KOG2472; Eukaryota.
DR   HOGENOM; CLU_020279_2_0_1; -.
DR   InParanoid; A0CJC7; -.
DR   OMA; FPGRCAN; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 3.30.56.10; -; 2.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR040659; PhetRS_B1.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   NCBIfam; TIGR00471; pheT_arch; 1.
DR   PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF18262; PhetRS_B1; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR   PROSITE; PS51483; B5; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT   DOMAIN          281..357
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   576 AA;  66149 MW;  BFF05F1DC1D718B9 CRC64;
     MPKISSDKKL FFKLLGKELN EEELEELVFR FGIEVEEREE EPDLLYFEIA ANRPDLLCIE
     NVVHALRIYM GLEKKRVYTF TPAKETIYVK AATQQIRPFV VGAILRDVTL TEDSFKSFLS
     FQDKIHQNYA RKRTLVSIGT HDLDKIEGPF FYDAKAPYDI VFQALKQTEQ MNCIDLFNKL
     REDQYLKGYL KIIENSPVYP VIYDNQKRVC SLPPIINGEH SKMSAETRNI LIEVTAIDEQ
     RALHTLNCLI SGFAIYNQKL NIEKVNIVYE LSQKQVVTPI VDERTLTTNI QYINKILGIN
     ITTQQACDLL LTMGIDSVAK DENILDCQVP FYRSDILQQC DIAEEIGIAY DYNKIEFKVP
     ETATTGSEYR LNKLSDMVRE EVALCGFVEC LNFVLMSIDE QTKMLNRPNL QNYVSLNNSK
     TPQFQSVRST LIPGILHTLQ ANSDSKLPIK LFEVSDVCVK GLKSEKDGFQ KGEGQVGAHN
     QRNLVAIHSS SKKTELEILH GLLDQLMIKL RVKKTDYHLK QSNDPLFFHQ LQAQIIYKDQ
     PIGGLGVVHP EVLERFDWKY PVTLLEMNIQ VILNDF
//
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