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Database: UniProt
Entry: A0A1E7FWF8_9STRA
LinkDB: A0A1E7FWF8_9STRA
Original site: A0A1E7FWF8_9STRA 
ID   A0A1E7FWF8_9STRA        Unreviewed;       652 AA.
AC   A0A1E7FWF8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=FRACYDRAFT_273892 {ECO:0000313|EMBL:OEU22465.1};
OS   Fragilariopsis cylindrus CCMP1102.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC   Fragilariopsis.
OX   NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU22465.1, ECO:0000313|Proteomes:UP000095751};
RN   [1] {ECO:0000313|EMBL:OEU22465.1, ECO:0000313|Proteomes:UP000095751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU22465.1,
RC   ECO:0000313|Proteomes:UP000095751};
RG   DOE Joint Genome Institute;
RA   Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA   Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA   Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA   Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA   Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA   Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA   Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT   "Extensive genetic diversity and differential bi-allelic expression allows
RT   diatom success in the polar Southern Ocean.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; KV784353; OEU22465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7FWF8; -.
DR   EnsemblProtists; OEU22465; OEU22465; FRACYDRAFT_273892.
DR   KEGG; fcy:FRACYDRAFT_273892; -.
DR   InParanoid; A0A1E7FWF8; -.
DR   OrthoDB; 5473299at2759; -.
DR   Proteomes; UP000095751; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IEA:InterPro.
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   ECO:0000313|EMBL:OEU22465.1}; 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:UP000095751}.
FT   DOMAIN          319..397
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   652 AA;  72418 MW;  76D7077420D59B4C CRC64;
     MPTVALEKDQ LFTHLGRTYT DDEFDELCFE FGVELDEITS EREEAEKSST VKLSKQQIAE
     LSENVIYKID IPANRYDLLC VEGLCRGLRI FLGDQDAPEY TIVEGEGAGG SATVTVIKTN
     TDTIRPFVVA AILKDVVFTP ERYASFIDLQ DQLHRNLCRQ RTLVAIGTHD LDTVEGPFVY
     DARPPTEIEF VPLTPDDRGA FNAKDLMEYY ETEVAVKHLK PYVPIIKNSP LYPVIVDSQN
     RVLSLPPIIN GTHSKITLDT KNVFIECTAT DLTKANIVLD TVVTMFSEYC AKPFTVVPVK
     VDYQDDSGNI VDSYVSPMLS KRRETAKIDF CNSLIGINLS PTEIQNLCNK VQLGPAQLLE
     NDTILEVTVP PTRSDILHAV DIAEDIAIAY GYNNIVKRVP KTNTVGGAEP LNQVGDLLRE
     EIGRAGYTEV LTHGLCSIHD NFTALQCPVR EDWAVSLSNP ANIEYQVVRT TLLPGLLKTF
     QHNKSASFAQ GFKLFEISDA VVIDRENSIT DTIVGARNVR KLCAAYAGPT SGFEIIHGLV
     DRIMTLMEVA PEASYVATSG KKSSATGGAD EEKYRISREG WYYTIAELPY NGNAHESKMY
     FPGRAAQVLL TKPSHKEKIR VGTFGILHPL VLKNFDIQYP SSVVEIDLEE LM
//
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