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Database: UniProt
Entry: A0A2C5XH83_9HYPO
LinkDB: A0A2C5XH83_9HYPO
Original site: A0A2C5XH83_9HYPO 
ID   A0A2C5XH83_9HYPO        Unreviewed;       610 AA.
AC   A0A2C5XH83;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=CDD81_6924 {ECO:0000313|EMBL:PHH62538.1};
OS   Ophiocordyceps australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH62538.1, ECO:0000313|Proteomes:UP000226192};
RN   [1] {ECO:0000313|EMBL:PHH62538.1, ECO:0000313|Proteomes:UP000226192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map64 {ECO:0000313|EMBL:PHH62538.1,
RC   ECO:0000313|Proteomes:UP000226192};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHH62538.1}.
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DR   EMBL; NJET01000069; PHH62538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5XH83; -.
DR   STRING; 1399860.A0A2C5XH83; -.
DR   OrthoDB; 5473299at2759; -.
DR   Proteomes; UP000226192; 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   CDD; cd00769; PheRS_beta_core; 1.
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:UP000226192}.
FT   DOMAIN          297..375
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   610 AA;  68718 MW;  1D00CCCD2FB5C30D CRC64;
     MPTISVDKYQ LFEALGKNFT RDEFEELCFE YGLELDEDTE GDDRPIINGV QEPPKLKIEI
     PANRYDMLCF EGIALNLNIF LGRVKPPNFR LVEPKSQTEQ TIVVAPETAR VRPYVAGAVL
     RNIKFTQDRY DSFIALQDKL HQNLARNRTL VSMGTHDLDT IQGPFTYEAL PPKDISFAPL
     NQTKVMNAEE LMTFYESDKH LGRYLHIIRD SPVYPVIYDA NRVVCSLPPI INGHHSRITL
     DTTNVFIEIT ATDVTKLKIV TDMLVTMFSA YCAEPFTVEP VQIVSEHNQM SCQTPSLHPR
     LTHAQVDYLN SCTGLNESPD SICKLLAKMA YDSRPSDTDA NILEVAIPPT RADVLHQCDI
     MEDLAVCYGF NKLPRTAPTR SATIGAPLMV NKLSDIVRIE AAMAGWSEVM PLTLCSHDEN
     FAWLNRKDDG NTVVRLANPK TLEYQVVRSS LLPGLLKTIR ENKGHSLPIK IFEVGDVVFK
     DESEERKARN QRHFAAAWCG KTSGFELVHG LLDRVLLMLR TAFVTHDEGL VAAGSLDYQV
     KQNPAKSDGY WIQELNDDTF FPGHAAAVYL RLGGKEQRIG EFGILHPTVL DKFDLRYPVS
     TLEVNLEVFL
//
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