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Database: UniProt
Entry: A0A0F4G649_9PEZI
LinkDB: A0A0F4G649_9PEZI
Original site: A0A0F4G649_9PEZI 
ID   A0A0F4G649_9PEZI        Unreviewed;       541 AA.
AC   A0A0F4G649;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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 alpha subunit {ECO:0000256|ARBA:ARBA00030612};
GN   ORFNames=TI39_contig5844g00008 {ECO:0000313|EMBL:KJX92497.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX92497.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX92497.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX92497.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006703}.
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:KJX92497.1}.
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DR   EMBL; LAFY01005799; KJX92497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4G649; -.
DR   STRING; 1047168.A0A0F4G649; -.
DR   OrthoDB; 4619at2759; -.
DR   Proteomes; UP000033647; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   Gene3D; 1.10.10.2320; -; 1.
DR   Gene3D; 1.10.10.2330; -; 1.
DR   Gene3D; 3.30.1370.240; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   NCBIfam; TIGR00468; pheS; 1.
DR   PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:KJX92497.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:KJX92497.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT   DOMAIN          390..510
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  60871 MW;  FE5F9E1AD56B2993 CRC64;
     MPGTRGPVPV PMNQTNGSNG EGRDLTLDIL HQLESTNPFK TEDVYPQKSQ AELKAALDRL
     ASRAMVEYDT NDTEQVILTG EGQQICDDGS HEYKVWEAVK KAGRLGLKDP ALSTASAKIG
     QGNAFKQQWV KKDGDALIPL KDTVVDATRE TLKYVHEYHT VPDQRQLKDF QKRKLVTTQK
     IITYEVRKGP KWGLEIPVEV TDLTADMLED GTWKSAAFKP YNFSALGAQQ NAGTLHPLNK
     VREEFRKIFF NWDFIEMPTG RFVDTGFWNF DALFVPQQHP ARDMQDTFYV SDPAEAGPPG
     PDPLADAALS KMEAESQLFS SNKADTPSTS KLDYDQYYAD IKAVHQDGKF GSVGYRYPYT
     DSETRKLVLR THTTAVSTYC LHRLAANPRP ARYFSIDRVF RNETVDATHL AEFHQIEGVI
     ADYGLTLGGL QAFLGKFFEQ LGITNLRFKP AYNPYTEPSM EVFGFHRGLD KWVEIGNSGM
     FRPEMLLPMG LPADLRVYGF GLSLERPTMI KYGVSNIREL LGHKVDLGFI ENNAAVRLDK
     D
//
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