ID A0A2I1GF64_9GLOM Unreviewed; 601 AA.
AC A0A2I1GF64;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, 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=RhiirA4_515995 {ECO:0000313|EMBL:PKY45235.1}, RhiirC2_777869
GN {ECO:0000313|EMBL:PKK71872.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY45235.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY45235.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY45235.1,
RC ECO:0000313|Proteomes:UP000234323}, and C2
RC {ECO:0000313|EMBL:PKK71872.1, ECO:0000313|Proteomes:UP000233469};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKK71872.1, ECO:0000313|Proteomes:UP000233469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2 {ECO:0000313|EMBL:PKK71872.1,
RC ECO:0000313|Proteomes:UP000233469};
RA Chen E.C.H., Morin E., Baudet D., Noel J., Ndikumana S., Charron P.,
RA St-Onge C., Giorgi J., Grigoriev I.V., Roux C., Martin F.M., Corradi N.;
RT "Extensive intraspecific genome diversity in a model arbuscular mycorrhizal
RT fungus.";
RL Submitted (OCT-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:PKY45235.1}.
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DR EMBL; LLXL01000478; PKK71872.1; -; Genomic_DNA.
DR EMBL; LLXI01000368; PKY45235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1GF64; -.
DR VEuPathDB; FungiDB:FUN_003980; -.
DR VEuPathDB; FungiDB:GLOIN_2v1777183; -.
DR VEuPathDB; FungiDB:RhiirA1_460995; -.
DR OrthoDB; 5473299at2759; -.
DR Proteomes; UP000233469; Unassembled WGS sequence.
DR Proteomes; UP000234323; 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 ECO:0000313|EMBL:PKY45235.1}; 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:UP000234323}.
FT DOMAIN 302..378
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 601 AA; 67958 MW; C93F8CBD7834C7E9 CRC64;
MPVVHVDKEE FYKALGKEYS TDEFSELCFD FGLELEEDTS EKELAIREVG TIKAEGLSEK
PILKIEIPAN RYDLLCHEGI SRAFLIFQGK AKPPTYKVVD PKDGQIQITV KSETAQIRPH
VVGAILRDIS FNEKNYSNFI ELQEKLHINL CRKRTLVAIG THDLDTLKPP FTYEALPPKS
IKFAPLNQPK EYDGEELMKF YEADKHIGKF LHIIRDSPVY PVIYDTNRVV CSLPPIINGD
HSKITLNTKN VFIECTATDL TKAKIVLNTI VTMFSEYCAE PFTIEPVEVI YPDGKICTYP
DLSPRFIKVK ADYINACIGV MLTSSEIITY LNRMALSAKL VNEAELSVEI PPTRADILHA
CDVMEDVAIA HGFNNIPKKT LKIINSTGKA LPINKLSDLV RKEIALSGWS EVLPLILCSH
DENFAYLNKK DDNSTAVKLE NPKTLEYQVV RSSLLPGILK TVRENKKHAL PIKVFEVSDV
VLKDDSLERK TRNERHVCAI YCAKVSGFEL IHGLVNRLMD MLNVKLVSVN GDDVGYYIKE
SENPTYFPNR CADIFLRRSS KSSSIVTSKI GNFGILHPNV LEKFEIMYPC SVVEFNLEEF
I
//
