ID V4Y6G3_9ARCH Unreviewed; 312 AA.
AC V4Y6G3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=A07HN63_01823 {ECO:0000313|EMBL:ESS08326.1};
OS uncultured archaeon A07HN63.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412873 {ECO:0000313|EMBL:ESS08326.1, ECO:0000313|Proteomes:UP000030667};
RN [1] {ECO:0000313|Proteomes:UP000030667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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}.
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DR EMBL; KI543218; ESS08326.1; -; Genomic_DNA.
DR AlphaFoldDB; V4Y6G3; -.
DR STRING; 1412873.A07HN63_01823; -.
DR PATRIC; fig|1412873.3.peg.1932; -.
DR Proteomes; UP000030667; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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 NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 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:ESS08326.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:ESS08326.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 167..307
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 312 AA; 35446 MW; B1F6D39CF347C308 CRC64;
MAGIEAAETV DQLTPEMLTS GEWDDVEFAE YNVEADAPEI EGGRKHILRQ TADRAKDVLV
GMGFQEMDGP HADADFWIND CLFMPQDHPA RTHWDRFALD VPPIQELPDQ LVDRVESAHR
EGVGEDGDGY HSPWDRDFAE AVALRGHTTS LSMRYLSGFA GADIEPPKRY FSVEKVYRND
TLDPTHLLEF FQIEGWVLAE DLSVRDLMGT FEEFYAQFGI TDLEFKPHYN PYTEPSFELF
GEHPTTGEIV EIGNSGLFRP EVLEPLGIEA DVMAWGLALE RLLMLMYGFE DIRDVHGTLC
DLELLRETEV LQ
//