ID A0A151BK03_9ARCH Unreviewed; 503 AA.
AC A0A151BK03;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00282};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00282};
GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00282};
GN ORFNames=AYL32_012970 {ECO:0000313|EMBL:KYH40180.1};
OS Candidatus Bathyarchaeota archaeon B26-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779371 {ECO:0000313|EMBL:KYH40180.1, ECO:0000313|Proteomes:UP000075437};
RN [1] {ECO:0000313|EMBL:KYH40180.1, ECO:0000313|Proteomes:UP000075437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B26-2 {ECO:0000313|EMBL:KYH40180.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00282};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00282};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00282}.
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, ECO:0000256|HAMAP-Rule:MF_00282}.
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:KYH40180.1}.
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DR EMBL; LUCE01000042; KYH40180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BK03; -.
DR STRING; 1779371.AYL32_012970; -.
DR PATRIC; fig|1779371.3.peg.853; -.
DR Proteomes; UP000075437; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 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; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00282,
KW ECO:0000313|EMBL:KYH40180.1};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00282};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00282};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00282};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00282}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00282}.
FT DOMAIN 250..479
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 346
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 386..388
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 427
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 452
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
SQ SEQUENCE 503 AA; 57156 MW; ADE78F9E6DBFB674 CRC64;
MSELREHERK TLLTLRSLGG RASVDEVAEK GNLAHAAVMR AALVLEESGL IKVSEERRTR
VRLNDEGRLY AEEGLPERRL VQALKEMGGE APIGSAGEAA GLSRELLAIA LGWISRKGWA
AVDRKERVLR MPIEPPTGAD ERLLALLKRE GTLTVEELDE ELQNAFKLLK GRKILHVEEE
TVRELELTDE GWRLVEKGIE AVEEVSQLTP VLIATGRWRE VRLRRYNIKA PVAKVWPGKK
HPYLRFLDEL RERLVALGFK EMTGPIVELS FFNCDALYMP QNHPAREVHD MYFIKEPVYG
SLKPYEEVLK NVKETHEDGW RTGSKGWGYR FSTLEASRLM LRSQTTALSA RTLLSRDLEI
PGKYFAIARC YRPDVVDRTH LTEFNQVEGI VLGEELTLRD LLGILERFAV EIAEADKVRF
RPGYFPFTEP SVELHAYKEG CGWLEFGGAG IFRPEVTLPL GVDVPVLAWG LGVDRIFMMK
AGIDDIRYLF TQDLEWLRAK GVV
//
