ID M0NR18_9EURY Unreviewed; 502 AA.
AC M0NR18;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ECO:0000313|EMBL:EMA60216.1};
GN ORFNames=C469_09130 {ECO:0000313|EMBL:EMA60216.1};
OS Halorubrum lipolyticum DSM 21995.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227482 {ECO:0000313|EMBL:EMA60216.1, ECO:0000313|Proteomes:UP000011650};
RN [1] {ECO:0000313|EMBL:EMA60216.1, ECO:0000313|Proteomes:UP000011650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21995 {ECO:0000313|EMBL:EMA60216.1,
RC ECO:0000313|Proteomes:UP000011650};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA60216.1}.
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DR EMBL; AOJG01000025; EMA60216.1; -; Genomic_DNA.
DR RefSeq; WP_008005853.1; NZ_AOJG01000025.1.
DR AlphaFoldDB; M0NR18; -.
DR STRING; 1227482.C469_09130; -.
DR PATRIC; fig|1227482.3.peg.1840; -.
DR OrthoDB; 372178at2157; -.
DR Proteomes; UP000011650; 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; 1.10.10.2320; -; 1.
DR Gene3D; 1.10.10.2330; -; 1.
DR Gene3D; 3.30.1370.240; -; 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 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:0000256|HAMAP-Rule:MF_00282};
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, ECO:0000313|EMBL:EMA60216.1};
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 245..490
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 339
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 382..384
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 422
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 424
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 448
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
SQ SEQUENCE 502 AA; 55093 MW; F077D56325058D16 CRC64;
MRLPERQLAV LEAASATDER TIDEIAAETG LKPETVTGAA FDLRDEGLCS VGETAAETLA
VTDEGRRYVD DGLPETRLYR AGVALGADES AVSMGRVIGE ADLDGPEVDI ALSNFARKGF
GSIDSGELTV DPDADPDADS EAAALSALAA GEDPAVDDSV LGQLDSRGLV ERGESVTRSV
TLTDDGVDAL MTGVEAAETV AQVTPELLAS GEWRDVEFSE YNVEADAPAV SGGRKHVLRR
TADRVKDVLV GMGFQEMEGP HADSDFWIND CLFMPQDHPA RTHWDRFALD VDPMEDIPEE
LIRRVESAHR DGWGEDGDGY HSPWSEEFAR EIALRGHTTS LSMRYLSGIA GAELEPPQRY
FSVEKVYRND TLDPTHLLEF FQIEGWVMAE DLSVRDLMGT FEEFYRQFGI TDIRFKPHYN
PYTEPSFELF GEHPETGEEI EIGNSGVFRE EVTGPLGVDC DVMAWGLALE RLAMLTTGAE
DIRDLHGTLA DIEFLRDAEV SY
//
