SYFA_SULTO
ID SYFA_SULTO Reviewed; 469 AA.
AC Q971D7; F9VP54;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00282};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00282};
GN Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=STK_14160;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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:0000255|HAMAP-Rule:MF_00282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00282};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00282}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00282}.
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DR EMBL; BA000023; BAK54562.1; -; Genomic_DNA.
DR RefSeq; WP_010979461.1; NC_003106.2.
DR AlphaFoldDB; Q971D7; -.
DR SMR; Q971D7; -.
DR STRING; 273063.STK_14160; -.
DR PRIDE; Q971D7; -.
DR EnsemblBacteria; BAK54562; BAK54562; STK_14160.
DR GeneID; 1459445; -.
DR KEGG; sto:STK_14160; -.
DR PATRIC; fig|273063.9.peg.1616; -.
DR eggNOG; arCOG00410; Archaea.
DR OMA; QIEGWVM; -.
DR OrthoDB; 22747at2157; -.
DR Proteomes; UP000001015; Chromosome.
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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.930.10; -; 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; IPR002831; Tscrpt_reg_TrmB_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01978; TrmB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..469
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126821"
FT BINDING 309
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 348..350
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 388
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ SEQUENCE 469 AA; 54397 MW; 8E105310F903654C CRC64;
MLSENEIKIL EYLSKKREAS AEDISKQLNI PIESVFSISQ LLKEKGYIEV EEKKVIKYEL
TDEGKRRLKE GFPEEKLVKL LDGKEKKIHE LKDKLGRDFE ISIGWAKRKG LVKIDGDTVI
PLVKDYEAKE EKEALINPEK ANKDILQQLL NRKLLIKKEE KILNIRLIRE PLEIKPALIF
LTPELLASGE WKKYALREYN VEAYPPFYPI GKKHFFKEFL ERLRDLMRDL GFKEVYSDYV
EIEFYNFDLL FQAQDHPARE IHDSFAISGK GKLTDEKLIQ RVKQIHERGW KYNWDVNISM
RLMLRSQTTA TTARVLASRP KPPIRVFTIG KVFRPDSIDA THLIEFHQLD GLVIEDNFTF
RDLLGTLKEI FNGIGIKEIR FKPAYFPFTE PSVEVYGKIE GLGWVEMAGA GLLRPEILEA
VEISSSAGAW GLGIDRLAML LLGLKDIRLL YATDIEYLRN RKVEINADN
