SYFB_THEKO
ID SYFB_THEKO Reviewed; 574 AA.
AC Q76KA7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00284};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00284};
DE AltName: Full=Tk-PheRSB;
GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=TK0925;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=14607984; DOI=10.1093/jb/mvg175;
RA Shiraki K., Tsuji M., Hashimoto Y., Fujimoto K., Fujiwara S., Takagi M.,
RA Imanaka T.;
RT "Genetic, enzymatic, and structural analyses of phenylalanyl-tRNA
RT synthetase from Thermococcus kodakaraensis KOD1.";
RL J. Biochem. 134:567-574(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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_00284};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00284};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00284}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00284,
CC ECO:0000305}.
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DR EMBL; AB093556; BAC99021.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85114.1; -; Genomic_DNA.
DR RefSeq; WP_011249876.1; NC_006624.1.
DR AlphaFoldDB; Q76KA7; -.
DR SMR; Q76KA7; -.
DR STRING; 69014.TK0925; -.
DR EnsemblBacteria; BAD85114; BAD85114; TK0925.
DR GeneID; 3235404; -.
DR KEGG; tko:TK0925; -.
DR PATRIC; fig|69014.16.peg.903; -.
DR eggNOG; arCOG00412; Archaea.
DR HOGENOM; CLU_020279_3_0_2; -.
DR InParanoid; Q76KA7; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 55024at2157; -.
DR PhylomeDB; Q76KA7; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR HAMAP; MF_00284; Phe_tRNA_synth_beta2; 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; IPR022918; Phe_tRNA_ligase_beta2_arc.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..574
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127010"
FT DOMAIN 278..353
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
SQ SEQUENCE 574 AA; 66211 MW; 7E36AC73A2C09452 CRC64;
MPKFDVSKRD LERLVGKTFS VEEWEDLFLY AKCELDDVWE ENGEIYFKAD SKDTNRPDLW
SAEGIARQIR FALGFQKGLP KYEIEKSDVV VYVDEKLKDI RPYGVYAIVE GLNIDEEALR
QMINLQEKVA LTFGRRRREV AIGIFDFDKV KPPIYYRAAE KTEKFVPLGY DEEMTLEEIL
EKHEKGREYG HLIKDKPYYP LLVDSEGKVL SMPPVINSET TGRVTTETKN VFVDITGWDL
NKVMLALNVV VTALAERGGK IKSVKVVYPD FEIETPDLTP KEFEVELDYI RKLAGLELSD
GEIKELLERM MYEVELENRR AKLRYPAFRD DIMHARDVLE DVLIAYGYNE IEPEEPKLAV
QGRGDKFIEF EDAVRELMVG FGLQEVMTFN LTNREAQYDR MNLPCGEHQE ECRDYFNHPP
AELVEIENPI SPKWSALRNW LIPSLLDFLS QNTHEEYPQK LFEVGKATLI DESRETKTVS
ESKLAVALAH PRVTFTEAKE ILEGVMRHLG FEYELEEAEH PSFIPGRVGK IIVNGETIGV
IGEIHPAVLE NWGIEMPVAA FELFLAPLYT EPYL
