SYFB_METAR
ID SYFB_METAR Reviewed; 553 AA.
AC Q0W0X4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=UNCMA_02960;
GN ORFNames=RRC225;
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
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 -!- 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}.
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DR EMBL; AM114193; CAJ37969.1; -; Genomic_DNA.
DR RefSeq; WP_012034625.1; NC_009464.1.
DR AlphaFoldDB; Q0W0X4; -.
DR SMR; Q0W0X4; -.
DR STRING; 351160.RRC225; -.
DR EnsemblBacteria; CAJ37969; CAJ37969; RRC225.
DR GeneID; 5143727; -.
DR KEGG; rci:RRC225; -.
DR PATRIC; fig|351160.9.peg.312; -.
DR eggNOG; arCOG00412; Archaea.
DR OMA; FPGRCAN; -.
DR OrthoDB; 55024at2157; -.
DR Proteomes; UP000000663; 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: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; IEA:UniProtKB-UniRule.
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 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..553
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_1000022431"
FT DOMAIN 273..349
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 327
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 333
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 336
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"
SQ SEQUENCE 553 AA; 61711 MW; D82D2B240D8830FE CRC64;
MATVTLNYPD LVKLIGIDLS LDKVREVMFE LGSETEDIQG DEVTFEVTSD RADLLSEEGI
ARMLRAYYSI ETGFRIPKLQ PSGYKLIVNR EVEPVRPYVT GAIVRNVQFT DESIKSLMHL
QEKLHGTFGR KRKKGAVGVH DLSKIKGREI HYRAVPGDSV KFVPLQSDEL MTLSDVLARH
PKGIDYRYVL EGKNLMPIIT DDEGIFSFPP IINSKRTEVT LNTHDLLIEL TGEDLRTIDY
MLNIVLYSLD LRGASIYSID VVYPDETLHR PDFNVRNIDI EVDYVNRVLG LELTAPDIKA
LLERMGFKVA ETGSDYLIVE VPPYRADILH KRDVVDDVGR AFGYNNITPS YPNTPSVGKL
TEATKLGDAI RNTMIGLGCQ DTFNFILIGK DEVFGKMNLP DDGTAVEISN PYAEQYNIVR
TSLIPSLMIV LSNNLHRDYP QNIFEVGTVA HLDSAENTGV KEIDHVACTL CYAKAGFNEI
KVKLQSLCAN FGKLDELKTV AAEHPSFIPG RCAEVRIGDK KVGIIGELSP VVLKSWGIEM
PVAAFEMEIA ALK
