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SYFB_METB6
ID   SYFB_METB6              Reviewed;         542 AA.
AC   A7I615;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Mboo_0658;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS55176.1; -; Genomic_DNA.
DR   RefSeq; WP_012106198.1; NC_009712.1.
DR   AlphaFoldDB; A7I615; -.
DR   SMR; A7I615; -.
DR   STRING; 456442.Mboo_0658; -.
DR   EnsemblBacteria; ABS55176; ABS55176; Mboo_0658.
DR   GeneID; 5411310; -.
DR   KEGG; mbn:Mboo_0658; -.
DR   eggNOG; arCOG00412; Archaea.
DR   HOGENOM; CLU_020279_3_0_2; -.
DR   OMA; FPGRCAN; -.
DR   OrthoDB; 55024at2157; -.
DR   Proteomes; UP000002408; 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..542
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_1000022417"
FT   DOMAIN          266..342
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         320
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         326
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         329
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         330
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   542 AA;  59639 MW;  C3B0D9EEFDF36C2A CRC64;
     MAIISLSYKY LERLTGTDRE TILKRLPMIG SEVERLEEDH ADVEFFPNRP DLFSVEGAAR
     AMRGFLGIET GLPRYMVKPS GIRFTIDSKL AAIRPCLASA VIRNVSFDDE SILSVMALQE
     ALHWAVGRGR SKVAIGIHDL DTITPPFHYV ASPRVRKFVP LDFTDELTLD GILEKHPKGR
     DYAKIVKDFP LFPLIVDNED HVCSFPPIIN GERTRVTTAT KNILLDVTGT DQRAVNVAAN
     IICTALAEAG ATIESVEING APFPDLAPAV RTVSVRECSA LIGVDLTAPQ MAELLEKMRF
     GAEPAGPDQV RVQVPCYRAD IMHDWDLFED VAIAYGYENF AVEVPPTFSI GKEHPANRIA
     GQARAILAGL GYLEMMPFTL TNERVLCDRM QRPGEPATLR LMHPISEEYT VVRTDIVPLL
     LEMLQVNRHR ELPQRLFATG DVIADLLTTQ RLAFVSTHAG ADFSEAYAHA DAVLRELGVA
     YSAEVSDDAA FIEGRRADII VGGKKAGVFG EIHPAVLTAF ELEQPVAAFE LDLRAVPGYP
     SP
 
 
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