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SYFB_METMJ
ID   SYFB_METMJ              Reviewed;         546 AA.
AC   A3CT77;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Memar_0644;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN56577.1; -; Genomic_DNA.
DR   RefSeq; WP_011843488.1; NC_009051.1.
DR   AlphaFoldDB; A3CT77; -.
DR   SMR; A3CT77; -.
DR   STRING; 368407.Memar_0644; -.
DR   EnsemblBacteria; ABN56577; ABN56577; Memar_0644.
DR   GeneID; 4847631; -.
DR   KEGG; mem:Memar_0644; -.
DR   eggNOG; arCOG00412; Archaea.
DR   HOGENOM; CLU_020279_3_0_2; -.
DR   OMA; FPGRCAN; -.
DR   OrthoDB; 55024at2157; -.
DR   Proteomes; UP000002146; 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   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.
FT   CHAIN           1..546
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_1000022424"
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   546 AA;  59768 MW;  28CAF115BCB4840F CRC64;
     MAIITLPYRY LERLAGTDRQ TIIDRVPMIG ADIERIEDDH VDVEFFPNRP DLYSPEGVAR
     AMRGFLGIEE GLPAYTVRPS GIAFSVDPGL ADIRPFLGSA VIRNVNLDEE AIESLMALQE
     ALHWAVGRGR GKVAIGVHDL DTVTPPFRYI ASPRNRSFVP LDFEREMTME EMLADHPKGR
     DYAHLVENFD TFPLIVDAEN RVLSFPPIIN GELTRVTAAT KNILLDCTGT DRRAVMTAVN
     IICTALIEAG ATVETVTVEG EEMPTLAPAE RVVSVAECSR LLGLSLTPQE MAGLLRRMRF
     DAEPDGDSRV RILVPCYRSD ILHDWDIFED VAIAYGIENF DAALPATSTV AQEHPIPAVA
     GAVRSVMTGL GYLEAIPFTL TNERVLYANM QREPAPGTLR LLHPISEEQT VVRTDLLPLL
     MEMLLANKHR ELPQRLFAVG DVVEDCVTYL KVAAVSIHPA ADFSEAYAAA DVLCRELSLS
     YTVVESADPA FLDGRRGDIV VDGKIVGVFG EIHPAVLGAF DLEHPVAALA LDLTAVPGYP
     ALPDTP
 
 
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