SYFB_METPE
ID SYFB_METPE Reviewed; 546 AA.
AC B8GEX4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Mpal_0569;
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:0-0(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; CP001338; ACL15941.1; -; Genomic_DNA.
DR RefSeq; WP_012617260.1; NC_011832.1.
DR AlphaFoldDB; B8GEX4; -.
DR SMR; B8GEX4; -.
DR STRING; 521011.Mpal_0569; -.
DR EnsemblBacteria; ACL15941; ACL15941; Mpal_0569.
DR GeneID; 7270153; -.
DR KEGG; mpl:Mpal_0569; -.
DR eggNOG; arCOG00412; Archaea.
DR HOGENOM; CLU_020279_3_0_2; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 55024at2157; -.
DR Proteomes; UP000002457; 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;
KW Reference proteome.
FT CHAIN 1..546
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_1000199337"
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; 60321 MW; 816B3C4567574726 CRC64;
MTIITLPYTY LTTLIGTDKE TILDRLPMIG SDIERIEDDH ADVEFFPDRP DLFSTEGVAR
AMRGFLGIET GSVTYEVKPS GVSFTIDPAL KEIRPFLGSA VIRGLSLSEE AIQSLMGLQE
ALHWAIGRGR KKMAIGLHDL DKITPPFRYC AAEKSRSFVP LDFTEPMTME QMLDEHPKGR
AYAHLVREHP RYPLIVDAED RVCSFPPIIN GDLTRVTTET KNILLDTTGT DQRAVEVTVK
IVCAALVEAG GTVESVTIDG VESPDLSPSV RTVSVDEGNK LLGLSLTAPE MATLLEKMRF
KATPDGTDRI RVEVPCYRAD IMHDWDIFED VAVAYGYENF DATLPETSTI GEQSQVSVIG
GAVREILTGL GYHEVMPFTL TSETVTYDLM QRERSPTALH LLHPITEDQT IVRTDLLPLL
LELLQMNRYR ELPQRIFCTG DVVEGISTHQ KAAAVSCHGA ADFSEAYAAA DALCRDLNLP
YTTAESTDPA FIDGRRGDII VDGTTVGVFG EISPRVILGF ELDHPIAAVE LDLRAVRAHR
DQRDRS
