SYFB_SYNE7
ID SYFB_SYNE7 Reviewed; 810 AA.
AC P74764; Q31NP6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=pheT; OrderedLocusNames=Synpcc7942_1293;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cranenburgh R.M., Robinson N.J.;
RT "Phenylalanyl-tRNA synthetase gene, pheT, from Synechococcus PCC 7942.";
RL J. Appl. Phycol. 8:81-82(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
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DR EMBL; X94345; CAA64071.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57323.1; -; Genomic_DNA.
DR RefSeq; WP_011377966.1; NC_007604.1.
DR AlphaFoldDB; P74764; -.
DR SMR; P74764; -.
DR STRING; 1140.Synpcc7942_1293; -.
DR PRIDE; P74764; -.
DR EnsemblBacteria; ABB57323; ABB57323; Synpcc7942_1293.
DR KEGG; syf:Synpcc7942_1293; -.
DR eggNOG; COG0072; Bacteria.
DR HOGENOM; CLU_016891_0_0_3; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1293-MON; -.
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:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00769; PheRS_beta_core; 1.
DR CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 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; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR033714; tRNA_bind_bactPheRS.
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; PF03147; FDX-ACB; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00472; pheT_bact; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..810
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126972"
FT DOMAIN 39..151
FT /note="tRNA-binding"
FT DOMAIN 408..494
FT /note="B5"
FT DOMAIN 716..809
FT /note="FDX-ACB"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT CONFLICT 196..215
FT /note="ELQTYPELPCLAISLQSEAC -> GTADLSRTTLSWRSLYKVKPG (in
FT Ref. 1; CAA64071)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> P (in Ref. 1; CAA64071)"
FT /evidence="ECO:0000305"
FT CONFLICT 600..602
FT /note="Missing (in Ref. 1; CAA64071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 89932 MW; 8F350615544513CA CRC64;
MRISLNWLRE LVQVDLEPEV LAEKLTLAGF EVEEIEDRRT WAAGVVVGRV LEREQHPNAD
RLSVCQVEIG QAEPVTIVCG ASNVRADIWV AVATLGSYLP CIDLKLKPTK LRGVRSEGMI
CSLSELGLTK ESEGIHIFPE DAGLQAGQPV GPLLGLDDVV LDLTSTANRA DALSLIGIAR
EVRALTAATL TLPEVELQTY PELPCLAISL QSEACSHYSG TIIEGVTIAP SPEWLQKRLQ
LAGIRTINNV VDITNYILLE YGQPLHAFDR QKLQAIAGSS DLAIGVRSAQ AGETLKTLDD
QERTLAEAAL VITAGDCPVA LAGVMGGADS EVSQETTQLL LEAAWFEPIA VRRSARSQGL
RTEASARYER GVNVTELPIA TQRAIDLLLQ IAGGTVISQT VATTTQTEPE HSITLRLQRI
NELLGPVQAE DEELKDLGAD DIERLLTAIG CHLTLVDDAV WQVRVPPYRY RDLEREIDLI
EEVARLYGYD NFGETLPPLG SDEGALSIDE SLRRQIRAVC RGVGLTELQH YSLVKPGSDR
QVHLANPLLA EYSALRLDLL SGLIDAFQYN WEQGNGPLWG FEIGRIFWRE EDGFFEADRM
GGILGGDPSR GRWQRGGKEQ AIDWYAAKGV LEEIFERFGL TIEFQPDRQD DRFHPGRTAS
LWLQGDRLGR FGQLHPSLCE GRGLPAEVYA FELDLDVWLD HLDQPERQVP RFQPYSSFPA
SDRDLAFFVD QSVTVAELER IIRRQGGALL SEVELFDQYC GEHVPENQRS LAFRLTYRAS
DRTLTEAEVE PVHDQVRQSL VERFRVTLRS
