SYFB_PHATC
ID SYFB_PHATC Reviewed; 706 AA.
AC A0T0H4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00283};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
RX PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA Green B.R.;
RT "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT lineage.";
RL Mol. Genet. Genomics 277:427-439(2007).
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_00283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00283};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00283}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}.
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DR EMBL; EF067920; ABK20672.1; -; Genomic_DNA.
DR RefSeq; YP_874449.1; NC_008588.1.
DR AlphaFoldDB; A0T0H4; -.
DR SMR; A0T0H4; -.
DR STRING; 556484.A0T0H4; -.
DR GeneID; 4524550; -.
DR InParanoid; A0T0H4; -.
DR Proteomes; UP000000759; Chloroplast.
DR GO; GO:0009507; C:chloroplast; 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: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; 3.30.70.380; -; 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; 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; 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; 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; 2.
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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..706
FT /note="Phenylalanine--tRNA ligase beta subunit,
FT chloroplastic"
FT /id="PRO_0000277248"
FT DOMAIN 300..388
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 612..705
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 372
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
SQ SEQUENCE 706 AA; 81082 MW; C73614BC814A04C7 CRC64;
MQISLKWIKE LIDIENVDLD DLIEKLTLGG FEVEEILELE INNEKQIALE ISSTANRSDS
LSIQGISVEI ASLFNKQPKV CKYFNSSLNW QQKIKNLTTI RTSKTECLMF TAVILEGLED
LTVPKWIQNK LVSSGIMPLN NLVDFQNYIL LETGYPFAFY DLDKVYSKVR TPTFSLSIEK
AENGSEFFAS NQINYKLDNS IFLVQANNIP ISIAGIIEND EIICHSKTSS LLIEGSIFSA
SKIRQQSRKL AIRTDRSARY EKSLKSTYLI EALYRLISLL RISNPSLVYK FHSSNKVLEK
VLKPIVLNYK TIVEILGPIK KRTNEHLIYI SPETVTDYLK RLNFKFLFDS STLNWEVTIP
SIRSDDITRE IDLIEEVGRL HGFNNFLTML PQIKSVGRAD FSYQTRKKIT SYLLNMGLTE
LIHYSLVSNE TFLKNEIKLV NPLLSDCSTL RVSLLPSLLM TIQENLKQGN SILEGFEYGH
VFSGNIETTL TEIEYVGGIF GGTKIKSSWF EKGQSLKWFE AKGKIEKLFQ QLNLGIHWRI
NSQTYTKKFL HPYRSAEIFL SSGKNIGVFG QLHPLLANKL GLSSEIYLFE LNLELIQQSL
QQNKLTIYSQ YSVYPKIVKD LSFIIKKNIK FDELEKIIYA NGTEFLSQIN LLDDYKGEFI
PEKHTSLCLQ LTFQSNKKTL ENKEIDRIVK NLKRVLELKV QAILRE
