SYFB_NEOYE
ID SYFB_NEOYE Reviewed; 719 AA.
AC Q1XDE1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) 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 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; AP006715; BAE92470.1; -; Genomic_DNA.
DR RefSeq; YP_537027.1; NC_007932.1.
DR AlphaFoldDB; Q1XDE1; -.
DR SMR; Q1XDE1; -.
DR PRIDE; Q1XDE1; -.
DR GeneID; 3978775; -.
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.
FT CHAIN 1..719
FT /note="Phenylalanine--tRNA ligase beta subunit,
FT chloroplastic"
FT /id="PRO_0000277247"
FT DOMAIN 318..403
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 625..718
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 381
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 387
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 390
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 391
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 719 AA; 83201 MW; 9F6793EBBAD81370 CRC64;
MNFLNYFYHS KKILLQKIDG QFMKVSLNWL KALGNIKTID IDNKYSTNTA GFEVEAIESI
IIGGEIDHIL DISSTANRSD VLSMIGLSRE VSALTGSSMF QLYINPIIDI FSKKETIISN
HDLLNCDNYF AAIIDEIRVK DSPDWLKNRL LSSGFTHRNL LTDISNYIML KWGQPINIID
LNKINNMNHK NSLTIRSNFP LGSNDQIKLN NENIELNKNI LVTQVNTNVT SIAGIGSNSD
FDTDYNTKSI LVESAIFKQS VVRKSSRVLN IRTESSIRQE RGLNVDNWKN AHFEALALIT
DLTCGNIRDT FCREKITDHA LNINLSIKKV HDILGPIMYN GQTRFLFFEE IQNILHSLNF
DLIYQNKENI EVTVPNYRRE DVFREIDVIE EIARIYGYHK FRSSVPNIQF NKRLSTKRKF
IDKSRSILRN LGLTELVHYS LIKSKGNIAL NNPLIQDYSN LRGSLLEGLI ESNLYNIKQS
NQTIDSFEIG TVFHNDQNKI VETTNLAIIL GGNLDIRSTW SHPAHSLNWY EAKGIVENFF
QRLNRQIEWT KKDILDGRIK FIQKGKFATL IYNNIIIGIF SELNQATYSE LGLNTKLFFL
EVNLNILEDC HNEFNYLSYQ IQPYSKYPSI IRDLSLIIPK NMEIKYLLKL LDQFYDKDLE
STTLFDQYID ESIGKEKKSI GLRFTYRSNE KTLTNSEIDY KQHQLQKKIV KQLNLKIRQ