SYFB_GRATL
ID SYFB_GRATL Reviewed; 697 AA.
AC Q6B8Z8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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}; Synonyms=syfB;
GN OrderedLocusNames=Grc000056;
OS Gracilaria tenuistipitata var. liui (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX NCBI_TaxID=285951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT "Comparative analysis of the complete plastid genome sequence of the red
RT alga Gracilaria tenuistipitata var. liui provides insights into the
RT evolution of rhodoplasts and their relationship to other plastids.";
RL J. Mol. Evol. 59:464-477(2004).
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; AY673996; AAT79637.1; -; Genomic_DNA.
DR RefSeq; YP_063562.1; NC_006137.1.
DR AlphaFoldDB; Q6B8Z8; -.
DR SMR; Q6B8Z8; -.
DR GeneID; 2944047; -.
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 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; 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 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..697
FT /note="Phenylalanine--tRNA ligase beta subunit,
FT chloroplastic"
FT /id="PRO_0000232833"
FT DOMAIN 283..368
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 609..697
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 346
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 352
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 355
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 356
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 697 AA; 81429 MW; 9376571FEE702F6C CRC64;
MKFSLRWLQQ IVDLNNIKFS TLVDKLSVSG FEVEDISRNS SNDDMIFDVT TTANRQDILC
TVGLAREISS IFNRDLKYKL YKDSIAISTH CLNILNSVSL LDLSIVNVNY FYNNRSPLWL
QYYLSSYNIK SLNLLTDIPQ YIYLKWGQSI EIFDKNKISS VPIQYSLFNL QKKSHIIYDS
PNIELEVLRY DDVILFPIGF SLNENIKCDA ATNSIVIMGY VCDKQYITDI KKKLKLSTYL
SQRCCNQGSR SDFLNAFYES VYLLGSFGFA TLGKFYGYHK LYNISRILFI DKVKIQNILG
SVKIGSYNYL TVKEIFTLLE RLNFLPIYDS LKSSFKIHIP VYRQDDIVRP IDVIEEVARI
YGFDNFISKL PLNPIDNKNI FLNNIFANKV YRIRYLLRCL GLHEAQNYSF YDYYPFNHDT
QIKIYNPLAQ DQSFLRSSLA VHLTLNQQDN LRQGNKDIEV FEIGKVFRLY SSSLEYDNTL
NSFEFLHLSG LIANSIFLRP SWSDKEQSLS WFHAKGMVEE FLDRLEVPVV WKKISDLDQS
NLFFNLMHLL NMNWTAIICN RFHEEIGIFG KLCNKSDFNS TYVFEFDLVK LIASIESLNH
INSIINPYSS YPSLTRDISL TVKNSCTISF IKARILSYEN NLIESIEVFN YYKDKSINAF
YNVGLRIVYR AHNRTLNYSD INRIDQEIDD LLNEYKL
