SYFB_CANAX
ID SYFB_CANAX Reviewed; 592 AA.
AC O13432; O94062;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 95.
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=FRS1; ORFNames=Ca49C4.04c;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 26555;
RX PubMed=9561746; DOI=10.1111/j.1574-6968.1998.tb12946.x;
RA Marcilla A., Pallotti C., Gomez-Lobo M., Caballero P., Valentin E.,
RA Sentandreu R.;
RT "Cloning and characterization of the phenylalanyl-tRNA synthetase beta
RT subunit gene from Candida albicans.";
RL FEMS Microbiol. Lett. 161:179-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Murphy L., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) 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;
CC Evidence={ECO:0000250|UniProtKB:A5K464};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000305}.
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DR EMBL; Y12589; CAA73166.1; -; mRNA.
DR EMBL; AL033503; CAA22014.1; -; Genomic_DNA.
DR PIR; T18243; T18243.
DR AlphaFoldDB; O13432; -.
DR SMR; O13432; -.
DR VEuPathDB; FungiDB:CAWG_01526; -.
DR VEuPathDB; FungiDB:CR_01760C_A; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 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; IPR041616; PheRS_beta_core.
DR InterPro; IPR040659; PhetRS_B1.
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; PF18262; PhetRS_B1; 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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..592
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127021"
FT DOMAIN 291..369
FT /note="B5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT CONFLICT 9
FT /note="E -> G (in Ref. 1; CAA73166)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="T -> S (in Ref. 1; CAA73166)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="N -> D (in Ref. 1; CAA73166)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..380
FT /note="TKPQAESLVAA -> DQTLRSKVFSCC (in Ref. 1; CAA73166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 66821 MW; ECEFF5F703190A94 CRC64;
MPTIPVDKED LFKLLGRSYT TEEFDELCFQ FGIELDEDTT EDVKGTDERP QLKIEVPANR
YDMLCIEGIA QALNEFLGNT SAPNYKLSPS KPEISLTIKE STYPIRQYAA SAILRNVNLD
ERAYDSFIAL QDKLHANLCR NRTLVAIGTH DLDTLTPPFT YEALAPKDIV FKPLNQTKEI
NGEELMEFYE KDKNIGKFLH IIKDSPVYPV MLDANRTVAS LPPIINSDHS KITLNTKNVW
IDVTGTDRTK TEIVINQLVA MFSRYCKEPF EIEPVQIISE HNNETRVCPN ITPRTAKAEI
SYINSCVGLN YSGEEISKLL KKMSLDATPS TEERDILDVK IPITRSDILH QCDIMEDVAI
GYGYDNLKKT KPQAESLVAA PLPVNKVADI LRLASSQAGY LEVMPLTLSS HDENFAWLKQ
KDDGTKAVKL ENPKTIEYQV VRTTLLPGIL KTVKENRKHS LPIKVFECGD IVLKNPELER
GAFNQRNWAA LYVGKTSGFE MVQGLLGKIM QTMRTPWLEN PSKDQRRGYW IEEDKENTTF
FPGRGAKIYF RNADNAEAKA IGSIGVLHPE VMNNFDIPYA ASSVEINAEV FL
