SYFB_YEAST
ID SYFB_YEAST Reviewed; 595 AA.
AC P15624; D6VY62; E9P8X0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
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; OrderedLocusNames=YLR060W; ORFNames=L2165;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3049607; DOI=10.1016/s0021-9258(19)37603-3;
RA Sanni A., Mirande M., Ebel J.-P., Boulanger Y., Waller J.-P., Fasiolo F.;
RT "Structure and expression of the genes encoding the alpha and beta subunits
RT of yeast phenylalanyl-tRNA synthetase.";
RL J. Biol. Chem. 263:15407-15415(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=338359; DOI=10.1016/0014-5793(77)81056-9;
RA Robbe-Saul S., Fasiolo F., Boulanger Y.;
RT "Phenylalanyl-tRNA synthetase from baker's yeast. Repeated sequences in the
RT two subunits.";
RL FEBS Lett. 84:57-62(1977).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 -!- INTERACTION:
CC P15624; P15625: FRS2; NbExp=2; IntAct=EBI-18684, EBI-18678;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 5440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally erroneously assigned as an alpha subunit.
CC {ECO:0000305|PubMed:3049607}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35151.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J03964; AAA35151.1; ALT_INIT; Genomic_DNA.
DR EMBL; X94607; CAA64307.1; -; Genomic_DNA.
DR EMBL; Z73232; CAA97591.1; -; Genomic_DNA.
DR EMBL; AY692778; AAT92797.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09378.1; -; Genomic_DNA.
DR PIR; S61634; YFBYBC.
DR RefSeq; NP_013161.1; NM_001181947.1.
DR AlphaFoldDB; P15624; -.
DR SMR; P15624; -.
DR BioGRID; 31335; 235.
DR ComplexPortal; CPX-1738; Phenylalanyl-tRNA synthetase complex.
DR DIP; DIP-6746N; -.
DR IntAct; P15624; 6.
DR MINT; P15624; -.
DR STRING; 4932.YLR060W; -.
DR CarbonylDB; P15624; -.
DR iPTMnet; P15624; -.
DR MaxQB; P15624; -.
DR PaxDb; P15624; -.
DR PRIDE; P15624; -.
DR EnsemblFungi; YLR060W_mRNA; YLR060W; YLR060W.
DR GeneID; 850749; -.
DR KEGG; sce:YLR060W; -.
DR SGD; S000004050; FRS1.
DR VEuPathDB; FungiDB:YLR060W; -.
DR eggNOG; KOG2472; Eukaryota.
DR GeneTree; ENSGT00530000063489; -.
DR HOGENOM; CLU_020279_2_0_1; -.
DR InParanoid; P15624; -.
DR OMA; FPGRCAN; -.
DR BioCyc; YEAST:G3O-32214-MON; -.
DR PRO; PR:P15624; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P15624; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:SGD.
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; IDA:SGD.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:338359"
FT CHAIN 2..595
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127023"
FT DOMAIN 292..370
FT /note="B5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT REGION 86..90
FT /note="3'-CCA residue in tRNA"
FT /evidence="ECO:0000255"
FT BINDING 348
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 354
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 BINDING 358
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 18
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="G -> D (in Ref. 1; AAA35151)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="F -> L (in Ref. 4; AAT92797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 67365 MW; 68DA23E49644F801 CRC64;
MPTVSVNKQQ LFDLLGKNYT SQEFDELCFE FGMEMDEDTT EEALKTGEEP ELKLDISANR
YDLLCIEGIS QSLNEYLERK ERPDYKLSKP TTKLIIDKST EQIRPFATAA VLRNIKLNEK
SYASFIALQD KLHANLCRNR SLVAMGTHDL DSIEGPFHYR ALPPKDIKFV PLNQTQEFTG
DKLIEFYKSP EQKNNIGRYV HIIEDSPVFP VIMDSKDRVC SLPPLINSEH SKISVNTRNI
LIDITATDKT KAEIVLNILT TMFSRYCDEP FTVEPVEIVS EHNGQSRLAP NFNDRIMDVS
IKYINSCLGL DQSADEIAHC LKKMSLHAVQ SKEDKDILHV DIPVTRPDIL HACDIMEDAA
VGYGFNNLPK GEKLSNANFI AKPLPINKVS DIFRVASSQA TWVEVLPLTL CSHDENFKFL
RQSDNGDLAV KLANPKTLEY QVVRTTLLPG ILKTVKENRK HSLPIKVFET GDVVFKDDKL
ERKAYNERHW AAIYVGKNSG FEIIQGLLGK IMQTFRTEWI ADYGAAASGR GYWIEEDDSV
KTYFPGRGAK VMFRSKEGAE PKQIGHLGVL HPEVMMNFDV PFAASFVEVN AEVFL
