EF3B_YEAST
ID EF3B_YEAST Reviewed; 1044 AA.
AC P53978; D6W1G4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Elongation factor 3B;
DE Short=EF-3B;
DE EC=3.6.4.- {ECO:0000269|PubMed:9544245};
DE AltName: Full=Homolog of EF-3;
DE AltName: Full=Translation elongation factor 3B;
GN Name=HEF3 {ECO:0000303|PubMed:33260587}; Synonyms=YEF3B, ZRG7;
GN OrderedLocusNames=YNL014W {ECO:0000312|SGD:S000004959}; ORFNames=N2846;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
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 [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX PubMed=9544245;
RX DOI=10.1002/(sici)1097-0061(199802)14:3<239::aid-yea219>3.0.co;2-b;
RA Sarthy A.V., McGonigal T., Capobianco J.O., Schmidt M., Green S.R.,
RA Moehle C.M., Goldman R.C.;
RT "Identification and kinetic analysis of a functional homolog of elongation
RT factor 3, YEF3 in Saccharomyces cerevisiae.";
RL Yeast 14:239-253(1998).
RN [4]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=9778796;
RX DOI=10.1002/(sici)1097-0061(19980915)14:12<1105::aid-yea313>3.0.co;2-y;
RA Maurice T.C., Mazzuci C.E., Ramanathan C.S., Rayn B.M., Warr G.A.,
RA Puziss J.W.;
RT "A highly conserved intraspecies homolog of the Saccharomyces cerevisiae
RT elongation factor-3 encoded by the HEF3 gene.";
RL Yeast 14:1105-1113(1998).
RN [5]
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 [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33260587; DOI=10.3390/genes11121432;
RA Goscinska K., Shahmoradi Ghahe S., Domogala S., Topf U.;
RT "Eukaryotic Elongation Factor 3 Protects Saccharomyces cerevisiae Yeast
RT from Oxidative Stress.";
RL Genes (Basel) 11:E1432-E1432(2020).
CC -!- FUNCTION: Ribosome-dependent ATPase that promotes the translation of
CC proteins required for detoxification of reactive oxygen species
CC (PubMed:33260587). Required for the ATP-dependent release of deacylated
CC tRNA from the ribosomal E-site during protein biosynthesis (By
CC similarity). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA
CC to the ribosomal A-site, which has reduced affinity for tRNA as long as
CC the E-site is occupied (By similarity). {ECO:0000250|UniProtKB:P16521,
CC ECO:0000269|PubMed:33260587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:9544245};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.102 mM for ATP {ECO:0000269|PubMed:9544245};
CC Vmax=5.7 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:9544245};
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P16521}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16521}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetatively growing cells at very
CC low levels. {ECO:0000269|PubMed:9544245, ECO:0000269|PubMed:9778796}.
CC -!- INDUCTION: Increases in mild (0.5 mM) hydrogen peroxide stress, and
CC decreases in stronger (1 mM) hydrogen peroxide stress.
CC {ECO:0000269|PubMed:33260587}.
CC -!- DISRUPTION PHENOTYPE: Decreases translation of proteins required for
CC detoxification of reactive oxygen species (PubMed:33260587). Sensitive
CC to hydrogen peroxide (PubMed:33260587). Increases GRX1 mRNA level
CC during vegetative growth (PubMed:33260587). Normal vegetative cell
CC population growth on glucose, galactose, and glycerol carbon sources,
CC at high temperature, and at standard temperature (PubMed:9778796,
CC PubMed:33260587). Normal mating and sporulation (PubMed:9778796).
CC {ECO:0000269|PubMed:33260587, ECO:0000269|PubMed:9778796}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; Z71290; CAA95874.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10530.1; -; Genomic_DNA.
DR PIR; S62926; S62926.
DR RefSeq; NP_014384.3; NM_001182853.3.
DR AlphaFoldDB; P53978; -.
DR SMR; P53978; -.
DR BioGRID; 35812; 71.
DR DIP; DIP-6529N; -.
DR IntAct; P53978; 17.
DR MINT; P53978; -.
DR STRING; 4932.YNL014W; -.
DR iPTMnet; P53978; -.
DR MaxQB; P53978; -.
DR PaxDb; P53978; -.
DR PRIDE; P53978; -.
DR EnsemblFungi; YNL014W_mRNA; YNL014W; YNL014W.
DR GeneID; 855718; -.
DR KEGG; sce:YNL014W; -.
DR SGD; S000004959; HEF3.
DR VEuPathDB; FungiDB:YNL014W; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR GeneTree; ENSGT00940000176346; -.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; P53978; -.
DR OMA; KVLLHNT; -.
DR BioCyc; YEAST:G3O-33053-MON; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:P53978; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53978; protein.
DR GO; GO:0022626; C:cytosolic ribosome; IPI:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IMP:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IMP:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IGI:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR040533; 4HB.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015688; Elongation_fac_3.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF5; PTHR19211:SF5; 1.
DR Pfam; PF17947; 4HB; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Elongation factor; Hydrolase;
KW Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT CHAIN 2..1044
FT /note="Elongation factor 3B"
FT /id="PRO_0000093459"
FT REPEAT 5..42
FT /note="HEAT 1"
FT REPEAT 86..123
FT /note="HEAT 2"
FT REPEAT 124..162
FT /note="HEAT 3"
FT REPEAT 166..203
FT /note="HEAT 4"
FT REPEAT 205..241
FT /note="HEAT 5"
FT REPEAT 242..279
FT /note="HEAT 6"
FT REPEAT 285..323
FT /note="HEAT 7"
FT DOMAIN 426..641
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 667..993
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 975..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 463..470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 701..708
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 187
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 196
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 789
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 972
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16521"
SQ SEQUENCE 1044 AA; 115869 MW; 7E040EE826D550F1 CRC64;
MSDSQQSITV LEELFRKLET ATSETREGIS SELSSFLNGN IIEHDVPEVF FDEFQKAIQS
KQKALNTLGA VAYIANETNL SPSVEPYIVA TVPSVCSKAG SKDNDVQLAA TKALKAIASA
VNPVAVKALL PHLIHSLETS NKWKEKVAVL EVISVLVDAA KEQIALRMPE LIPVLSESMW
DTKKGVKEAA TTTITKATET VDNKDIERFI PKLIECIANP NEVPETVHLL GATTFVAEVT
PATLSIMVPL LSRGLAERET SIKRKAAVII DNMCKLVEDP QVVAPFLGKL LPGLKNNFAT
IADPEAREVT LKALKTLRRV GNVGEDDVLP EISHAGDVST TLGVIKELLE PEKVAPRFTI
VVEYIAAIAA NLIDERIIDQ QTWFTHVTPY MTIFLHEKTA KEILDDFRKR AVDNIPVGPN
FQDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRGRRYG LCGPNGAGKS TLMRSIANGQ
VDGFPTQDEC RTVYVEHDID NTHSDMSVLD FVYSGNVGTK DVITSKLKEF GFSDEMIEMP
IASLSGGWKM KLALARAVLK DADILLLDEP TNHLDTVNVE WLVNYLNTCG ITSVIVSHDS
GFLDKVCQYI IHYEGLKLRK YKGNLSEFVQ KCPTAQSYYE LGASDLEFQF PTPGYLEGVK
TKQKAIVKVS NMTFQYPGTT KPQVSDVTFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP
TSGEVYTHEN CRIAYIKQHA FAHIESHLDK TPSEYIQWRF QTGEDRETMD RANRQINEND
AEAMNKIFKI EGTPRRVAGI HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWL
PRGELIESHS KMVAEIDMKE ALASGQFRAL TRKEIELHCA MLGLDSELVS HSRIRGLSGG
QKVKLVLAAC TWQRPHLIVL DEPTNYLDRD SLGALSKALK AFEGGVIIIT HSAEFTKNLT
DEVWAVKDGK MTPSGHNWVA GQGAGPRIEK KEEEGDKFDA MGNKINSGKK KSKLSSAELR
KKKKERMKKK KEMGDEYVSS DEDF
