EF3_ASHGO
ID EF3_ASHGO Reviewed; 1044 AA.
AC Q75EV6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Elongation factor 3;
DE Short=EF-3;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P16521};
GN Name=TEF3; OrderedLocusNames=AAL028W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 400; 422; 424; 427 AND 454.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic
CC translation elongation (By similarity). Required for the ATP-dependent
CC release of deacylated tRNA from the ribosomal E-site during protein
CC biosynthesis (By similarity). Stimulates the eEF1A-dependent binding of
CC aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for
CC tRNA as long as the E-site is occupied (By similarity).
CC {ECO:0000250|UniProtKB:P16521}.
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:0000250|UniProtKB:P16521};
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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; AE016814; AAS50338.2; -; Genomic_DNA.
DR RefSeq; NP_982514.2; NM_207867.2.
DR AlphaFoldDB; Q75EV6; -.
DR SMR; Q75EV6; -.
DR STRING; 33169.AAS50338; -.
DR EnsemblFungi; AAS50338; AAS50338; AGOS_AAL028W.
DR GeneID; 4618454; -.
DR KEGG; ago:AGOS_AAL028W; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; Q75EV6; -.
DR OMA; VLSEAMW; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000000591; Chromosome I.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Elongation factor; Hydrolase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1044
FT /note="Elongation factor 3"
FT /id="PRO_0000093453"
FT REPEAT 5..42
FT /note="HEAT 1"
FT REPEAT 45..80
FT /note="HEAT 2"
FT REPEAT 86..123
FT /note="HEAT 3"
FT REPEAT 124..162
FT /note="HEAT 4"
FT REPEAT 166..203
FT /note="HEAT 5"
FT REPEAT 205..241
FT /note="HEAT 6"
FT REPEAT 242..279
FT /note="HEAT 7"
FT REPEAT 285..323
FT /note="HEAT 8"
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..1000
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"
SQ SEQUENCE 1044 AA; 115848 MW; B5E4DCD5DB989DF6 CRC64;
MSDSAQSIKV LGELFEKLSV ATAENREATA TEIASFLNGN IIEHDVPEEF FKNLTKAVKD
KKTAAAALET IAHIANENNL SPSVEPYIVD LVPEVCVKTG DKDKDVQSIA SETLLAIVKA
IDPVAIKVIL PHLTKSLVTT NKWQEKVSVL AAISALVDAA KTQVALRMPE LIPVLSEAMW
DTKKEVKHAA TATMTKATET VDNKDIERFI PELIQCIADP SQVSETVHLL GATTFVAEVT
PATLSIMVPL LNRGLAERET SIKRKAAVII DNMCKLVEDP QVVAPFLEKL LPGLKNNFAT
IADPEAREVT LRGLKTLRRV GNVSDDDTLP EVSHAGDIVT TRGVLDELTK DTPIAPRFAP
VVNYIAAIAA DLIDERIIDQ QAWFTHVTPY MTVFFHEKQS KEIIDDFRKR AVDNIPVGPN
FDDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRARRYG LCGPNGAGKS TLMRAIANGQ
VDGFPTQDEC RTVYVEHDID GTQADTSVLD FVFQGDVGTR EVITEKLREF GFSDEMIAMP
IMSLSGGWKM KLALARAVLK NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSIIVSHDS
GFLDNVCQYI IHYEGLKLRK YKGNLSEFVK KCPTAKSYYE LGASDLEFKF PEPGFLEGVK
TKQKAIVKVS NMSFQYPGTS KPQIADINFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP
TTGEVYTHEN CRIAYIKQHA FAHIENHLDK TPSEYIQWRF QTGEDRETMD RANRQINESD
AESMNKIFKI DGTPRRIAGI HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWL
PRGELIESHS KMVAEVDMKE ALASGQFRPL TRKEIEEHCA MLGLEAELVS HSRIRGLSGG
QKVKLVLAAC TWQRPHLIVL DEPTNYLDRD SLGALSKALK AFEGGVIIIT HSAEFTKDLT
EEVWAVKDGI MTPSGHNWVS GQGSGPRLEK KEDEGDKFDA MGNKIATGNK KKKLSSAELR
KKKKERMKKK KELGDAYVSS DDEF
