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Database: UniProt
Entry: Q75EV6
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Original site: Q75EV6 
ID   EF3_EREGS               Reviewed;        1044 AA.
AC   Q75EV6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   24-JAN-2024, entry version 115.
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   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya 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; 284811.Q75EV6; -.
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   OrthoDB; 49929at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblFungi.
DR   GO; GO:0042788; C:polysomal 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:0001933; P:negative regulation of protein phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR   CDD; cd03221; ABCF_EF-3; 1.
DR   CDD; cd18626; CD_eEF3; 1.
DR   CDD; cd00882; Ras_like_GTPase; 1.
DR   Gene3D; 1.20.1390.20; -; 1.
DR   Gene3D; 2.40.50.990; -; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; eEF3_ABC2_chromodomain-like.
DR   InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR   InterPro; IPR040533; EF3_4HB.
DR   InterPro; IPR047036; EF3_4HB_sf.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   PANTHER; PTHR19211:SF5; ELONGATION FACTOR 3A-RELATED; 1.
DR   Pfam; PF17947; 4HB; 1.
DR   Pfam; PF00005; ABC_tran; 3.
DR   Pfam; PF21040; CEP104-like_TOG; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
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