EF3_CANGA
ID EF3_CANGA Reviewed; 1045 AA.
AC O93796; Q6FXJ2;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Elongation factor 3;
DE Short=EF-3;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P16521};
GN Name=TEF3; OrderedLocusNames=CAGL0B03487g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=9782488; DOI=10.1099/00221287-144-9-2407;
RA Nakayama H., Izuta M., Nagahashi S., Sihta E.Y., Sato Y., Yamazaki T.,
RA Arisawa M., Kitada K.;
RT "A controllable gene-expression system for the pathogenic fungus Candida
RT glabrata.";
RL Microbiology 144:2407-2415(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AB012141; BAA33959.1; -; Genomic_DNA.
DR EMBL; CR380948; CAG58023.1; -; Genomic_DNA.
DR RefSeq; XP_445123.1; XM_445123.1.
DR AlphaFoldDB; O93796; -.
DR SMR; O93796; -.
DR STRING; 5478.XP_445123.1; -.
DR PRIDE; O93796; -.
DR EnsemblFungi; CAG58023; CAG58023; CAGL0B03487g.
DR GeneID; 2886522; -.
DR KEGG; cgr:CAGL0B03487g; -.
DR CGD; CAL0127772; TEF3.
DR VEuPathDB; FungiDB:CAGL0B03487g; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; O93796; -.
DR OMA; VLSEAMW; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002428; Chromosome B.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblFungi.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0042788; C:polysomal ribosome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IEA:EnsemblFungi.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0006415; P:translational termination; 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; 2.
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..1045
FT /note="Elongation factor 3"
FT /id="PRO_0000093455"
FT REPEAT 5..42
FT /note="HEAT 1"
FT REPEAT 43..85
FT /note="HEAT 2"
FT REPEAT 86..123
FT /note="HEAT 3"
FT REPEAT 125..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 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 974..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1028
FT /note="Basic 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 CONFLICT 854
FT /note="A -> T (in Ref. 1; BAA33959)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="K -> R (in Ref. 1; BAA33959)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="E -> K (in Ref. 1; BAA33959)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="V -> F (in Ref. 1; BAA33959)"
FT /evidence="ECO:0000305"
FT CONFLICT 971
FT /note="M -> I (in Ref. 1; BAA33959)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="K -> R (in Ref. 1; BAA33959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1045 AA; 115896 MW; 12E91A1A0DDCE9EE CRC64;
MTDSDQSLKV LEELFKNLSV ATADNRVEAA QEVASFLNGN IIEHDIPEKF FEELAKAVKD
KKTSANFLEA VAHIANEANL SPSVEPFVIT LVPEICAKAG DKDKDVQAVA SKTLVAISKA
INPVAIKAYL PHLTKSLETT NKWQEKVSVL AAISALVDAA KEQVALRMPE LIPVLSETMW
DTKKEVKEAA TATMTKATET VDNKDIERFI PQLISCIADP KQVPETVHLL GATTFVAEVT
PATLSIMVPL LSRGLAERET SIKRKAAVII DNMCKLVEDP QVVAPFLDKL LPGLKNNYAT
IADPEAREVT LRGLKTLRRV GNVTEDDVLP EISHAGDIET TLGVINELLK GENVAPRFKI
VVEYIAAMAG DLIDERVIDQ QAWFTHITPY MTIFMHERNA KDVLDEFRKR AVDNIPVGPN
FDDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRGRRYG LCGPNGAGKS TLMRAIANGQ
VDGFPTPEEC MTVYVEHDID GTHADTSVLD FVVSSEVGTK EAITAKLVEF GFTEEMINMP
ISSLSGGWKM KLALARAVLK NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSVIVSHDS
GFLDNVCQYI IHYEGLKLRK YKGNLSEFVK KCPTAQSYYE LGASDLEFKF PEPGYLEGVK
TKQKAIVKVS NMTFQYPGTS KPQISDISFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP
TSGEVYTHEN CRIAYIKQHA FAHIESHLDK TPSEYIQWRF QTGEDRETMD RANRQINEND
AEAMNKIFKI EGTPRRIAGI HARRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI
PRGELVESHS KMVAEVDMKE ALASGQFRPL TRKEIEEHCA MLGLDAELVS HSRIRGLSGG
QKVKLVLAAC SWQRPHLIVL DEPTNYLDRD SLGALSKALK AFEGGVIIIT HSAEFTKNLT
EEVWAVKDGK MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA MGNKIAGGKK KKKLSSAELR
KKKKERMKKK KELGDAYVSS DDEDF
