EF3_CANAL
ID EF3_CANAL Reviewed; 1050 AA.
AC P25997; A0A1D8PN72; Q59NQ0; Q59NU9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Elongation factor 3;
DE Short=EF-3;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P16521};
GN Name=CEF3; Synonyms=TEF3; OrderedLocusNames=CAALFM_C501580CA;
GN ORFNames=CaO19.11629, CaO19.4152;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=1579463; DOI=10.1093/nar/20.7.1705;
RA Myers K.K., Fonzi W.A., Sypherd P.S.;
RT "Isolation and sequence analysis of the gene for translation elongation
RT factor 3 from Candida albicans.";
RL Nucleic Acids Res. 20:1705-1710(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1626427; DOI=10.1002/yea.320080502;
RA Didomenico B., Lupisella J.A., Sandbaken M.G., Chakraburtty K.;
RT "Isolation and sequence analysis of the gene encoding translation
RT elongation factor 3 from Candida albicans.";
RL Yeast 8:337-352(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-148.
RX PubMed=1584022; DOI=10.1111/j.1365-2958.1992.tb02168.x;
RA Colhurst D.R., Schauder B.S., Hyaes M.V., Tuite M.F.;
RT "Elongation factor 3 (EF-3) from Candida albicans shows both structural and
RT functional similarity to EF-3 from Saccharomyces cerevisiae.";
RL Mol. Microbiol. 6:1025-1033(1992).
RN [7]
RP PROTEIN SEQUENCE OF 301-306 AND 309-310, SUBCELLULAR LOCATION, AND
RP ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(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:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: Has antigenic properties.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; Z11484; CAA77567.1; -; Genomic_DNA.
DR EMBL; Z12822; CAA78282.1; -; Genomic_DNA.
DR EMBL; CP017627; AOW29591.1; -; Genomic_DNA.
DR PIR; S25363; S25363.
DR RefSeq; XP_711356.2; XM_706264.2.
DR AlphaFoldDB; P25997; -.
DR SMR; P25997; -.
DR BioGRID; 1230099; 2.
DR STRING; 237561.P25997; -.
DR COMPLUYEAST-2DPAGE; P25997; -.
DR PRIDE; P25997; -.
DR GeneID; 3647040; -.
DR KEGG; cal:CAALFM_C501580CA; -.
DR CGD; CAL0000190871; CEF3.
DR VEuPathDB; FungiDB:C5_01580C_A; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; P25997; -.
DR OrthoDB; 164580at2759; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:P25997; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0002181; P:cytoplasmic translation; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Elongation factor;
KW Hydrolase; Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..1050
FT /note="Elongation factor 3"
FT /id="PRO_0000093454"
FT REPEAT 46..83
FT /note="HEAT 1"
FT REPEAT 89..126
FT /note="HEAT 2"
FT REPEAT 127..165
FT /note="HEAT 3"
FT REPEAT 169..206
FT /note="HEAT 4"
FT REPEAT 208..244
FT /note="HEAT 5"
FT REPEAT 245..282
FT /note="HEAT 6"
FT REPEAT 288..326
FT /note="HEAT 7"
FT DOMAIN 429..646
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 672..998
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 980..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1034
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 706..713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 111
FT /note="T -> A (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="Missing (in Ref. 1; CAA77567)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="S -> T (in Ref. 1; CAA77567 and 2; CAA78282)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="V -> F (in Ref. 1; CAA77567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 116925 MW; B37507FE3B595B86 CRC64;
MSAASESKYS TEVLSELLSK LQVADNKDEA ASNISTFLNS SIVEHDVPVE FFEDLKKQIQ
SKDAKVSLAA LDAYKHIAST NGLSPSVEPY VVDLVSEVAV KAGDKNKDVQ TAASDALLAI
ASAITPTAVK AILPKLIDNL TNTNKWTEKV AILRAVSQLV DTAKAQIALR MPELIPVLSE
SMWDTKKEVK EAATATMTKS TETIDNKDIE KFIPQLISCI AKPTEVPETV HLLGATTFVS
EVTMATLSIM APLLSRGLAE RDTAIKRKAA VIVDNMCKLV EDPQIVAPFM DKLLPGLKNN
FANMADPEAR EVTQRALNTL RRVGAVGEND SIPEVSTAGD IDVTLNEFNK LVADKKIAKR
FDVALNYIAA IAGDLVDERE IQPEAWLQNV LPFATIFLHE KEAKEIIEEF RKRAIDNIPQ
PPSFEDEEDE GEDLCNCEFS LAYGAKILLN KTQFRLKRNR RYGLCGPNGA GKSTLMRAIA
NGQVEGFPTQ DECKTVYVEH DIDGTHADTT VVEFVIEDGE VGLTKDVVVD KLREFNFSDE
MINMPIQSLS GGWKMKLALA RAVLKNADIL LLDEPTNHLD TVNVAWLVNY LNTCGITSII
VSHDSGFLDN VTQYIIHYEG FKLRKYKGNL SEFVKKCPSA QSYYELGASD LEFRFPEPGF
LEGVKTKQKA IVKVSNMSFQ YPGTSKPQIQ DINFQCSLSS RIAVIGPNGA GKSTLINVLT
GELLPTTGEV YVHENCRIAY IKQHAFAHID NHLDKTPSEY IQWRFQTGED RETMDRASRQ
INEEDEQNMN KIFKIEGTPR RIAGIHARRK FKNSYEYEIS WMLGENIGMK NERWVPMMSV
DNTWLPRGEL METHAKLVAE VDMKEALASG QFRPLTRKEI EEHCAMLGLD AELVSHSRIR
GLSGGQKVKL VLAACTWQRP HLIVLDEPTN YLDRDSLGAL SKALKAFEGG IVIITHSAEF
TKDLTEEVWA VLDGRMTPSG HNWVQGQGSG PRIEKKDDEE EDKFDAMGNK IAAAKKKKKL
SSAELRKKKK ERMKKKKELG DAYVSSDEEF
