ERF3_KLULA
ID ERF3_KLULA Reviewed; 700 AA.
AC Q9HGI8; Q6CQF8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit;
DE AltName: Full=ERF-3;
DE Short=ERF3;
DE AltName: Full=ERF2;
DE AltName: Full=Polypeptide release factor 3;
DE AltName: Full=Translation release factor 3;
GN Name=SUP35; OrderedLocusNames=KLLA0D17424g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11430816; DOI=10.1016/s1097-2765(01)00259-3;
RA Nakayashiki T., Ebihara K., Bannai H., Nakamura Y.;
RT "Yeast [PSI+] 'prions' that are crosstransmissible and susceptible beyond a
RT species barrier through a quasi-prion state.";
RL Mol. Cell 7:1121-1130(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: Involved in translation termination. Stimulates the activity
CC of ERF1. Binds guanine nucleotides.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. ERF3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AB039749; BAB12680.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00927.1; -; Genomic_DNA.
DR RefSeq; XP_453831.1; XM_453831.1.
DR AlphaFoldDB; Q9HGI8; -.
DR SMR; Q9HGI8; -.
DR STRING; 28985.XP_453831.1; -.
DR EnsemblFungi; CAH00927; CAH00927; KLLA0_D17424g.
DR GeneID; 2893045; -.
DR KEGG; kla:KLLA0_D17424g; -.
DR eggNOG; KOG0459; Eukaryota.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; Q9HGI8; -.
DR OMA; KINAPFM; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0018444; C:translation release factor complex; IEA:EnsemblFungi.
DR GO; GO:0019003; F:GDP binding; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0000287; F:magnesium ion binding; IEA:EnsemblFungi.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:EnsemblFungi.
DR GO; GO:0003747; F:translation release factor activity; IEA:EnsemblFungi.
DR GO; GO:0002184; P:cytoplasmic translational termination; IEA:EnsemblFungi.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003285; Sup35.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01343; YEASTERF.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..700
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091486"
FT DOMAIN 272..498
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 10..136
FT /note="Several sort of repeats"
FT REGION 114..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..267
FT /note="Charged"
FT REGION 281..288
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 337..341
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 358..361
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 420..423
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 462..464
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 114..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 358..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 420..423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 700 AA; 77639 MW; 53F9905442F6B025 CRC64;
MSDQQNQDQG QGQGYNQYNQ YGQYNQYYNQ QGYQGYNGQQ GAPQGYQAYQ AYGQQPQGAY
QGYNPQQAQG YQPYQGYNAQ QQGYNAQQGG HNNNYNKNYN NKNSYNNYNK QGYQGAQGYN
AQQPTGYAAP AQSSSQGMTL KDFQNQQGST NAAKPKPKLK LASSSGIKLV GAKKPVAPKT
EKTDESKEAT KTTDDNEEAQ SELPKIDDLK ISEAEKPKTK ENTPSADDTS SEKTTSAKAD
TSTGGANSVD ALIKEQEDEV DEEVVKDMFG GKDHVSIIFM GHVDAGKSTM GGNLLYLTGS
VDKRTVEKYE REAKEAGRQG WYLSWVMDTN KEERNDGKTI EVGRAYFETE KRRYTILDAP
GHKMYVSEMI GGASQADIGI LVISARKGEY ETGFEKGGQT REHALLAKTQ GVNKMIVVIN
KMDDPTVGWD KERYDHCVGN LTNFLKAVGY NVKEDVIFMP VSGYTGAGLK ERVDPKDCPW
YTGPSLLEYL DNMKTTDRHI NAPFMLPIAS KMKDMGTVVE GKIESGHIRK GNQTLLMPNR
TSVEILTIYN ETESEVDMAV CGEQVRLRIK GVEEEEISAG FVLTSPKNPV KNVTRFVAQI
AIVELKSIMS AGFSCVMHIH TAIEEVTVTR LLHKLEKGSN RKSKKPPAFA KKGMKIIAVI
ETNEPVCVET YDDYPQLGRF TLRDQGTTIA IGKIVKILEN
