ERF3_DEBHA
ID ERF3_DEBHA Reviewed; 701 AA.
AC Q9HGI6; Q6BWQ4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 4.
DT 03-AUG-2022, entry version 113.
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=DEHA2B09526g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
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 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; AB039751; BAB12682.3; -; Genomic_DNA.
DR EMBL; CR382134; CAG85369.1; -; Genomic_DNA.
DR RefSeq; XP_457365.1; XM_457365.1.
DR AlphaFoldDB; Q9HGI6; -.
DR SMR; Q9HGI6; -.
DR STRING; 4959.XP_457365.1; -.
DR EnsemblFungi; CAG85369; CAG85369; DEHA2B09526g.
DR GeneID; 2913288; -.
DR KEGG; dha:DEHA2B09526g; -.
DR VEuPathDB; FungiDB:DEHA2B09526g; -.
DR eggNOG; KOG0459; Eukaryota.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; Q9HGI6; -.
DR OMA; DNINIRY; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
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; 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..701
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091485"
FT DOMAIN 276..501
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 20..131
FT /note="Several sort of repeats"
FT REGION 91..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..271
FT /note="Charged"
FT REGION 164..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..292
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 341..345
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 362..365
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 424..427
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 465..467
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 230..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 362..366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 424..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 107
FT /note="N -> S (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="E -> Q (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="A -> T (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="V -> A (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="I -> V (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="M -> V (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="A -> T (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="F -> Y (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="I -> V (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="N -> S (in Ref. 1; BAB12682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 77267 MW; 3630E42B7B3CFBA3 CRC64;
MSDDQQYNQD KLSQDFQNTS IGSGEQQQQS YQQYQQQPQQ NNFNANSAPT FTPSGQQGGY
QGGYQGGYQG GYQNYSQGGY QNYNQGYQNY NQGYQGYQNN NRGGYNNYNN RGGYNNYNNY
NQQDQQPVQN QGMSLADFQK QQNAQANLNK PKKTLKLASS SGIKLANAKK APETESKEAT
PAATEKEATP AATEKEATPA ATEKEATPAA TEKETTPAPA KKEATPASVK SESKPASKST
SKVATKESTP VTSDKVIQEQ VDEVDEEVVK DMFGGKDHVS IIFMGHVDAG KSTMGGNILY
LTGSVDKRTV DKYEREAKDA GRQGWYLSWV MDTNKEERSD GKTIEVGKAY FETEKRRYTI
LDAPGHKMYV SEMIGGASQA DVGILVISAR KGEYETGFEK GGQTREHALL AKTQGVNKII
VVVNKMDDPT VGWAEDRYKD CITKLGTFLK GIGYAKDDII FMPVSGYTGA GIKDRVNPKD
CPWYSGPSLL EFLDNMKTMQ RHINGPFMLP ISGKMKDMGT IIEGKIESGH IKKGGNLLLM
PNKASIEVVA IFNETEQECD AAFCGEQVRL KIKGVEEEDL APGYVLTSPL KPIKTITRFE
AQIAIVELKS ILSNGFSCVM HLHTAIEEVT FIELKHKLEK GTNRKSKKPP AFAKKGMKVI
AILETNESVC AETYADYPQL GRFTLRDQGT TIAIGKITKV L
