ID   ERF3_ZYGRO              Reviewed;         662 AA.
AC   Q9HGI4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 83.
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;
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 42981 / IAM 12879 / JCM 22060 / S-96;
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).
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; AB039753; BAB12684.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HGI4; -.
DR   SMR; Q9HGI4; -.
DR   eggNOG; KOG0459; Eukaryota.
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; 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; Repeat.
FT   CHAIN           1..662
FT                   /note="Eukaryotic peptide chain release factor GTP-binding
FT                   subunit"
FT                   /id="PRO_0000091489"
FT   DOMAIN          235..461
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          9..102
FT                   /note="Several sort of repeats"
FT   REGION          73..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..230
FT                   /note="Charged"
FT   REGION          244..251
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          300..304
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          321..324
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          383..386
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          425..427
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   COMPBIAS        85..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         244..251
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         321..325
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         383..386
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         318
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   662 AA;  73780 MW;  2641046199FB1E04 CRC64;
     MSDPNQNGQQ GGQQNAGGNY YQQYFQKLTQ QAQAGGGYQP YGGYGGYGGY GGYQPYGGYQ
     QFYQDGQQAQ QGAYNGYPYQ AQGAPGGFNN YNNQFQPQQQ SQGMTLDDFH KQKQTSQSAP
     PKQKKSLKLV SSSGIKLANA TKKPKEDEKK EEEPKKEEKK AEPKEQESKK EEPKREGTPR
     PAAAKDEKKE DLPKLEKLKI KEEQAAANAS GADSLIKEQE EEVDEGVVND MFGGKDHMSI
     IFMGHVDAGK STMGGNILYM TGSVDKRTVE KYEREAKDAG KQGWYLSWVM DTNREERDDG
     KTIEVGRAYF ETEKRRYTIL DAPGHKMYVS EMIGGASQAD VGILVISARK GEYETGFEKG
     GQTREHALLA KTQGVNKLIV TINKMDDPTV NWSKERYDQC VKNLSNFLKA IGYNVKEEVV
     FMPVSGYSGA GLGTRVDPKE CPWYDGPALL EYMDNMSHVD RKMNAPFMLP IAAKMRDMGT
     IVEGKIESGH IRKGHSTLLM PNKIPVEIQN IYNETENEVD MAICGEQVKL KIKGVEEEDI
     APGFVLTSPK NPVKNVTRFV AQVAIVELKS ILSSGFSCVM HVHTAIEEVR ITKLLHKLER
     GTNRKSKKPP AFAKKGMKII AVLETERPVC VETYQDYPQL GRFTLRDQGT TIAIGKIVKI
     IE