ERF3_CANAX
ID ERF3_CANAX Reviewed; 715 AA.
AC O13354;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2005E;
RX PubMed=11932450; DOI=10.1099/00221287-148-4-1049;
RA Resende C., Parham S.N., Tinsley C., Ferreira P., Duarte J.A., Tuite M.F.;
RT "The Candida albicans Sup35p protein (CaSup35p): function, prion-like
RT behaviour and an associated polyglutamine length polymorphism.";
RL Microbiology 148:1049-1060(2002).
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; AF020554; AAB82541.1; -; Genomic_DNA.
DR AlphaFoldDB; O13354; -.
DR SMR; O13354; -.
DR PRIDE; O13354; -.
DR VEuPathDB; FungiDB:C2_09720W_A; -.
DR VEuPathDB; FungiDB:CAWG_06045; -.
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; Repeat.
FT CHAIN 1..715
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091483"
FT DOMAIN 290..515
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5..128
FT /note="Several sort of repeats"
FT REGION 129..285
FT /note="Charged"
FT REGION 168..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..306
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 355..359
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 376..379
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 438..441
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 479..481
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 168..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 376..380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 438..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 79074 MW; 740964B9561C49B3 CRC64;
MANASLNGDQ SKQQQQQQQQ QQQQQNYYNP NAAQSFVPQG GYQQFQQFQP QQQQQQYGGY
NQYNQYQGGY QQNYNNRGGY QQGYNNRGGY QQNYNNRGGY QGYNQNQQYG GYQQYNSQPQ
QQQQQQSQGM SLADFQKQKT EQQASLNKPA VKKTLKLAGS SGIKLANATK KVDTTSKPQS
KESSPAPAPA ASASASAPQE EKKEEKEAAA ATPAAAPETK KETSAPAETK KEATPTPAAK
NESTPIPAAA AKKESTPVSN SASVATADAL VKEQEDEIDE EVVKDMFGGK DHVSIIFMGH
VDAGKSTMGG NILYLTGSVD KRTVEKYERE AKDAGRQGWY LSWVMDTNKE ERNDGKTIEV
GKAYFETDKR RYTILDAPGH KMYVSEMIGG ASQADVGILV ISARKGEYET GFEKGGQTRE
HALLAKTQGV NKIIVVVNKM DDSTVGWSKE RYQECTTKLG AFLKGIGYAK DDIIYMPVSG
YTGAGLKDRV DPKDCPWYDG PSLLEYLDNM DTMNRKINGP FMMPVSGKMK DLGTIVEGKI
ESGHVKKGTN LIMMPNKTPI EVLTIFNETE QECDTAFSGE QVRLKIKGIE EEDLQPGYVL
TSPKNPVKTV TRFEAQIAIV ELKSILSNGF SCVMHLHTAI EEVKFIELKH KLEKGTNRKS
KKPPAFAKKG MKIIAILEVG ELVCAETYKD YPQLGRFTLR DQGTTIAIGK ITKLL
