ERF3_CANMA
ID ERF3_CANMA Reviewed; 712 AA.
AC Q9HGI7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 79.
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 maltosa (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5479;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
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; AB039750; BAB12681.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9HGI7; -.
DR SMR; Q9HGI7; -.
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..712
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091484"
FT DOMAIN 287..512
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 16..143
FT /note="Several sort of repeats"
FT REGION 76..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..282
FT /note="Charged"
FT REGION 184..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..303
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 352..356
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 373..376
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 435..438
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 476..478
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 198..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 373..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 435..438
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 712 AA; 78631 MW; 729B6A814735C469 CRC64;
MSNPQDQLSN DLANASISGD QSKQPQQQQP QQQQPYFNPN QAQAFVPTGG YQQFQPQQQQ
QYGGYQQNYT QYQAGGYQQN YNNRGGYQQN YNNRGGYQQN YNNRGGYQQQ QQQQYQAYNP
NQQYGGYQAY NPQQQQQQQT QSQGMSLADF QKQKAEQQAS LNKPAVKKTL KLASSSGIKL
ANATKKVDTA KPAASKEASP APKDEEASAE PEAKKESTPV PASSSPAPAA ADSTPAPVKK
ESTPTPSVAS KSAPVSASAS VVTADALAKE QEDEVDEEVV KDMFGGKDHV SIIFMGHVDA
GKSTMGGNIL YLTGSVDKRT VEKYEREAKD AGRQGWYLSW VMDTNKEERN DGKTIEVGKA
YFETDKRRYT ILDAPGHKMY VSEMIGGASQ ADVGILVISA RKGEYETGFE KGGQTREHAL
LAKTQGVNKI IVVVNKMDDP TVNWSKERYQ ECTTKLGVFL KGIGYNKDDI INMPVSGYTG
AGLKDRVNPK DCPWYEGPSL LEYLDNMDTM NRKINGPFMM PVSGKMKDLG TVVEGKIESG
HVKKGTNLIL MPNKTPVEVL TIYNETEQEA DTAFSGEQVR LKIKGVEEED LQPGYVLTSP
KNPVKTVTKF EAQIAIVELK SILSNGFSCV MHLHTAIEEV KFVELKHKLE KGTNRKSKKP
PAFAKKGMKI IAILEVSEPV CAETYKDYPQ LGRFTLRDQG TTIAIGKITK LL
