ERF3_OGAPI
ID ERF3_OGAPI Reviewed; 741 AA.
AC P23637;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Omnipotent suppressor protein 2;
DE AltName: Full=Polypeptide release factor 3;
DE AltName: Full=Translation release factor 3;
GN Name=SUP2;
OS Ogataea pini (Yeast) (Pichia pinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=4923;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MH4;
RX PubMed=2080663; DOI=10.1002/yea.320060603;
RA Kushnirov V.V., Ter-Avanesyan M.D., Didichenko S.A., Smirnov V.N.,
RA Chernoff Y.O., Derkach I.L., Novikova O.N., Inge-Vechtomov S.G.,
RA Neistat M.A., Tolstorukov I.I.;
RT "Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and
RT Saccharomyces cerevisiae.";
RL Yeast 6:461-472(1990).
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; X56910; CAA40231.1; -; Genomic_DNA.
DR PIR; S12921; S12921.
DR AlphaFoldDB; P23637; -.
DR SMR; P23637; -.
DR PRIDE; P23637; -.
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..741
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091487"
FT DOMAIN 316..541
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 5..135
FT /note="Several sort of repeats"
FT REGION 59..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..311
FT /note="Charged"
FT REGION 199..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..332
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 381..385
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 402..405
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 464..467
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 505..507
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 59..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 325..332
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 464..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 741 AA; 82373 MW; A3F30DA3B367EB45 CRC64;
MSQDQQQQQQ FNANNLAGNV QNINLNAPAY DPAVQSYIPN TAQAFVPSAQ PYIPGQQEQQ
FGQYGQQQQN YNQGGYNNYN NRGGYSNNRG GYNNSNRGGY SNYNSYNTNS NQGGYSNYNN
NYANNSYNNN NNYNNNYNQG YNNYNSQPQG QDQQQETGSG QMSLEDYQKQ QKESLNKLNT
KPKKVLKLNL NSSTVKAPIV TKKKEEEPVN QESKTEEPAK EEIKNQEPAE AENKVEEESK
VEAPTAAKPV SESEFPASTP KTEAKASKEV AAAAAALKKE VSQAKKESNV TNADALVKEQ
EEQIDASIVN DMFGGKDHMS IIFMGHVDAG KSTMGGNLLF LTGAVDKRTV EKYEREAKDA
GRQGWYLSWI MDTNKEERND GKTIEVGKSY FETDKRRYTI LDAPGHKLYI SEMIGGASQA
DVGVLVISSR KGEYEAGFER GGQSREHAIL AKTQGVNKLV VVINKMDDPT VNWSKERYEE
CTTKLAMYLK GVGYQKGDVL FMPVSGYTGA GLKERVSQKD APWYNGPSLL EYLDSMPLAV
RKINDPFMLP ISSKMKDLGT VIEGKIESGH VKKGQNLLVM PNKTQVEVTT IYNETEAEAD
SAFCGEQVRL RLRGIEEEDL SAGYVLSSIN HPVKTVTRFE AQIAIVELKS ILSTGFSCVM
HVHTAIEEVT FTQLLHNLQK GTNRRSKKAP AFAKQGMKII AVLETTEPVC IESYDDYPQL
GRFTLRDQGQ TIAIGKVTKL L
