ERF3_DICDI
ID ERF3_DICDI Reviewed; 557 AA.
AC Q7YZN9; Q54Y49;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit;
DE AltName: Full=ERF2;
DE AltName: Full=Eukaryotic release factor 3;
DE Short=ERF-3;
DE Short=ERF3;
DE AltName: Full=Polypeptide release factor 3;
DE AltName: Full=Translation release factor 3;
GN Name=erf3; ORFNames=DDB_G0277919;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12853641; DOI=10.1093/nar/gkg440;
RA Inagaki Y., Blouin C., Susko E., Roger A.J.;
RT "Assessing functional divergence in EF-1alpha and its paralogs in
RT eukaryotes and archaebacteria.";
RL Nucleic Acids Res. 31:4227-4237(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Involved in translation termination. Stimulates the activity
CC of erf1. Binds guanine nucleotides (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AY185331; AAO61461.1; -; mRNA.
DR EMBL; AAFI02000023; EAL68132.1; -; Genomic_DNA.
DR RefSeq; XP_642353.1; XM_637261.1.
DR AlphaFoldDB; Q7YZN9; -.
DR SMR; Q7YZN9; -.
DR STRING; 44689.DDB0214990; -.
DR PaxDb; Q7YZN9; -.
DR EnsemblProtists; EAL68132; EAL68132; DDB_G0277919.
DR GeneID; 8621558; -.
DR KEGG; ddi:DDB_G0277919; -.
DR dictyBase; DDB_G0277919; eRF3.
DR eggNOG; KOG0459; Eukaryota.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; Q7YZN9; -.
DR OMA; KINAPFM; -.
DR PhylomeDB; Q7YZN9; -.
DR Reactome; R-DDI-72764; Eukaryotic Translation Termination.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q7YZN9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0018444; C:translation release factor complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003747; F:translation release factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
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 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 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..557
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000328333"
FT DOMAIN 115..342
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 40..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..131
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 180..184
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 201..204
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 262..265
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 304..306
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 262..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 60698 MW; 9D684D1948ADB53B CRC64;
MKLNPNASSF VPKFVAKPAA PAPAAPVAVV AEPVAAPVVA EPTPTPAPVE TKEEPTTTAT
TTSVSSIKTE EDLENIKPTE SVYKVEDDDI EDDDEVDEVA EKIEQVVKVL PEDSREHLNI
VFLGHVDAGK STLSGSIMVL TGQVDPHTLA KYEREAKENH REGWIYAYIM DTNEEERTKG
KTVEVGRAHF ETTKKRYTIL DAPGHRLYVP NMIIGAAQAD VGILVISSKK GEFEAGVEGG
QTIEHARLAK MIGIKYLVVF VNKMDEPTVK WSKARYDEIT DKLTVHLKKC GWNPKKDFHF
VPGSGYGTLN VLAPLAPGVC DWYSGPSLIG TLDNLSGMER NEGGALRIPI TTSYKDRGIV
NVIGKVESGT ISVGQSIHIM PGKTKVEVIS LTGDICSFKT ARPGENITIA LKGIEGDDSI
RPGSILAEIN RPVPVVSEIE AIVYILDMPE ERRLFTPSFS AIFHAHTAVE DVTVKSLIAT
IDTKTSTEIK QKPTFCKVGD AVKCRLVLGR AVCLEEFTTN PQLARFTIRD STKTIAFGKV
INIGKKAKEE IARQTKA
