ERF3_SCHPO
ID ERF3_SCHPO Reviewed; 662 AA.
AC O74718; P78857;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 166.
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; ORFNames=SPCC584.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JY333;
RX PubMed=9701287; DOI=10.1017/s1355838298971874;
RA Ito K., Ebihara K., Nakamura Y.;
RT "The stretch of C-terminal acidic amino acids of translational release
RT factor eRF1 is a primary binding site for eRF3 of fission yeast.";
RL RNA 4:958-972(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 383-662.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND SER-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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; D79214; BAA33530.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21821.1; -; Genomic_DNA.
DR EMBL; D89207; BAA13868.1; -; mRNA.
DR PIR; T41442; T41442.
DR PIR; T43011; T43011.
DR PIR; T51948; T51948.
DR RefSeq; NP_588225.1; NM_001023215.2.
DR PDB; 1R5B; X-ray; 2.35 A; A=196-662.
DR PDB; 1R5N; X-ray; 2.90 A; A=196-662.
DR PDB; 1R5O; X-ray; 3.20 A; A=196-662.
DR PDB; 3E20; X-ray; 3.50 A; A/D/E/J=467-662.
DR PDBsum; 1R5B; -.
DR PDBsum; 1R5N; -.
DR PDBsum; 1R5O; -.
DR PDBsum; 3E20; -.
DR AlphaFoldDB; O74718; -.
DR SMR; O74718; -.
DR BioGRID; 276042; 10.
DR DIP; DIP-59469N; -.
DR IntAct; O74718; 1.
DR STRING; 4896.SPCC584.04.1; -.
DR iPTMnet; O74718; -.
DR MaxQB; O74718; -.
DR PaxDb; O74718; -.
DR PRIDE; O74718; -.
DR EnsemblFungi; SPCC584.04.1; SPCC584.04.1:pep; SPCC584.04.
DR GeneID; 2539479; -.
DR KEGG; spo:SPCC584.04; -.
DR PomBase; SPCC584.04; sup35.
DR VEuPathDB; FungiDB:SPCC584.04; -.
DR eggNOG; KOG0459; Eukaryota.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; O74718; -.
DR OMA; KINAPFM; -.
DR PhylomeDB; O74718; -.
DR Reactome; R-SPO-72764; Eukaryotic Translation Termination.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; O74718; -.
DR PRO; PR:O74718; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0018444; C:translation release factor complex; IDA:PomBase.
DR GO; GO:0019003; F:GDP binding; IMP:CAFA.
DR GO; GO:0005525; F:GTP binding; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0002184; P:cytoplasmic translational termination; IGI:PomBase.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:InterPro.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR DisProt; DP00396; -.
DR Gene3D; 3.40.50.300; -; 1.
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; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..662
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091488"
FT DOMAIN 236..464
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..252
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 301..305
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 322..325
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 384..387
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 427..429
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 322..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 384..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 79..80
FT /note="QQ -> LL (in Ref. 1; BAA33530)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="E -> D (in Ref. 3; BAA13868)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..398
FT /note="RY -> SN (in Ref. 3; BAA13868)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="E -> G (in Ref. 1; BAA33530)"
FT /evidence="ECO:0000305"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1R5N"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1R5N"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:1R5N"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:1R5O"
FT HELIX 395..413
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:1R5B"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1R5O"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 451..457
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 475..487
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:1R5B"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 556..566
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:1R5O"
FT STRAND 621..630
FT /evidence="ECO:0007829|PDB:1R5B"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:1R5B"
FT HELIX 638..641
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:1R5B"
FT STRAND 652..661
FT /evidence="ECO:0007829|PDB:1R5B"
SQ SEQUENCE 662 AA; 72556 MW; 54AE41EA6AF6168A CRC64;
MASNQPNNGE QDEQLAKQTS KLSMSAKAPT FTPKAAPFIP SFQRPGFVPV NNIAGGYPYA
QYTGQGQNSN SPHPTKSYQQ YYQKPTGNTV DEDKSRVPDF SKKKSFVPPK PAIPKGKVLS
LGGNTSAPKS TKPISISLGG TKAPTTTKPA APAAQSKTET PAPKVTSEST KKETAAPPPQ
ETPTKSADAE LAKTPSAPAA ALKKAAEAAE PATVTEDATD LQNEVDQELL KDMYGKEHVN
IVFIGHVDAG KSTLGGNILF LTGMVDKRTM EKIEREAKEA GKESWYLSWA LDSTSEEREK
GKTVEVGRAY FETEHRRFSL LDAPGHKGYV TNMINGASQA DIGVLVISAR RGEFEAGFER
GGQTREHAVL ARTQGINHLV VVINKMDEPS VQWSEERYKE CVDKLSMFLR RVAGYNSKTD
VKYMPVSAYT GQNVKDRVDS SVCPWYQGPS LLEYLDSMTH LERKVNAPFI MPIASKYKDL
GTILEGKIEA GSIKKNSNVL VMPINQTLEV TAIYDEADEE ISSSICGDQV RLRVRGDDSD
VQTGYVLTST KNPVHATTRF IAQIAILELP SILTTGYSCV MHIHTAVEEV SFAKLLHKLD
KTNRKSKKPP MFATKGMKII AELETQTPVC MERFEDYQYM GRFTLRDQGT TVAVGKVVKI
LD
