ERF1_SCHPO
ID ERF1_SCHPO Reviewed; 433 AA.
AC P79063;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE Short=Eukaryotic release factor 1;
DE Short=eRF1;
GN Name=sup45; ORFNames=SPAC1834.01;
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=8643594; DOI=10.1073/pnas.93.11.5443;
RA Ito K., Ebihara K., Uno M., Nakamura Y.;
RT "Conserved motifs in prokaryotic and eukaryotic polypeptide release
RT factors: tRNA-protein mimicry hypothesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5443-5448(1996).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; D63883; BAA09933.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB75769.1; -; Genomic_DNA.
DR PIR; T43243; T43243.
DR RefSeq; NP_594680.1; NM_001020109.2.
DR PDB; 3E20; X-ray; 3.50 A; B/C/H/K=1-433.
DR PDBsum; 3E20; -.
DR AlphaFoldDB; P79063; -.
DR SMR; P79063; -.
DR BioGRID; 278624; 3.
DR DIP; DIP-59470N; -.
DR IntAct; P79063; 1.
DR STRING; 4896.SPAC1834.01.1; -.
DR iPTMnet; P79063; -.
DR MaxQB; P79063; -.
DR PaxDb; P79063; -.
DR PRIDE; P79063; -.
DR EnsemblFungi; SPAC1834.01.1; SPAC1834.01.1:pep; SPAC1834.01.
DR GeneID; 2542148; -.
DR KEGG; spo:SPAC1834.01; -.
DR PomBase; SPAC1834.01; sup45.
DR VEuPathDB; FungiDB:SPAC1834.01; -.
DR eggNOG; KOG0688; Eukaryota.
DR HOGENOM; CLU_035759_2_1_1; -.
DR InParanoid; P79063; -.
DR OMA; GQEMEVV; -.
DR PhylomeDB; P79063; -.
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; P79063; -.
DR PRO; PR:P79063; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0018444; C:translation release factor complex; IDA:PomBase.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:PomBase.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR GO; GO:1990825; F:sequence-specific mRNA binding; EXP:PomBase.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central.
DR GO; GO:0002184; P:cytoplasmic translational termination; IPI:PomBase.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR Gene3D; 3.30.960.10; -; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR024049; eRF1_1_sf.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR PANTHER; PTHR10113; PTHR10113; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF55481; SSF55481; 1.
DR TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..433
FT /note="Eukaryotic peptide chain release factor subunit 1"
FT /id="PRO_0000143166"
FT MOD_RES 182
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:3E20"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 373..380
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:3E20"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:3E20"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:3E20"
SQ SEQUENCE 433 AA; 48803 MW; 5648B6EA2FD90997 CRC64;
MSETAEKAIE IWKIRRLVKQ LINCHGNGTS MITLIIPPGE QISRYSNMLA EEYGTASNIK
SRVNRLSVLS AITSTRERLK LYNKVPDNGL VIYCGEVIME GNKTRKLNID FEPFKPINTS
QYLCDNKFHT EALAELLESD QRFGFIVMDG HQTLYGVVSG SAREVLQRFT VDLPKKHGRG
GQSALRFARL RDEKRHNYVR KVAEGAVQHF ITDDKPNVAG IVLAGSADFK TELGQSDLFD
QRLQSRIIKT VDVSYGGDAG FNQAIELAAD TLSNVKYVQE KKLIQRFFDE ISLDSGKYCF
GVVDTMNALQ EGAVETLLCF ADLDMIRYEF KNSEGNPVIT YMTKEQEEKD STNSFLLDKD
TGAEMELVSS MLLSEWLAEH YKDYGANLEF VSDRSQEGMQ FVKGFGGIGA VMRYQLDLSM
LDPESDEFYS DSD
