DOM34_YEAST
ID DOM34_YEAST Reviewed; 386 AA.
AC P33309; D6W1H6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein DOM34;
DE EC=3.1.-.- {ECO:0000269|PubMed:17889667};
GN Name=DOM34; OrderedLocusNames=YNL001W; ORFNames=N2016;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8402262;
RA Lalo D., Stettler S., Mariotte S., Slonimski P.P., Thuriaux P.;
RT "Two yeast chromosomes are related by a fossil duplication of their
RT centromeric regions.";
RL C. R. Acad. Sci. III, Sci. Vie 316:367-373(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=7941739; DOI=10.1002/yea.320100412;
RA Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.;
RT "Organization of the centromeric region of chromosome XIV in Saccharomyces
RT cerevisiae.";
RL Yeast 10:523-533(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7985421; DOI=10.1002/yea.320100709;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast
RT chromosome XIV, encompassing the centromere sequence.";
RL Yeast 10:945-951(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP INTERACTION WITH HBS1.
RX PubMed=11909951; DOI=10.1128/mcb.22.8.2564-2574.2002;
RA Carr-Schmid A., Pfund C., Craig E.A., Kinzy T.G.;
RT "Novel G-protein complex whose requirement is linked to the translational
RT status of the cell.";
RL Mol. Cell. Biol. 22:2564-2574(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION.
RX PubMed=16554824; DOI=10.1038/nature04530;
RA Doma M.K., Parker R.;
RT "Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation
RT elongation.";
RL Nature 440:561-564(2006).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INTERACTION WITH HBS1.
RX PubMed=17889667; DOI=10.1016/j.molcel.2007.07.019;
RA Lee H.H., Kim Y.-S., Kim K.H., Heo I., Kim S.K., Kim O., Kim H.K.,
RA Yoon J.Y., Kim H.S., Kim do J., Lee S.J., Yoon H.J., Kim S.J., Lee B.G.,
RA Song H.K., Kim V.N., Park C.-M., Suh S.W.;
RT "Structural and functional insights into Dom34, a key component of no-go
RT mRNA decay.";
RL Mol. Cell 27:938-950(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, SUBUNIT, INTERACTION WITH
RP HBS1, AND DOMAIN.
RX PubMed=18180287; DOI=10.1074/jbc.m708224200;
RA Graille M., Chaillet M., van Tilbeurgh H.;
RT "Structure of yeast Dom34: a protein related to translation termination
RT factor Erf1 and involved in No-Go decay.";
RL J. Biol. Chem. 283:7145-7154(2008).
CC -!- FUNCTION: Involved in protein translation. Together with HBS1, may
CC function in recognizing stalled ribosomes and triggering
CC endonucleolytic cleavage of the mRNA, a mechanism to release non-
CC functional ribosomes and degrade damaged mRNAs. The complex formed by
CC DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA
CC substrates, but does not cleave single-stranded RNA. Acts as
CC endonuclease; has no exonuclease activity. Increases the affinity of
CC HBS1 for GTP, but nor for GDP. Promotes G1 progression and
CC differentiation and is involved in mitotic and meiotic cell divisions.
CC {ECO:0000269|PubMed:16554824, ECO:0000269|PubMed:17889667,
CC ECO:0000269|PubMed:18180287}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:17889667};
CC -!- SUBUNIT: Monomer. Interacts with HBS1. {ECO:0000269|PubMed:11909951,
CC ECO:0000269|PubMed:17889667, ECO:0000269|PubMed:18180287}.
CC -!- INTERACTION:
CC P33309; P32769: HBS1; NbExp=8; IntAct=EBI-6012, EBI-8194;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold
CC (PubMed:18180287). It harbors the endoribonuclease activity
CC (PubMed:17889667). {ECO:0000269|PubMed:17889667,
CC ECO:0000269|PubMed:18180287}.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34575.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L11277; AAA34575.1; ALT_INIT; Genomic_DNA.
DR EMBL; X77114; CAA54375.1; -; Genomic_DNA.
DR EMBL; Z71277; CAA95860.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10542.1; -; Genomic_DNA.
DR PIR; S45456; S45456.
DR RefSeq; NP_014397.1; NM_001182840.1.
DR PDB; 2VGM; X-ray; 2.60 A; A=1-386.
DR PDB; 2VGN; X-ray; 2.50 A; A/B=1-386.
DR PDB; 3IZQ; EM; -; 0=1-386.
DR PDB; 3J16; EM; -; A=1-386.
DR PDB; 5M1J; EM; 3.30 A; A1=1-381.
DR PDBsum; 2VGM; -.
DR PDBsum; 2VGN; -.
DR PDBsum; 3IZQ; -.
DR PDBsum; 3J16; -.
DR PDBsum; 5M1J; -.
DR AlphaFoldDB; P33309; -.
DR SMR; P33309; -.
DR BioGRID; 35824; 291.
DR ComplexPortal; CPX-465; DOM34-HBS1 ribosome dissociation complex.
DR DIP; DIP-7520N; -.
DR IntAct; P33309; 15.
DR MINT; P33309; -.
DR STRING; 4932.YNL001W; -.
DR MaxQB; P33309; -.
DR PaxDb; P33309; -.
DR PRIDE; P33309; -.
DR EnsemblFungi; YNL001W_mRNA; YNL001W; YNL001W.
DR GeneID; 855731; -.
DR KEGG; sce:YNL001W; -.
DR SGD; S000004946; DOM34.
DR VEuPathDB; FungiDB:YNL001W; -.
DR eggNOG; KOG2869; Eukaryota.
DR GeneTree; ENSGT00390000016326; -.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; P33309; -.
DR OMA; PAFYAKT; -.
DR BioCyc; YEAST:G3O-33043-MON; -.
DR EvolutionaryTrace; P33309; -.
DR PRO; PR:P33309; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P33309; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:SGD.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IDA:ComplexPortal.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:ComplexPortal.
DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:ComplexPortal.
DR GO; GO:0032790; P:ribosome disassembly; IDA:SGD.
DR GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR Gene3D; 2.30.30.870; -; 1.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR038069; Pelota/DOM34_N.
DR InterPro; IPR004405; Transl-rel_pelota.
DR PANTHER; PTHR10853; PTHR10853; 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; SSF159065; SSF159065; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Endonuclease;
KW Hydrolase; Meiosis; Metal-binding; Mitosis; Nuclease; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..386
FT /note="Protein DOM34"
FT /id="PRO_0000143191"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:2VGN"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2VGN"
FT TURN 136..140
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:2VGN"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2VGN"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2VGM"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:2VGN"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:2VGN"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:2VGN"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2VGN"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:2VGN"
SQ SEQUENCE 386 AA; 44058 MW; 4E8B7D9BBCD60888 CRC64;
MKVISLKKDS FNKGGAVITL LPEDKEDLFT VYQIVDKDDE LIFKKKFTSK LDEAGKKKST
DLVKLKIKVI SEDFDMKDEY LKYKGVTVTD ESGASNVDIP VGKYLSFTLD YVYPFTIIKQ
NFNKFMQKLL NEACNIEYKS DTAAVVLQEG IAHVCLVTSS STILKQKIEY SMPKKKRTTD
VLKFDEKTEK FYKAIYSAMK KDLNFDKLKT IILCSPGFYA KILMDKIFQY AEEEHNKKIL
DNKGMFFIAH CSTGYLQGIN EVLKNPLYAS KLQDTKYSKE IMVMDEFLLH LNKDDDKAWY
GEKEVVKAAE YGAISYLLLT DKVLHSDNIA QREEYLKLMD SVESNGGKAL VLSTLHSLGE
ELDQLTGIAC ILKYPLPDLD EDDGEE
