EFG1P_YEAST
ID EFG1P_YEAST Reviewed; 233 AA.
AC Q3E705; D6VV49; P53328;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=rRNA-processing protein EFG1;
DE AltName: Full=Exit from G1 protein 1;
GN Name=EFG1; OrderedLocusNames=YGR271C-A; ORFNames=G9368, YGR272C;
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=ATCC 204508 / S288c;
RX PubMed=9133740;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<365::aid-yea78>3.0.co;2-f;
RA Ruzzi M., Marconi A., Saliola M., Fabiani L., Montebove F., Frontali L.;
RT "The sequence of a 8 kb segment on the right arm of yeast chromosome VII
RT identifies four new open reading frames and the genes for yTAFII145.";
RL Yeast 13:365-368(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION IN RRNA PROCESSING.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [6]
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 [7]
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 [8]
RP FUNCTION, AND IDENTIFICATION OF FRAMESHIFT.
RX PubMed=16510898; DOI=10.1101/gr.4355406;
RA Kastenmayer J.P., Ni L., Chu A., Kitchen L.E., Au W.-C., Yang H.,
RA Carter C.D., Wheeler D., Davis R.W., Boeke J.D., Snyder M.A., Basrai M.A.;
RT "Functional genomics of genes with small open reading frames (sORFs) in S.
RT cerevisiae.";
RL Genome Res. 16:365-373(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC -!- FUNCTION: Involved in rRNA processing. Required growth at elevated
CC temperatures, resistance to hydroxyurea and for cell cycle progression.
CC {ECO:0000269|PubMed:12837249, ECO:0000269|PubMed:16510898}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EFG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58894.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA97302.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X84098; CAA58894.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z73057; CAA97302.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY558513; AAS56839.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08360.1; -; Genomic_DNA.
DR PIR; S64605; S64605.
DR RefSeq; NP_076891.4; NM_001184474.3.
DR AlphaFoldDB; Q3E705; -.
DR SMR; Q3E705; -.
DR BioGRID; 33521; 89.
DR IntAct; Q3E705; 1.
DR MINT; Q3E705; -.
DR STRING; 4932.YGR271C-A; -.
DR MaxQB; Q3E705; -.
DR PaxDb; Q3E705; -.
DR PRIDE; Q3E705; -.
DR EnsemblFungi; YGR271C-A_mRNA; YGR271C-A; YGR271C-A.
DR GeneID; 853188; -.
DR KEGG; sce:YGR271C-A; -.
DR SGD; S000007608; EFG1.
DR VEuPathDB; FungiDB:YGR271C-A; -.
DR eggNOG; KOG4484; Eukaryota.
DR HOGENOM; CLU_066912_2_0_1; -.
DR InParanoid; Q3E705; -.
DR OMA; HMIRFFE; -.
DR BioCyc; YEAST:G3O-31007-MON; -.
DR ChiTaRS; EFG1; yeast.
DR PRO; PR:Q3E705; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q3E705; protein.
DR GO; GO:0030685; C:nucleolar preribosome; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0071027; P:nuclear RNA surveillance; IMP:SGD.
DR GO; GO:0000321; P:re-entry into mitotic cell cycle after pheromone arrest; IMP:SGD.
DR InterPro; IPR019310; Efg1.
DR Pfam; PF10153; Efg1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; rRNA processing.
FT CHAIN 1..233
FT /note="rRNA-processing protein EFG1"
FT /id="PRO_0000245390"
FT REGION 194..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..109
FT /evidence="ECO:0000255"
FT COMPBIAS 194..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 152
FT /note="G -> A (in Ref. 4; AAS56839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 27121 MW; 5DB64BB999DA3510 CRC64;
MAKLQRKRSK ALGSSLEMSQ IMDAGTNKIK RRIRDLERLL KKKKDILPST VIIEKERNLQ
ALRLELQNNE LKNKIKANAK KYHMVRFFEK KKALRKYNRL LKKIKESGAD DKDLQQKLRA
TKIELCYVIN FPKTEKYIAL YPNDTPSTDP KGVELTNLRR EQFLKLVAER MDANTLNVSF
EEILKGKKLD EDSIGLTLSP DKDHEDGSQV SPTQDRKELD QVVGEDEKDD FFE
