SEF1_YEAST
ID SEF1_YEAST Reviewed; 1148 AA.
AC P34228; D6VPT5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Putative transcription factor SEF1;
DE AltName: Full=Suppressor of essential function protein 1;
DE AltName: Full=Suppressor protein SEF1;
GN Name=SEF1; OrderedLocusNames=YBL066C; ORFNames=YBL0501, YBL0526;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-789.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [4]
RP FUNCTION.
RX PubMed=9483797;
RX DOI=10.1002/(sici)1097-0061(19980115)14:1<77::aid-yea201>3.0.co;2-p;
RA Groom K.R., Heyman H.C., Steffen M.C., Hawkins L., Martin N.C.;
RT "Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue
RT bypass the unknown essential function, but not the mitochondrial RNase P
RT function, of the S. cerevisiae RPM2 gene.";
RL Yeast 14:77-87(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-806, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Putative transcription factor that seems to be involved in
CC the sporulation process. Suppresses the lethal phenotype of RPM2
CC deletion. {ECO:0000269|PubMed:9483797}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA84885.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; Z35827; CAA84885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z23261; CAA80783.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07055.1; -; Genomic_DNA.
DR PIR; S45801; S45801.
DR RefSeq; NP_009487.2; NM_001178306.1.
DR AlphaFoldDB; P34228; -.
DR BioGRID; 32634; 118.
DR DIP; DIP-2559N; -.
DR IntAct; P34228; 9.
DR MINT; P34228; -.
DR STRING; 4932.YBL066C; -.
DR iPTMnet; P34228; -.
DR MaxQB; P34228; -.
DR PaxDb; P34228; -.
DR PRIDE; P34228; -.
DR EnsemblFungi; YBL066C_mRNA; YBL066C; YBL066C.
DR GeneID; 852214; -.
DR KEGG; sce:YBL066C; -.
DR SGD; S000000162; SEF1.
DR VEuPathDB; FungiDB:YBL066C; -.
DR eggNOG; ENOG502QR4T; Eukaryota.
DR GeneTree; ENSGT00940000176683; -.
DR HOGENOM; CLU_010150_0_0_1; -.
DR OMA; LVWCVHE; -.
DR BioCyc; YEAST:G3O-28962-MON; -.
DR PRO; PR:P34228; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P34228; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Sporulation; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..1148
FT /note="Putative transcription factor SEF1"
FT /id="PRO_0000114977"
FT DNA_BIND 57..87
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1148 AA; 127992 MW; 41553B72ED667645 CRC64;
MVKDNRDSDQ DQDFSSAHMK RQPEQQQLQQ HQFPSKKQRI SHHDDSHQIN HRPVTSCTHC
RQHKIKCDAS QNFPHPCSRC EKIGLHCEIN PQFRPKKGSQ LQLLRQDVDE IKSKLDTLLA
NDSVFVHLLQ QIPMGNSLLN KLNLHPTPTP GTIIPNPDSS PSSGSPTSSA AQRDSKVSVQ
TYLSREPQLL QANQGSNTNK FKANNEASSH MTLRASSLAQ DSKGLVATEP NKLPPLLNDS
ALPNNSKESL PPALQMAFYK NNSAGNTPNG PFSPIQKTYS PHTTSTTVTT TTNQPPFAAT
SHVATNNNAD RTKTPVVATT TTMPLLPSPH ANVDEFVLGD ISISIEKANR LHHIFVTRYL
PYFPIMYSNN ATELYSQSQL LFWTVMLTAC LSDPEPTMYC KLSSLIKQLA IETCWIRTPR
STHISQALLI LCIWPLPNQK VLDDCSYRFV GLAKSLSYQL GLHRGEFISE FTRTQTSMPN
AEKWRTRTWL GIFFAELCWA SILGLPPTSQ TDYLLEKALS CGDEESEEDN NDSIDNNNND
KRNKKDEPHV ESKYKLPGSF RRLLSLANFQ AKLSHIIGSS TSSPDGLLEP KYRAETLSIL
GKELDLLAKT LNFQSDDTVN IYFLYVKLTV CCFAFLPETP PTDQIPYVTE AYLTATKIVT
LLNNLLETHQ LIELPIYIRQ AATFSALILF KLQLTPLLPD KYFDSARQSV VTIHRLYRNQ
LTAWATSVEN DISRTASMLE KLNFVLIMHP EVFVEEDGII SRMRSHLTGS LFYDLVWCVH
EARRREMDPE YNKQALEKAA KKRKFSSNGI YNGTSSTGGI TDRKLYPLPL YNHISRDDFE
TVTKTTPSGT TVTTLVPTKN ALKQAEKLAK TNNGDSDGSI MEINGIPLSM LGETGSVKFQ
SLFANTSNSN DYNNNRTLLD ASNDISIPSN SIYPVASVPA SNNNPQSTKV DYYSNGPSVI
PDLSMKRSVS TPVNHFPASV PGLRNHPVGN LSNNVTLGID HPIPREHSNL QNVTMNYNNQ
FSNANAIGRS QSSMSHSRTP IASKSNNMTD LHSVVSDPGS SKSTAYPPLS LFSKSNDINS
NKTNQRFSTG TNTVTSSNFQ TIDNENNVKT PGNKLTDFFQ QQSAGWIEGN SSNDDFFGWF
DMNMEQGF
