MTAL2_YEAST
ID MTAL2_YEAST Reviewed; 210 AA.
AC P0CY08; D6VQV2; P01367; P01368; Q6B2C0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Mating-type protein ALPHA2;
DE Short=MATalpha2 protein;
DE AltName: Full=Alpha-2 repressor;
GN Name=MATALPHA2; Synonyms=ALPHA-2, MAT2A, MATAL2; OrderedLocusNames=YCR039C;
GN ORFNames=YCR39C;
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].
RX PubMed=7021055; DOI=10.1101/sqb.1981.045.01.113;
RA Nasmyth K.A., Tatchell K., Hall B.D., Astell C., Smith M.;
RT "Physical analysis of mating-type loci in Saccharomyces cerevisiae.";
RL Cold Spring Harb. Symp. Quant. Biol. 45:961-981(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1789011; DOI=10.1002/yea.320070815;
RA Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C.,
RA Soustelle C.;
RT "The MAT locus revisited within a 9.8 kb fragment of chromosome III
RT containing BUD5 and two new open reading frames.";
RL Yeast 7:881-888(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [6]
RP DNA-BINDING SPECIFICITY.
RX PubMed=3893743; DOI=10.1016/s0092-8674(85)80119-7;
RA Johnson A.D., Herskowitz I.;
RT "A repressor (MAT alpha 2 Product) and its operator control expression of a
RT set of cell type specific genes in yeast.";
RL Cell 42:237-247(1985).
RN [7]
RP MUTAGENESIS BY DOMAIN DELETION.
RX PubMed=2887035; DOI=10.1126/science.2887035;
RA Hall M.N., Johnson A.D.;
RT "Homeo domain of the yeast repressor alpha 2 is a sequence-specific DNA-
RT binding domain but is not sufficient for repression.";
RL Science 237:1007-1012(1987).
RN [8]
RP DOMAINS, AND DIMERIZATION.
RX PubMed=3061876; DOI=10.1101/gad.2.7.807;
RA Sauer R.T., Smith D.L., Johnson A.D.;
RT "Flexibility of the yeast alpha 2 repressor enables it to occupy the ends
RT of its operator, leaving the center free.";
RL Genes Dev. 2:807-816(1988).
RN [9]
RP MUTAGENESIS OF LEU-196.
RX PubMed=2851482; DOI=10.1093/genetics/120.1.75;
RA Strathern J., Shafer B., Hicks J., McGill C.;
RT "a/Alpha-specific repression by MAT alpha 2.";
RL Genetics 120:75-81(1988).
RN [10]
RP PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.
RX PubMed=20110468; DOI=10.1126/science.1183147;
RA Hwang C.S., Shemorry A., Varshavsky A.;
RT "N-terminal acetylation of cellular proteins creates specific degradation
RT signals.";
RL Science 327:973-977(2010).
RN [11]
RP SIMILARITY TO HOMEOBOX PROTEINS.
RX PubMed=6429549; DOI=10.1038/310070a0;
RA Shepherd J.C.W., McGinnis W., Carrasco A.E., De Robertis E.M.,
RA Gehring W.J.;
RT "Fly and frog homoeo domains show homologies with yeast mating type
RT regulatory proteins.";
RL Nature 310:70-71(1984).
RN [12]
RP INTERACTION WITH TUP1, AND MUTAGENESIS OF ILE-4; LEU-9; LEU-10 AND GLU-71.
RX PubMed=7995523; DOI=10.1101/gad.8.23.2857;
RA Komachi K., Redd M.J., Johnson A.D.;
RT "The WD repeats of Tup1 interact with the homeo domain protein alpha 2.";
RL Genes Dev. 8:2857-2867(1994).
RN [13]
RP FUNCTION IN MATING-TYPE REGULATION.
RX PubMed=8664541; DOI=10.1016/0959-437x(95)80022-0;
RA Johnson A.D.;
RT "Molecular mechanisms of cell-type determination in budding yeast.";
RL Curr. Opin. Genet. Dev. 5:552-558(1995).
RN [14]
RP INTERACTION WITH SSN6.
RX PubMed=7498787; DOI=10.1101/gad.9.23.2903;
RA Smith R.L., Redd M.J., Johnson A.D.;
RT "The tetratricopeptide repeats of Ssn6 interact with the homeo domain of
RT alpha 2.";
RL Genes Dev. 9:2903-2910(1995).
RN [15]
RP INTERACTION WITH MCM1, AND MUTAGENESIS OF 114-LEU--THR-120.
RX PubMed=8628280; DOI=10.1128/mcb.16.5.2135;
RA Mead J., Zhong H., Acton T.B., Vershon A.K.;
RT "The yeast alpha2 and Mcm1 proteins interact through a region similar to a
RT motif found in homeodomain proteins of higher eukaryotes.";
RL Mol. Cell. Biol. 16:2135-2143(1996).
RN [16]
RP INTERACTION WITH SSN6, AND MUTAGENESIS OF ARG-173.
RX PubMed=10759558; DOI=10.1073/pnas.070506797;
RA Smith R.L., Johnson A.D.;
RT "A sequence resembling a peroxisomal targeting sequence directs the
RT interaction between the tetratricopeptide repeats of Ssn6 and the
RT homeodomain of alpha 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF HOMEOBOX.
RX PubMed=1682054; DOI=10.1016/0092-8674(91)90526-5;
RA Wolberger C., Vershon A.K., Liu B., Johnson A.D., Pabo C.O.;
RT "Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a
RT general model for homeodomain-DNA interactions.";
RL Cell 67:517-528(1991).
RN [18]
RP STRUCTURE BY NMR OF HOMEOBOX.
RX PubMed=1673952; DOI=10.1101/gad.5.5.764;
RA Phillips C.L., Vershon A.K., Johnson A.D., Dahlquist F.W.;
RT "Secondary structure of the homeo domain of yeast alpha 2 repressor
RT determined by NMR spectroscopy.";
RL Genes Dev. 5:764-772(1991).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1, AND
RP MUTAGENESIS OF ILE-192; LEU-196; LEU-199 AND LEU-200.
RX PubMed=7569974; DOI=10.1126/science.270.5234.262;
RA Li T., Stark M.R., Johnson A.D., Wolberger C.;
RT "Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound
RT to DNA.";
RL Science 270:262-269(1995).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH MCM1.
RX PubMed=9490409; DOI=10.1038/35563;
RA Tan S., Richmond T.J.;
RT "Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex.";
RL Nature 391:660-666(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1.
RX PubMed=9838003; DOI=10.1093/nar/26.24.5707;
RA Li T., Jin Y., Vershon A.K., Wolberger C.;
RT "Crystal structure of the MATa1/MATalpha2 homeodomain heterodimer in
RT complex with DNA containing an A-tract.";
RL Nucleic Acids Res. 26:5707-5718(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOMEOBOX.
RX PubMed=12466549; DOI=10.1093/nar/gkf661;
RA Aishima J., Gitti R.K., Noah J.E., Gan H.H., Schlick T., Wolberger C.;
RT "A Hoogsteen base pair embedded in undistorted B-DNA.";
RL Nucleic Acids Res. 30:5244-5252(2002).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1, AND
RP MUTAGENESIS OF SER-181; ASN-182 AND ARG-185.
RX PubMed=12121651; DOI=10.1016/s0969-2126(02)00790-6;
RA Ke A., Mathias J.R., Vershon A.K., Wolberger C.;
RT "Structural and thermodynamic characterization of the DNA binding
RT properties of a triple alanine mutant of MATalpha2.";
RL Structure 10:961-971(2002).
CC -!- FUNCTION: Mating type proteins are sequence specific DNA-binding
CC proteins that act as master switches in yeast differentiation by
CC controlling gene expression in a cell type-specific fashion.
CC Transcriptional corepressor that binds cooperatively with MCM1 to a 31-
CC basepair DNA sequence termed the a-specific gene (asg) operator, to
CC repress the transcription of a-cell-specific genes. Additionally, in
CC a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-
CC basepair DNA sequence termed the haploid-specific gene (hsg) operator,
CC to repress transcription of haploid-specific genes and of MATALPHA1.
CC {ECO:0000269|PubMed:8664541}.
CC -!- SUBUNIT: Binds DNA with a high specificity as a heterotetramer
CC consisting of an ALPHA2 dimer and an MCM1 dimer. Also binds DNA with a
CC high specificity as a heterodimer of A1 and ALPHA2 in a/alpha diploid
CC cells. Interacts with the general transcription repressor complex
CC SSN6/TUP1. {ECO:0000269|PubMed:10759558, ECO:0000269|PubMed:12121651,
CC ECO:0000269|PubMed:7498787, ECO:0000269|PubMed:7569974,
CC ECO:0000269|PubMed:7995523, ECO:0000269|PubMed:8628280,
CC ECO:0000269|PubMed:9490409, ECO:0000269|PubMed:9838003}.
CC -!- INTERACTION:
CC P0CY08; P11746: MCM1; NbExp=2; IntAct=EBI-10443, EBI-10528;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Only present in alpha-cells and in a/alpha diploid
CC cells.
CC -!- DOMAIN: The N-terminal domain is required for the interaction with the
CC WD repeats of TUP1 and for dimerization. {ECO:0000269|PubMed:3061876}.
CC -!- DOMAIN: The homeobox domain binds to DNA and interacts with the TPR
CC repeats of SSN6. {ECO:0000269|PubMed:3061876}.
CC -!- DOMAIN: The unstructured, flexible linker domain contains eight
CC residues (Leu-114 to Gln-121), which, in the presence of MCM1, adopt a
CC beta-fold and mediate the cooperative interaction to MCM1.
CC {ECO:0000269|PubMed:3061876}.
CC -!- DOMAIN: The C-terminal tail domain is disordered in the monomer, even
CC when bound to DNA. In the ternary complex with A1 and DNA, 16 residues
CC (Ile-190 to Leu-205) of the C-terminal tail undergo a conformational
CC change, becoming ordered and contacting the A1 homeodomain.
CC {ECO:0000269|PubMed:3061876}.
CC -!- MISCELLANEOUS: There are three genetic loci for mating type genes in
CC S.cerevisiae. MAT is the expression locus that determines the mating
CC type of the cell, whereas HML (containing HMLALPHA1 and HMLALPHA2) and
CC HMR (containing HMRA1 and HMRA2) represent silenced repositories of
CC mating type information. The mating type is determined by the MAT
CC locus, which contains either a copy of HML or of HMR. Diploid cells are
CC usually heterozygous for the MAT locus.
CC -!- SIMILARITY: Belongs to the TALE/M-ATYP homeobox family. {ECO:0000305}.
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DR EMBL; L00060; AAA34762.1; -; Genomic_DNA.
DR EMBL; X63853; CAA45335.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42306.1; -; Genomic_DNA.
DR EMBL; AY692810; AAT92829.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07518.1; -; Genomic_DNA.
DR PIR; S19398; JFBYA2.
DR RefSeq; NP_009866.1; NM_001178708.1.
DR RefSeq; NP_009868.3; NM_001178753.1.
DR PDB; 1AKH; X-ray; 2.50 A; B=128-210.
DR PDB; 1APL; X-ray; 2.70 A; C/D=128-210.
DR PDB; 1K61; X-ray; 2.10 A; A/B/C/D=132-191.
DR PDB; 1LE8; X-ray; 2.30 A; B=128-210.
DR PDB; 1MNM; X-ray; 2.25 A; C/D=103-189.
DR PDB; 1YRN; X-ray; 2.50 A; B=128-210.
DR PDBsum; 1AKH; -.
DR PDBsum; 1APL; -.
DR PDBsum; 1K61; -.
DR PDBsum; 1LE8; -.
DR PDBsum; 1MNM; -.
DR PDBsum; 1YRN; -.
DR AlphaFoldDB; P0CY08; -.
DR SMR; P0CY08; -.
DR BioGRID; 30922; 7.
DR BioGRID; 31022; 22.
DR ComplexPortal; CPX-684; Mating-type MATalpha2-MATa1 complex.
DR ComplexPortal; CPX-692; Mating-type MATalpha2-MCM1 complex.
DR IntAct; P0CY08; 3.
DR iPTMnet; P0CY08; -.
DR MaxQB; P0CY08; -.
DR EnsemblFungi; YCL067C_mRNA; YCL067C; YCL067C.
DR EnsemblFungi; YCR039C_mRNA; YCR039C; YCR039C.
DR GeneID; 850292; -.
DR GeneID; 850406; -.
DR KEGG; sce:YCL067C; -.
DR KEGG; sce:YCR039C; -.
DR SGD; S000000635; MATALPHA2.
DR VEuPathDB; FungiDB:YCL067C; -.
DR VEuPathDB; FungiDB:YCR039C; -.
DR HOGENOM; CLU_091806_1_0_1; -.
DR InParanoid; P0CY08; -.
DR BioCyc; YEAST:G3O-29351-MON; -.
DR EvolutionaryTrace; P0CY08; -.
DR PRO; PR:P0CY08; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P0CY08; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:ComplexPortal.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR DisProt; DP02806; -.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA-binding;
KW Homeobox; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..210
FT /note="Mating-type protein ALPHA2"
FT /id="PRO_0000049186"
FT DNA_BIND 129..191
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..102
FT /note="N-terminal domain"
FT REGION 103..128
FT /note="Flexible linker"
FT REGION 190..210
FT /note="C-terminal tail"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:20110468"
FT MUTAGEN 4
FT /note="I->T: Reduces the ability of ALPHA2 to repress
FT transcription, but binds normally to DNA and MCM1."
FT /evidence="ECO:0000269|PubMed:7995523"
FT MUTAGEN 9
FT /note="L->F: Reduces the ability of ALPHA2 to repress
FT transcription, but binds normally to DNA and MCM1."
FT /evidence="ECO:0000269|PubMed:7995523"
FT MUTAGEN 10
FT /note="L->S: Reduces the ability of ALPHA2 to repress
FT transcription, but binds normally to DNA and MCM1. Disrupts
FT interaction with TUP1."
FT /evidence="ECO:0000269|PubMed:7995523"
FT MUTAGEN 71
FT /note="E->K: Reduces the ability of alpha2 to repress
FT transcription, but binds normally to DNA and MCM1."
FT /evidence="ECO:0000269|PubMed:7995523"
FT MUTAGEN 114
FT /note="L->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 115
FT /note="V->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 116
FT /note="F->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 117
FT /note="N->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 118
FT /note="V->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 119
FT /note="V->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 120
FT /note="T->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes."
FT /evidence="ECO:0000269|PubMed:2887035"
FT MUTAGEN 173
FT /note="R->A: Reduces the ability of ALPHA2/MCM1 to repress
FT a-specific genes. Disrupts interaction with SSN6."
FT /evidence="ECO:0000269|PubMed:10759558"
FT MUTAGEN 181
FT /note="S->A: In ALPHA2-3A; defective in binding DNA alone
FT or in complex with MCM1, but binds DNA normally in complex
FT with A1; when associated with A-182 and A-185."
FT /evidence="ECO:0000269|PubMed:12121651"
FT MUTAGEN 182
FT /note="N->A: In ALPHA2-3A; defective in binding DNA alone
FT or in complex with MCM1, but binds DNA normally in complex
FT with A1; when associated with A-181 and A-185."
FT /evidence="ECO:0000269|PubMed:12121651"
FT MUTAGEN 185
FT /note="R->A: In ALPHA2-3A; defective in binding DNA alone
FT or in complex with MCM1, but binds DNA normally in complex
FT with A1; when associated with A-181 and A-182."
FT /evidence="ECO:0000269|PubMed:12121651"
FT MUTAGEN 192
FT /note="I->A: Disrupts the ability of A1/ALPHA2 to repress
FT haploid-specific genes."
FT /evidence="ECO:0000269|PubMed:7569974"
FT MUTAGEN 196
FT /note="L->A,S: Disrupts the ability of A1/ALPHA2 to repress
FT haploid-specific genes."
FT /evidence="ECO:0000269|PubMed:2851482,
FT ECO:0000269|PubMed:7569974"
FT MUTAGEN 199
FT /note="L->A: Disrupts the ability of A1/ALPHA2 to repress
FT haploid-specific genes."
FT /evidence="ECO:0000269|PubMed:7569974"
FT MUTAGEN 200
FT /note="L->A: Disrupts the ability of A1/ALPHA2 to repress
FT haploid-specific genes."
FT /evidence="ECO:0000269|PubMed:7569974"
FT CONFLICT 56
FT /note="G -> L (in Ref. 1; AAA34762)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="K -> KK (in Ref. 1; AAA34762)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="N -> S (in Ref. 5; AAT92829)"
FT /evidence="ECO:0000305"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1MNM"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1MNM"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1K61"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1K61"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1K61"
FT HELIX 173..188
FT /evidence="ECO:0007829|PDB:1K61"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:1LE8"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1LE8"
SQ SEQUENCE 210 AA; 24282 MW; 30CD6A486D7D76CE CRC64;
MNKIPIKDLL NPQITDEFKS SILDINKKLF SICCNLPKLP ESVTTEEEVE LRDILGFLSR
ANKNRKISDE EKKLLQTTSQ LTTTITVLLK EMRSIENDRS NYQLTQKNKS ADGLVFNVVT
QDMINKSTKP YRGHRFTKEN VRILESWFAK NIENPYLDTK GLENLMKNTS LSRIQIKNWV
SNRRRKEKTI TIAPELADLL SGEPLAKKKE
