ADA2_CANAL
ID ADA2_CANAL Reviewed; 445 AA.
AC Q59WH0; A0A1D8PEY3;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcriptional adapter 2;
GN Name=ADA2; OrderedLocusNames=CAALFM_C110860CA;
GN ORFNames=CaO19.2331, CaO19.9867;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=16552442; DOI=10.1371/journal.ppat.0020021;
RA Bruno V.M., Kalachikov S., Subaran R., Nobile C.J., Kyratsous C.,
RA Mitchell A.P.;
RT "Control of the C. albicans cell wall damage response by transcriptional
RT regulator Cas5.";
RL PLoS Pathog. 2:E21-E21(2006).
RN [5]
RP FUNCTION.
RX PubMed=19666778; DOI=10.1128/ec.00163-09;
RA Pukkila-Worley R., Peleg A.Y., Tampakakis E., Mylonakis E.;
RT "Candida albicans hyphal formation and virulence assessed using a
RT Caenorhabditis elegans infection model.";
RL Eukaryot. Cell 8:1750-1758(2009).
RN [6]
RP FUNCTION.
RX PubMed=19279142; DOI=10.1091/mbc.e08-11-1093;
RA Sellam A., Askew C., Epp E., Lavoie H., Whiteway M., Nantel A.;
RT "Genome-wide mapping of the coactivator Ada2p yields insight into the
RT functional roles of SAGA/ADA complex in Candida albicans.";
RL Mol. Biol. Cell 20:2389-2400(2009).
RN [7]
RP FUNCTION.
RX PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT "Portrait of Candida albicans adherence regulators.";
RL PLoS Pathog. 8:E1002525-E1002525(2012).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation of
CC approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. SAGA acetylates
CC nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac
CC and H3K23ac). SAGA interacts with DNA via upstream activating sequences
CC (UASs). SALSA, an altered form of SAGA, may be involved in positive
CC transcriptional regulation. ADA preferentially acetylates nucleosomal
CC histones H3 (to form H3K14ac and H3K18ac) and H2B. Required for
CC expression of many CAS5-dependent genes. Plays a key role in cell wall
CC integrity, cell adhesion, hyphal development and pathogenesis.
CC {ECO:0000269|PubMed:16552442, ECO:0000269|PubMed:19279142,
CC ECO:0000269|PubMed:19666778, ECO:0000269|PubMed:22359502}.
CC -!- SUBUNIT: Component of SAGA complex, SALSA complex, and ADA complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017623; AOW26713.1; -; Genomic_DNA.
DR RefSeq; XP_713936.2; XM_708843.2.
DR AlphaFoldDB; Q59WH0; -.
DR SMR; Q59WH0; -.
DR BioGRID; 1227479; 1.
DR STRING; 237561.Q59WH0; -.
DR PRIDE; Q59WH0; -.
DR GeneID; 3644450; -.
DR KEGG; cal:CAALFM_C110860CA; -.
DR CGD; CAL0000192402; ADA2.
DR VEuPathDB; FungiDB:C1_10860C_A; -.
DR eggNOG; KOG0457; Eukaryota.
DR HOGENOM; CLU_018273_3_0_1; -.
DR InParanoid; Q59WH0; -.
DR OMA; EFETEYF; -.
DR OrthoDB; 812864at2759; -.
DR PRO; PR:Q59WH0; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IEA:EnsemblFungi.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:CGD.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0044114; P:development of symbiont in host; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0016573; P:histone acetylation; IMP:CGD.
DR GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CGD.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Cell wall biogenesis/degradation; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Virulence;
KW Zinc; Zinc-finger.
FT CHAIN 1..445
FT /note="Transcriptional adapter 2"
FT /id="PRO_0000422794"
FT DOMAIN 63..115
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 357..445
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 5..61
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 319..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 445 AA; 51110 MW; 906898F5F06FF2F2 CRC64;
MDSRTKLFHC DVCSSDCTNR IRIQCAICTD YDLCVPCFAA GLTTGDHKPW HDYQIIEQNT
YPIFDRDWGA DEELLLIQGC ETSGLGNWAD IADHIGNRSK EEVAEHYFKI YLESKDYPLP
EMNKDFTDVS PLQFLEERKE RLEKRKNIPL PPPRGKPVAS VPLCHEIQGY MPGRLEFDHE
AENEAEIPIK DMVFDPEDSA NDIDLKLTIL DIYNSRLTTR AERKRVMILN HLLDYRKNIG
SDKRKSKEEK DLLKKINAFI RILTPEDFES FSRDLLTELK CRMKIQQLQT WRRNGITTLE
DGAKFEKDKV IRAAHYQRMG NGTGSGRHSQ TPGLTNGNSF NGNGHRNKFS PQPEFRSKST
TARAPLDISH AADFELLSAE EKQLCATLRI LPKPYLAIKN QLMREAVKNN GVLKKKDARQ
ALKIDVNKAS KIYEFFVHMG WCSQG
