ADA2_SCHPO
ID ADA2_SCHPO Reviewed; 437 AA.
AC Q9P7J7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transcriptional adapter 2;
GN Name=ada2 {ECO:0000250|UniProtKB:Q02336}; ORFNames=SPCC24B10.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB76217.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18199689; DOI=10.1091/mbc.e07-04-0377;
RA Hirota K., Mizuno K.I., Shibata T., Ohta K.;
RT "Distinct chromatin modulators regulate the formation of accessible and
RT repressive chromatin at the fission yeast recombination hotspot ade6-M26.";
RL Mol. Biol. Cell 19:1162-1173(2008).
RN [4]
RP STRUCTURE BY NMR OF 62-112.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SANT domain of fission yeast SPCC24B10.08c
RT protein.";
RL Submitted (OCT-2007) to the PDB data bank.
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. At
CC the promoters, SAGA is required for recruitment of the basal
CC transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction and promoter selectivity, interaction with transcription
CC activators, and chromatin modification through histone acetylation
CC (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC altered form of SAGA, may be involved in positive transcriptional
CC regulation. SLIK is proposed to have partly overlapping functions with
CC SAGA. It preferentially acetylates methylated histone H3. ADA
CC preferentially acetylates nucleosomal histones H3 (to form H3K14ac and
CC H3K18ac) and H2B (By similarity). Required for full activation of
CC chromatin alteration and meiotic recombination at meiotic recombination
CC hot spot ade6-M26. Also required for the regulation of transcription
CC and chromatin structure around ade6-M26 in response to osmotic stress.
CC Needed for hyperacetylation of histone H3 around ade6-M26.
CC {ECO:0000250|UniProtKB:Q02336, ECO:0000269|PubMed:18199689}.
CC -!- SUBUNIT: Component of the SAGA, SALSA, SLIK and ADA complexes.
CC {ECO:0000250|UniProtKB:Q02336}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Cells are sensitive to replication stress
CC hydroxyurea (HU) and also exhibits weak sensitivity to ultraviolet (UV)
CC and methylmethane sulfonate (MMS). {ECO:0000269|PubMed:18199689}.
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; CU329672; CAB76217.1; -; Genomic_DNA.
DR PIR; T50415; T50415.
DR RefSeq; NP_588011.1; NM_001023002.2.
DR PDB; 2ELK; NMR; -; A=62-112.
DR PDBsum; 2ELK; -.
DR AlphaFoldDB; Q9P7J7; -.
DR BMRB; Q9P7J7; -.
DR SMR; Q9P7J7; -.
DR BioGRID; 275745; 13.
DR IntAct; Q9P7J7; 2.
DR MINT; Q9P7J7; -.
DR STRING; 4896.SPCC24B10.08c.1; -.
DR MaxQB; Q9P7J7; -.
DR PaxDb; Q9P7J7; -.
DR EnsemblFungi; SPCC24B10.08c.1; SPCC24B10.08c.1:pep; SPCC24B10.08c.
DR GeneID; 2539174; -.
DR KEGG; spo:SPCC24B10.08c; -.
DR PomBase; SPCC24B10.08c; ada2.
DR VEuPathDB; FungiDB:SPCC24B10.08c; -.
DR eggNOG; KOG0457; Eukaryota.
DR HOGENOM; CLU_018273_3_0_1; -.
DR InParanoid; Q9P7J7; -.
DR OMA; EFETEYF; -.
DR PhylomeDB; Q9P7J7; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR EvolutionaryTrace; Q9P7J7; -.
DR PRO; PR:Q9P7J7; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA recombination; Meiosis;
KW Metal-binding; Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..437
FT /note="Transcriptional adapter 2"
FT /id="PRO_0000324663"
FT DOMAIN 61..114
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 347..437
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 3..59
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2ELK"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:2ELK"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:2ELK"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:2ELK"
SQ SEQUENCE 437 AA; 50478 MW; 1FD6F81E6E6A0B9B CRC64;
MPPQKYHCNV CAQDITRSIH IRCVECVDFD LCIPCFTSGA SLGTHHPSHP YRIIETNSYP
IFDENWGADE ELLLIDACET LGLGNWADIA DYVGNARTKE ECRDHYLKTY IESDCYPLAS
VELPGPVDRI AFAARKRARI EAFQPPPIIP QKPLASTPQC HEIQGYMPGR LEFDQEYMNE
AELPIKDMNF DDDLHESAKH EMQLKLTMLN IYNSRLTRRA VRKQTIFNHN LLDYRRLQAN
EKRMSKEERN LLNKTKAFAR LLTGPDYQKF VNSYHEQITL KKQISDLQEW RQMGLTTLEQ
GHKYERDKTQ KFLLSKASAS YDKQLRHVKS FNQTTSAPFQ VRDIQKIVPR KPATPTMFSA
SADRQLLSED EQALCSKLQI FPKPFLALKF ALISASLTSK KPFQKTDAVN LFKHLDANKV
EQVYDFFHNA RWIGAPT
