Reviewed, UniProtKB/Swiss-Prot Q9P7J7 (ADA2_SCHPO)

Names and origin

Protein names

Recommended name:
    Transcriptional adapter 2

Gene names

Name:	ada2
ORF Names:	SPCC24B10.08c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B By similarity. Required for full activation of chromatin alteration and meiotic recombination at meiotic recombination hot spot ade6-M26. Also required for the regulation of transcription and chromatin structure around ade6-M26 in response to osmotic stress. Needed for hyperacetylation of histone H3 around ade6-M26. Ref.3 UniProtKB Q02336
Subunit structure	Component of the SAGA, SALSA, SLIK and ADA complexes By similarity. UniProtKB Q02336
Subcellular location	Nucleus.
Disruption phenotype	Cells are sensitive to replication stress hydroxyurea (HU) and also exhibits weak sensitivity to ultraviolet (UV) and methylmethane sulfonate (MMS). Ref.3
Sequence similarities	Contains 1 SANT domain. Contains 1 SWIRM domain. Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Biological process	DNA recombination Meiosis Stress response Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chromatin remodeling Inferred by curator. Source: GeneDB_SPombe histone acetylation Ref.3 Inferred from mutant phenotype. Source: UniProtKB reciprocal meiotic recombination Ref.3 Inferred from mutant phenotype. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW response to osmotic stress Ref.3 Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear chromatin Non-traceable author statement. Source: GeneDB_SPombe
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Transcriptional adapter 2

PRO_0000324663

Regions

Domain

61 – 114

54

SANT

Domain

347 – 437

91

SWIRM

Zinc finger

2 – 49

48

ZZ-type

Secondary structure

1

.

.

.

.

.

.

.

.

437

Helix Strand Turn

Details...

Helix

68 – 80

13

Turn

81 – 84

4

Helix

86 – 93

8

Helix

99 – 109

11

Sequences

	Sequence		Length	Mass (Da)
	Q9P7J7-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1FD6F81E6E6A0B9B	FASTA	437	50,478
	10 20 30 40 50 60 MPPQKYHCNV CAQDITRSIH IRCVECVDFD LCIPCFTSGA SLGTHHPSHP YRIIETNSYP 70 80 90 100 110 120 IFDENWGADE ELLLIDACET LGLGNWADIA DYVGNARTKE ECRDHYLKTY IESDCYPLAS 130 140 150 160 170 180 VELPGPVDRI AFAARKRARI EAFQPPPIIP QKPLASTPQC HEIQGYMPGR LEFDQEYMNE 190 200 210 220 230 240 AELPIKDMNF DDDLHESAKH EMQLKLTMLN IYNSRLTRRA VRKQTIFNHN LLDYRRLQAN 250 260 270 280 290 300 EKRMSKEERN LLNKTKAFAR LLTGPDYQKF VNSYHEQITL KKQISDLQEW RQMGLTTLEQ 310 320 330 340 350 360 GHKYERDKTQ KFLLSKASAS YDKQLRHVKS FNQTTSAPFQ VRDIQKIVPR KPATPTMFSA 370 380 390 400 410 420 SADRQLLSED EQALCSKLQI FPKPFLALKF ALISASLTSK KPFQKTDAVN LFKHLDANKV 430 EQVYDFFHNA RWIGAPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Distinct chromatin modulators regulate the formation of accessible and repressive chromatin at the fission yeast recombination hotspot ade6-M26." Hirota K., Mizuno K.I., Shibata T., Ohta K. Mol. Biol. Cell 19:1162-1173(2008) [PubMed: 18199689] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]	"Solution structure of the SANT domain of fission yeast SPCC24B10.08c protein." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 62-112.

Cross-references

Sequence databases

EMBLGenBankDDBJ

CU329672 Genomic DNA. Translation: CAB76217.1.

PIR

T50415.

RefSeq

NP_588011.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ELK	NMR	-	A	62-112	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9P7J7.

Genome annotation databases

GeneID

2539174.

GenomeReviews

Gene locus ada2 in contig CU329672_GR.

KEGG

spo:SPCC24B10.08c.

NMPDR

fig|4896.1.peg.349.

Organism-specific databases

GeneDB_Spombe

SPCC24B10.08c.

Phylogenomic databases

OMA

QILERRY

OrthoDB

EOG9FTXH2

Gene expression databases

ArrayExpress

Q9P7J7.

Family and domain databases

InterPro

IPR009057. Homeodomain-like.
IPR014778. Myb_DNA-bd.
IPR001005. SANT_DNA-bd.
IPR017884. SANT_eukarya.
IPR007526. SWIRM.
IPR016827. Transcriptional_adaptor_2.
IPR000433. Znf_ZZ.
[Graphical view]

Pfam

PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]

PIRSF

PIRSF025024. Transcriptional_adaptor_2. 1 hit.

SMART

SM00717. SANT. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

PROSITE

PS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ADA2_SCHPO

Accession

Primary (citable) accession number: Q9P7J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	October 1, 2000
Last modified:	November 24, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)