Q27198 (Q27198_TETTH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: HAT A1 EMBL AAB01099.1
Organism	Tetrahymena thermophila EMBL AAB01099.1
Taxonomic identifier	5911 [NCBI]
Taxonomic lineage	Eukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Hymenostomatida › Tetrahymenina › Tetrahymenidae › Tetrahymena

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Bromodomain SAAS SAAS001487
Technical term	3D-structure PDB 1PUA PDB 1Q2C PDB 1QSN PDB 1QSR PDB 5GCN PDB 1QST PDB 1M1D PDB 1PU9 PDB 1Q2D
Gene Ontology (GO)
Molecular function	N-acetyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	126 – 139	14	Coenzyme A binding PDB 1PUA PDB 1Q2C PDB 1QSN PDB 5GCN PDB 1PU9 PDB 1Q2D
	Region	164 – 171	8	Coenzyme A binding PDB 1Q2C PDB 5GCN

Sequences

	Sequence		Length	Mass (Da)
	Q27198 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E69C1C0C518DEEA1	FASTA	418	48,560
	10 20 30 40 50 60 MADQEKSAQD AQNAAPQETA FVGMNGEETG LGFATRDQGA KVEEDQGLLD FDILTNDGTH 70 80 90 100 110 120 RNMKLLIDLK NIFSRQLPKM PKEYIVKLVL DRHHESMVIL KNKQKVIGGI CFRQYKPQRF 130 140 150 160 170 180 AEVAFLAVTA NEQVRGYGTR LMNKFKDHMQ KQNIEYLLTY ADNFAIGYFK KQGFTKEHRM 190 200 210 220 230 240 PQEKWKGYIK DYDGGTLMEC YIHPYVDYGN ISQIIKRQKE LLIERIKKLS LNEKVFSGKE 250 260 270 280 290 300 YAALIQNSMD NEDPENPKVN PSDIPGVAFS GWEWKDYHEL KKSKERSFNL QCANVIENMK 310 320 330 340 350 360 RHKQSWPFLD PVNKDDVPDY YDVITDPIDI KAIEKKLQNN QYVDKDQFIK DVKRIFTNAK 370 380 390 400 410 IYNQPDTIYY KAAKELEDFV EPYLTKLKDT KESNTPSNNN SAHGSKKPLP VRKSIKKK

References

[1]	"Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation." Brownell J.E., Zhou J., Ranalli T., Kobayashi R., Edmondson D.G., Roth S.Y., Allis C.D. Cell 84:843-851(1996) [PubMed: 8601308] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A." Lin Y., Fletcher C.M., Zhou J., Allis C.D., Wagner G. Nature 400:86-89(1999) [PubMed: 10403255] [Abstract] Cited for: STRUCTURE BY NMR OF 47-210 IN COMPLEX WITH COENZYME A.
[3]	"Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide." Rojas J.R., Trievel R.C., Zhou J., Mo Y., Li X., Berger S.L., Allis C.D., Marmorstein R. Nature 401:93-98(1999) [PubMed: 10485713] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 49-208 IN COMPLEX WITH COENZYME A.
[4]	"Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor." Poux A.N., Cebrat M., Kim C.M., Cole P.A., Marmorstein R. Proc. Natl. Acad. Sci. U.S.A. 99:14065-14070(2002) [PubMed: 12391296] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 48-209.
[5]	"Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase." Clements A., Poux A.N., Lo W.-S., Pillus L., Berger S.L., Marmorstein R. Mol. Cell 12:461-473(2003) [PubMed: 14536085] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 49-209 IN COMPLEX WITH COENZYME A.
[6]	"Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates." Poux A.N., Marmorstein R. Biochemistry 42:14366-14374(2003) [PubMed: 14661947] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 49-209 IN COMPLEX WITH COENZYME A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U47321 mRNA. Translation: AAB01099.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M1D	X-ray	2.20	A/C	48-209	[»]
1PU9	X-ray	2.30	A	48-209	[»]
1PUA	X-ray	2.30	A	48-209	[»]
1Q2C	X-ray	2.25	A	49-209	[»]
1Q2D	X-ray	2.25	A	49-209	[»]
1QSN	X-ray	2.20	A	49-209	[»]
1QSR	X-ray	2.00	A	49-209	[»]
1QST	X-ray	1.70	A	49-208	[»]
5GCN	NMR	-	A	47-210	[»]

ProteinModelPortal

Q27198.

SMR

Q27198. Positions 46-210.

ModBase

Search...

Protein-protein interaction databases

STRING

Q27198.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.20.920.10. Bromodomain. 1 hit.

Pfam

PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF47370. Bromodomain. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q27198_TETTH

Accession

Primary (citable) accession number: Q27198

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)