Q9EZJ8 (Q9EZJ8_THEAQ) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Recommended name: RNA polymerase sigma factor RuleBase RU000715
Organism	Thermus aquaticus EMBL AAG36964.1
Taxonomic identifier	271 [NCBI]
Taxonomic lineage	Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released By similarity. RuleBase RU000715
Sequence similarities	Belongs to the sigma-70 factor family. RuleBase RU000715

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	DNA-binding RuleBase RU000715 SAAS SAAS013325
Molecular function	Sigma factor SAAS SAAS013325 RuleBase RU000715
Technical term	3D-structure PDB 1KU7 PDB 1KU3 PDB 1KU2 PDB 1L9U PDB 1L9Z PDB 1RIO PDB 3LES
Gene Ontology (GO)
Biological process	transcription initiation, DNA-dependent Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro sigma factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9EZJ8 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 5D8ACF5713DE55AD	FASTA	438	49,847
	10 20 30 40 50 60 MKKSKSKKKA AKAQEVEVKE PVKEPEPLPE LEAAEDLQDL PEPDPELLAS EPELEDLADP 70 80 90 100 110 120 LDLEGPLEAD LLPEEGLLEE EEEELSLPKV STSDPVRQYL HEIGQVPLLT LEEEIDLARK 130 140 150 160 170 180 VEEGMEAIKK LSEATGLDQE LIREVVRAKI LGTARIQKIP GLKEKPDPKT VEEVDGKLKS 190 200 210 220 230 240 LPKELKRYLH IAREGEAARQ HLIEANLRLV VSIAKKYTGR GLSFLDLIQE GNQGLIRAVE 250 260 270 280 290 300 KFEYKRRFKF STYATWWIRQ AINRAIADQA RTIRIPVHMV ETINKLSRTA RQLQQELGRE 310 320 330 340 350 360 PSYEEIAEAM GPGWDAKRVE ETLKIAQEPV SLETPIGDEK DSFYGDFIPD ENLPSPVEAA 370 380 390 400 410 420 AQSLLSEELE KALSKLSERE AMVLKLRKGL IDGREHTLEE VGAYFGVTRE RIRQIENKAL 430 RKLKYHESRT RKLRDFLE

References

[1]	"Recombinant Thermus aquaticus RNA Polymerase-A New Tool for Structure-Based Analysis of Transcription Function." Minakhin L., Nechaev S., Campbell E., Severinov K. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Structure of the bacterial RNA polymerase promoter specificity sigma subunit." Campbell E.A., Muzzin O., Chlenov M., Sun J.L., Olson C.A., Weinman O., Trester-Zedlitz M.L., Darst S.A. Mol. Cell 9:527-539(2002) [PubMed: 11931761] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 366-438.
[3]	"Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution." Murakami K.S., Masuda S., Darst S.A. Science 296:1280-1284(2002) [PubMed: 12016306] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 92-438.
[4]	"Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex." Murakami K.S., Masuda S., Campbell E.A., Muzzin O., Darst S.A. Science 296:1285-1290(2002) [PubMed: 12016307] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (6.50 ANGSTROMS).
[5]	"Structure of a ternary transcription activation complex." Jain D., Nickels B.E., Sun L., Hochschild A., Darst S.A. Mol. Cell 13:45-53(2004) [PubMed: 14731393] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 366-438.
[6]	"Elicitation of structure-specific antibodies by epitope scaffolds." Ofek G., Guenaga F.J., Schief W.R., Skinner J., Baker D., Wyatt R., Kwong P.D. Proc. Natl. Acad. Sci. U.S.A. 107:17880-17887(2010) [PubMed: 20876137] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 93-271.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF291720 Genomic DNA. Translation: AAG36964.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KU2	X-ray	2.90	A/B	92-332	[»]
1KU3	X-ray	1.80	A	366-438	[»]
1KU7	X-ray	2.40	A/D	366-438	[»]
1L9U	X-ray	4.00	H/Q	92-438	[»]
1L9Z	X-ray	6.50	H	1-438	[»]
1RIO	X-ray	2.30	H	366-438	[»]
3LES	X-ray	2.77	A/B	93-271	[»]
3LEV	X-ray	2.50	A	93-271	[»]
3N97	X-ray	3.25	A/D	366-423	[»]

ProteinModelPortal

Q9EZJ8.

SMR

Q9EZJ8. Positions 89-438.

ModBase

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Protein-protein interaction databases

DIP

DIP-49014N.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR014284. RNA_pol_sigma-70.
IPR000943. RNA_pol_sigma70.
IPR009042. RNA_pol_sigma70_r1_2.
IPR007627. RNA_pol_sigma70_r2.
IPR007624. RNA_pol_sigma70_r3.
IPR007630. RNA_pol_sigma70_r4.
IPR013325. RNA_pol_sigma_r2.
IPR013324. RNA_pol_sigma_r3_r4.
IPR012760. RNA_pol_sigma_RpoD_C.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.

Pfam

PF00140. Sigma70_r1_2. 1 hit.
PF04542. Sigma70_r2. 1 hit.
PF04539. Sigma70_r3. 1 hit.
PF04545. Sigma70_r4. 1 hit.
[Graphical view]

PRINTS

PR00046. SIGMA70FCT.

SUPFAM

SSF88946. Sigma_r2. 1 hit.
SSF88659. Sigma_r3_r4. 2 hits.

TIGRFAMs

TIGR02393. RpoD_Cterm. 1 hit.
TIGR02937. Sigma70-ECF. 1 hit.

PROSITE

PS00716. SIGMA70_2. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q9EZJ8_THEAQ

Accession

Primary (citable) accession number: Q9EZJ8

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	October 19, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)