P58192 (RPOA2_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase subunit A''
EC=2.7.7.6

Gene names

Name:	rpoA2
Ordered Locus Names:	SSO0223

Organism

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Taxonomic identifier

273057 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. HAMAP MF_00411
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). HAMAP MF_00411
Subunit structure	This RNA polymerase is composed of 13 subunits By similarity.
Sequence similarities	Belongs to the RNA polymerase beta' chain family.
Sequence caution	The sequence AAK40565.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity 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 – 392

392

DNA-directed RNA polymerase subunit A'' HAMAP MF_00411

PRO_0000074026

Secondary structure

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392

Helix Strand Turn

Details...

Helix

11 – 17

7

Helix

20 – 23

4

Helix

29 – 34

6

Turn

39 – 41

3

Helix

47 – 56

10

Helix

57 – 59

3

Helix

67 – 74

8

Turn

75 – 78

4

Helix

79 – 81

3

Helix

102 – 109

8

Beta strand

118 – 122

5

Beta strand

124 – 126

3

Helix

131 – 139

9

Beta strand

243 – 245

3

Beta strand

247 – 252

6

Turn

256 – 260

5

Beta strand

265 – 270

6

Helix

276 – 281

6

Helix

283 – 292

10

Turn

293 – 297

5

Helix

298 – 300

3

Helix

307 – 317

11

Beta strand

318 – 322

5

Turn

328 – 331

4

Beta strand

332 – 336

5

Helix

338 – 343

6

Helix

350 – 356

7

Beta strand

365 – 367

3

Helix

368 – 372

5

Beta strand

377 – 379

3

Turn

380 – 382

3

Beta strand

384 – 386

3

Sequences

	Sequence		Length	Mass (Da)
	P58192 [UniParc]. Last modified June 20, 2001. Version 1. Checksum: 5B0E871D056CE08B	FASTA	392	43,488
	10 20 30 40 50 60 MIDEKDKPYL EEKVKQASNI LPQKIVDDLK NLILNKEIIV TRDEIDKIFD LAIKEYSEGL 70 80 90 100 110 120 IAPGEAIGIV AAQSVGEPGT QMTLRTFHFA GIRELNVTLG LPRLIEIVDA KKVPSTPMMT 130 140 150 160 170 180 IYLTDEYKRD RDKALEVARK LEYTKIENVV SSTSIDIASM SIILQLDNEM LKDKGVTVDD 190 200 210 220 230 240 VKKAIGRLKL GDFMIEESED STLNINFANI DSIAALFKLR DKILNTKIKG IKGIKRAIVQ 250 260 270 280 290 300 KKGDEYIILT DGSNLSGVLS VKGVDVAKVE TNNIREIEEV FGIEAAREII IREISKVLAE 310 320 330 340 350 360 QGLDVDIRHI LLIADVMTRT GIVRQIGRHG VTGEKNSVLA RAAFEVTVKH LLDAAARGDV 370 380 390 EEFKGVVENI IIGHPIKLGT GMVELTMRPI LR

References

[1]

"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

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Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE006641 Genomic DNA. Translation: AAK40565.1. Different initiation.

PIR

F90163.

RefSeq

NP_341775.1. NC_002754.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PMZ	X-ray	3.40	C/G	1-392	[»]
3HKZ	X-ray	3.40	C/M	1-392	[»]

ProteinModelPortal

P58192.

SMR

P58192. Positions 8-392.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1455375.

GenomeReviews

Gene locus SSO0223 in contig AE006641_GR.

KEGG

sso:SSO0223.

NMPDR

fig|273057.1.peg.198.

Phylogenomic databases

HOGENOM

HBG297327.

OMA

RPIGRHG.

ProtClustDB

PRK04309.

Enzyme and pathway databases

BioCyc

SSOL273057:SSO0223-MONOMER.

Family and domain databases

HAMAP

MF_00411. RNApol_arch_A.
[Tree]

InterPro

IPR012757. DNA-dir_RpoA2.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]

KO

K03042.

Pfam

PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02389. RNA_pol_rpoA2. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RPOA2_SULSO

Accession

Primary (citable) accession number: P58192

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	June 20, 2001
Last modified:	November 16, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program