O28951 (PIWI_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Piwi protein AF_1318

Alternative name(s):
AfPiwi

Gene names

Ordered Locus Names:

AF_1318

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as short interfering RNAs (siRNAs), and may cleave or repress the translation of mRNAs which are complementary to them By similarity.
Sequence similarities	Belongs to the argonaute family. Contains 1 Piwi domain.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing
Ligand	Metal-binding RNA-binding
Molecular function	Ribonucleoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal 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 – 427

427

Piwi protein AF_1318

PRO_0000378146

Regions

Domain

110 – 406

297

Piwi

Sites

Metal binding

159

1

Divalent metal cation

Metal binding

427

1

Divalent metal cation; via carboxylate

Experimental info

Mutagenesis

123

1

Y → A: Reduced binding affinity for siRNA. Ref.4

Mutagenesis

127

1

K → A: Reduced binding affinity for siRNA. Ref.4

Mutagenesis

137

1

Q → A: Reduced binding affinity for siRNA. Ref.4

Mutagenesis

163

1

K → A: Reduced binding affinity for siRNA. Ref.4

Mutagenesis

427

1

L → LG: Reduced binding to siRNA. Ref.2

Secondary structure

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427

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Beta strand

20 – 24

5

Beta strand

45 – 54

10

Helix

59 – 74

16

Beta strand

82 – 87

6

Beta strand

89 – 92

4

Helix

93 – 105

13

Beta strand

112 – 117

6

Helix

120 – 131

12

Beta strand

137 – 140

4

Helix

141 – 143

3

Turn

146 – 148

3

Helix

149 – 163

15

Beta strand

181 – 183

3

Beta strand

188 – 196

9

Beta strand

198 – 202

5

Beta strand

208 – 213

6

Helix

219 – 221

3

Helix

222 – 234

13

Turn

238 – 240

3

Beta strand

247 – 253

7

Helix

265 – 277

13

Beta strand

286 – 294

9

Beta strand

298 – 300

3

Beta strand

315 – 328

14

Beta strand

341 – 353

13

Turn

357 – 359

3

Helix

360 – 375

16

Helix

389 – 397

9

Helix

401 – 406

6

Helix

419 – 422

4

Sequences

	Sequence		Length	Mass (Da)
	O28951 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: F925081F3AFB47CD	FASTA	427	49,244
	10 20 30 40 50 60 MMEYKIVENG LTYRIGNGAS VPISNTGELI KGLRNYGPYE VPSLKYNQIA LIHNNQFSSL 70 80 90 100 110 120 INQLKSQISS KIDEVWHIHN INISEFIYDS PHFDSIKSQV DNAIDTGVDG IMLVLPEYNT 130 140 150 160 170 180 PLYYKLKSYL INSIPSQFMR YDILSNRNLT FYVDNLLVQF VSKLGGKPWI LNVDPEKGSD 190 200 210 220 230 240 IIIGTGATRI DNVNLFCFAM VFKKDGTMLW NEISPIVTSS EYLTYLKSTI KKVVYGFKKS 250 260 270 280 290 300 NPDWDVEKLT LHVSGKRPKM KDGETKILKE TVEELKKQEM VSRDVKYAIL HLNETHPFWV 310 320 330 340 350 360 MGDPNNRFHP YEGTKVKLSS KRYLLTLLQP YLKRNGLEMV TPIKPLSVEI VSDNWTSEEY 370 380 390 400 410 420 YHNVHEILDE IYYLSKMNWR GFRSRNLPVT VNYPKLVAGI IANVNRYGGY PINPEGNRSL QTNPWFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Crystal structure of a PIWI protein suggests mechanisms for siRNA recognition and slicer activity." Parker J.S., Roe S.M., Barford D. EMBO J. 23:4727-4737(2004) [PubMed: 15565169] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), RNA-BINDING, MUTAGENESIS OF LEU-427.
[3]	"Structural insights into mRNA recognition from a PIWI domain-siRNA guide complex." Parker J.S., Roe S.M., Barford D. Nature 434:663-666(2005) [PubMed: 15800628] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN A COMPLEX WITH SIRNA DUPLEX, RNA-BINDING.
[4]	"Structural basis for 5'-end-specific recognition of guide RNA by the A. fulgidus Piwi protein." Ma J.-B., Yuan Y.-R., Meister G., Pei Y., Tuschl T., Patel D.J. Nature 434:666-670(2005) [PubMed: 15800629] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN A COMPLEX WITH SIRNA DUPLEX, DNA-BINDING, RNA-BINDING, MUTAGENESIS OF TYR-123; LYS-127; GLN-137 AND LYS-163.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000782 Genomic DNA. Translation: AAB89939.1.

PIR

E69414.

RefSeq

NP_070147.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W9H	X-ray	1.95	A	1-427	[»]
1YTU	X-ray	2.50	A/B	1-427	[»]
2BGG	X-ray	2.20	A/B	1-427	[»]
2W42	X-ray	1.90	A/B	1-427	[»]

ProteinModelPortal

O28951.

SMR

O28951. Positions 1-427.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1484544.

GenomeReviews

Gene locus AF_1318 in contig AE000782_GR.

KEGG

afu:AF1318.

NMPDR

fig|224325.1.peg.1308.

TIGR

AF_1318.

Enzyme and pathway databases

BioCyc

AFUL224325:AF_1318-MONOMER.

Family and domain databases

InterPro

IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]

KO

K07578.

Pfam

PF02171. Piwi. 1 hit.
[Graphical view]

SMART

SM00950. Piwi. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS50822. PIWI. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PIWI_ARCFU

Accession

Primary (citable) accession number: O28951

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program