Skip Header

Contribute Send feedback
Read comments (?) or add your own

O77460 (IPYR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inorganic pyrophosphatase

EC=3.6.1.1
Alternative name(s):
Nucleosome-remodeling factor 38 kDa subunit
Pyrophosphate phospho-hydrolase
Short name=PPase
Gene names
Name:Nurf-38
ORF Names:CG4634
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis. Nurf-38 may have adapted to deliver pyrophosphatase to chromatin to assist in replication or transcription by efficient removal of the inhibitory metabolite. Ref.1 Ref.5

Catalytic activity

Diphosphate + H2O = 2 phosphate.

Cofactor

Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product By similarity.

Subunit structure

Component of the NURF complex composed of Caf1, E(bx), Nurf-38 and Iswi.

Subcellular location

Cytoplasm. Nucleus.

Miscellaneous

The ATPase activity of NURF is stimulated by the presence of nucleosomes rather than by free DNA.

Sequence similarities

Belongs to the PPase family.

Sequence caution

The sequence AAC97111.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAL68291.1 differs from that shown. Reason: Frameshift at position 18.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Inorganic pyrophosphatase
PRO_0000137572

Sites

Metal binding1661Magnesium 1 By similarity
Metal binding1711Magnesium 1 By similarity
Metal binding1711Magnesium 2 By similarity
Metal binding2031Magnesium 1 By similarity
Binding site1291Diphosphate By similarity

Experimental info

Mutagenesis1291R → A: Drastic reduction of activity. Ref.1
Sequence conflict193 – 1942TI → QF in AAC97111. Ref.1
Sequence conflict193 – 1942TI → QF in AAC97112. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O77460 [UniParc].

Last modified August 31, 2004. Version 3.
Checksum: B4B7341CD5A3E5F2

FASTA33837,939
        10         20         30         40         50         60 
MLAKITRSSF YASRAVGRLS GSIPTSPAAL ASNCRYIQIE RKRTKSHEMA LYETVEKGAK 

        70         80         90        100        110        120 
NSPSYSLYFK NKCGNVISPM HDIPLYANEE KTIYNMVVEV PRWTNAKMEI SLKTPMNPIK 

       130        140        150        160        170        180 
QDIKKGKLRF VANCFPHKGY IWNYGALPQT WENPDHIEPS TGCKGDNDPI DVIEIGYRVA 

       190        200        210        220        230        240 
KRGDVLKVKV LGTIALIDEG ETDWKIIAID VNDPLASKVN DIADVDQYFP GLLRATVEWF 

       250        260        270        280        290        300 
KIYKIPDGKP ENQFAFNGDA KNADFANTII AETHKFWQNL VHQSPASGSI STTNITNRNS 

       310        320        330 
EHVIPKEEAE KILAEAPDGG QVEEVSDTVD TWHFIHLK 

« Hide

References

« Hide 'large scale' references
[1]"Inorganic pyrophosphatase is a component of the Drosophila nucleosome remodeling factor complex."
Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.
Genes Dev. 12:3206-3216(1998) [PubMed: 9784495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, MUTAGENESIS OF ARG-129.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Purification and properties of an ATP-dependent nucleosome remodeling factor."
Tsukiyama T., Wu C.
Cell 83:1011-1020(1995) [PubMed: 8521501] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF085600 Genomic DNA. Translation: AAC97111.1. Different initiation.
AF085601 mRNA. Translation: AAC97112.1.
AE013599 Genomic DNA. Translation: AAF47227.2.
AY075479 mRNA. Translation: AAL68291.1. Frameshift.
RefSeqNP_001137758.1. NM_001144286.2.
NP_523849.3. NM_079125.3.
UniGeneDm.1958.

3D structure databases

ProteinModelPortalO77460.
SMRO77460. Positions 51-337.
ModBaseSearch...

Protein-protein interaction databases

IntActO77460. 1 interaction.
MINTMINT-286916.
STRINGO77460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072343; FBpp0072250; FBgn0016687.
GeneID37922.
KEGGdme:Dmel_CG4634.
NMPDRfig|7227.3.peg.7338.

Organism-specific databases

CTD37922.
FlyBaseFBgn0016687. Nurf-38.

Phylogenomic databases

eggNOGinNOG04019.
GeneTreeEMGT00050000017751.
InParanoidO77460.
OMASTGCKGD.
OrthoDBEOG4J0ZQZ.
PhylomeDBO77460.

Gene expression databases

BgeeO77460.
GermOnlineCG4634. Drosophila melanogaster.

Family and domain databases

InterProIPR008162. Pyrophosphatase.
[Graphical view]
Gene3DG3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
KOK11726.
PANTHERPTHR10286. Pyrophosphatase. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMSSF50324. Pyrophosphatase. 1 hit.
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio806063.

Entry information

Entry nameIPYR_DROME
AccessionPrimary (citable) accession number: O77460
Secondary accession number(s): Q9W150
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 31, 2004
Last modified: January 25, 2012
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families