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Q9VAM9

- MESH1_DROME

UniProt

Q9VAM9 - MESH1_DROME

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Protein

Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1

Gene
Mesh1, CG11900
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

ppGpp hydrolyzing enzyme involved in starvation response.1 Publication

Catalytic activityi

Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.1 Publication

Cofactori

Manganese.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Manganese
Metal bindingi62 – 621Manganese
Metal bindingi63 – 631Manganese
Active sitei66 – 661Nucleophile Inferred
Active sitei67 – 671Nucleophile Inferred
Metal bindingi123 – 1231Manganese

GO - Molecular functioni

  1. guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Source: FlyBase
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoric diester hydrolase activity Source: InterPro

GO - Biological processi

  1. guanosine tetraphosphate catabolic process Source: FlyBase
  2. response to starvation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1 (EC:3.1.7.2)
Alternative name(s):
Metazoan SpoT homolog 1
Short name:
Mesh1
Penta-phosphate guanosine-3'-pyrophosphohydrolase
Short name:
(ppGpp)ase
Gene namesi
Name:Mesh1
ORF Names:CG11900
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039650. Mesh1.

Pathology & Biotechi

Disruption phenotypei

Induces retarded body growth and impaired starvation resistance. Mutants have highly down-regulated DNA and protein synthesis-related genes and up-regulated stress-responsible genes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 179179Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1PRO_0000402127Add
BLAST

Proteomic databases

PaxDbiQ9VAM9.
PRIDEiQ9VAM9.

Expressioni

Gene expression databases

BgeeiQ9VAM9.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0084776.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1913
Beta strandi26 – 294
Helixi34 – 4512
Turni46 – 483
Helixi53 – 608
Turni61 – 633
Helixi64 – 674
Helixi72 – 798
Helixi81 – 899
Helixi98 – 10710
Helixi114 – 13320
Helixi141 – 15818
Helixi163 – 17614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NQWX-ray2.90A/B1-179[»]
ProteinModelPortaliQ9VAM9.
SMRiQ9VAM9. Positions 2-179.

Family & Domainsi

Sequence similaritiesi

Belongs to the MESH1 family.

Phylogenomic databases

eggNOGiCOG0317.
GeneTreeiENSGT00390000011608.
InParanoidiQ9VAM9.
KOiK01139.
OMAiYVNHVIN.
OrthoDBiEOG7X3QTC.
PhylomeDBiQ9VAM9.

Family and domain databases

InterProiIPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
[Graphical view]
PfamiPF01966. HD. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VAM9-1 [UniParc]FASTAAdd to Basket

« Hide

MATYPSAKFM ECLQYAAFKH RQQRRKDPQE TPYVNHVINV STILSVEACI    50
TDEGVLMAAL LHDVVEDTDA SFEDVEKLFG PDVCGLVREV TDDKSLEKQE 100
RKRLQIENAA KSSCRAKLIK LADKLDNLRD LQVNTPTGWT QERRDQYFVW 150
AKKVVDNLRG TNANLELKLD EIFRQRGLL 179
Length:179
Mass (Da):20,569
Last modified:May 1, 2000 - v1
Checksum:i9227D3DA9AD4E983
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF56875.1.
BT024375 mRNA. Translation: ABC86437.1.
RefSeqiNP_651682.1. NM_143425.2.
UniGeneiDm.24112.

Genome annotation databases

EnsemblMetazoaiFBtr0085407; FBpp0084776; FBgn0039650.
GeneIDi43456.
KEGGidme:Dmel_CG11900.
UCSCiCG11900-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF56875.1 .
BT024375 mRNA. Translation: ABC86437.1 .
RefSeqi NP_651682.1. NM_143425.2.
UniGenei Dm.24112.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NQW X-ray 2.90 A/B 1-179 [» ]
ProteinModelPortali Q9VAM9.
SMRi Q9VAM9. Positions 2-179.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0084776.

Proteomic databases

PaxDbi Q9VAM9.
PRIDEi Q9VAM9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085407 ; FBpp0084776 ; FBgn0039650 .
GeneIDi 43456.
KEGGi dme:Dmel_CG11900.
UCSCi CG11900-RA. d. melanogaster.

Organism-specific databases

CTDi 43456.
FlyBasei FBgn0039650. Mesh1.

Phylogenomic databases

eggNOGi COG0317.
GeneTreei ENSGT00390000011608.
InParanoidi Q9VAM9.
KOi K01139.
OMAi YVNHVIN.
OrthoDBi EOG7X3QTC.
PhylomeDBi Q9VAM9.

Miscellaneous databases

GenomeRNAii 43456.
NextBioi 834034.
PROi Q9VAM9.

Gene expression databases

Bgeei Q9VAM9.

Family and domain databases

InterProi IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
[Graphical view ]
Pfami PF01966. HD. 1 hit.
[Graphical view ]
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J., Park S., Wan K., Yu C., Celniker S.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, MANGANESE-BINDING SITES.

Entry informationi

Entry nameiMESH1_DROME
AccessioniPrimary (citable) accession number: Q9VAM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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