Q7K4Q5 (Y0417_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable protein phosphatase CG10417
EC=3.1.3.16

Gene names

ORF Names:

CG10417

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein dephosphorylation Non-traceable author statement PubMed 10908587. Source: FlyBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Non-traceable author statement PubMed 10908587. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 662	662	Probable protein phosphatase CG10417		PRO_0000372839
Regions
	Compositional bias	183 – 222	40	Ala-rich
Sites
	Metal binding	57	1	Manganese 1 By similarity
	Metal binding	57	1	Manganese 2 By similarity
	Metal binding	58	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	506	1	Manganese 2 By similarity
	Metal binding	555	1	Manganese 2 By similarity
Amino acid modifications
	Modified residue	289	1	Phosphoserine Ref.4
	Modified residue	306	1	Phosphoserine Ref.5
	Modified residue	592	1	Phosphoserine Ref.5
	Modified residue	594	1	Phosphoserine Ref.5
	Modified residue	599	1	Phosphoserine Ref.5
	Modified residue	637	1	Phosphothreonine Ref.5
	Modified residue	639	1	Phosphoserine Ref.5
	Modified residue	641	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q7K4Q5 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: C34171B9B030996E	FASTA	662	72,370
	10 20 30 40 50 60 MGAYLSHPKT DKTSTDQFNE LLAVGASSMQ GWRNSQEDAH NSILNFDNNT SFFAVYDGHG 70 80 90 100 110 120 GAEVAQYCAD KLPHFLKNLE TYKNGQFEVA LKEAFLGFDK TLLDPSIVSI LKILAGEHNF 130 140 150 160 170 180 VDAEADDYEE EDLAELQEES NLPLNEVLEK YKGLPQKKDL DLKSSDHKEN FKMRSPYFRG 190 200 210 220 230 240 RRAAALAAEA TNKAVMDPSA KPDGSSTSAA AAAAALSADG VANSRNPSNV VNPMAGADSN 250 260 270 280 290 300 TTTSINDLST KNAALKDDSV NDQNEGSNGT DFKHTLVSSS NKKLFATGSN DMTELNQSSK 310 320 330 340 350 360 NEFTNSSTSK EFERNINSSQ DDEFTDDDAD YEENDNVKSP DTSSAESSDC TENDDDGDED 370 380 390 400 410 420 GNEDSDEEET DEDQMANDNF CANMIEEPGK DSGCTAVVCL LQGRDLYVAN AGDSRCVISR 430 440 450 460 470 480 SGQAIEMSID HKPEDDEEAS RIIKAGGRVT LDGRVNGGLN LSRALGDHAY KTNVTLPAEE 490 500 510 520 530 540 QMISALPDIK KLIITPEDEF MVLACDGIWN YMSSEEVVEF VRCRLKDNKK LSTICEELFD 550 560 570 580 590 600 NCLAPNTMGD GTGCDNMTAV IVQFKKKLQE LQSTIPPNQT EDKLLKTSEN VSHSLNDQSA 610 620 630 640 650 660 SKRCASQNAD ADDEILEKNN SKRLKTDLEQ ENIKDRTPSP SNQNEDPTQK AIKEVTIIVS SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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. , 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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-592; SER-594; SER-599; THR-637; SER-639 AND SER-641, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF57333.1. AY051748 mRNA. Translation: AAK93172.1.
RefSeq	NP_610169.1. NM_136325.3. NP_724410.1. NM_165430.2.
UniGene	Dm.490.
3D structure databases
ProteinModelPortal	Q7K4Q5.
SMR	Q7K4Q5. Positions 1-117, 387-565.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0085428.
Proteomic databases
PaxDb	Q7K4Q5.
PRIDE	Q7K4Q5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0086091; FBpp0085427; FBgn0033021. FBtr0086092; FBpp0085428; FBgn0033021.
GeneID	35492.
KEGG	dme:Dmel_CG10417.
UCSC	CG10417-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0033021. CG10417.
Phylogenomic databases
eggNOG	COG0631.
GeneTree	ENSGT00650000093052.
InParanoid	Q7K4Q5.
KO	K01090.
OMA	IWNSMES.
OrthoDB	EOG4HMGRJ.
PhylomeDB	Q7K4Q5.
Gene expression databases
Bgee	Q7K4Q5.
Family and domain databases
Gene3D	3.60.40.10. 2 hits.
InterPro	IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 2 hits. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	35492.
NextBio	793693.

Entry information

Entry name

Y0417_DROME

Accession

Primary (citable) accession number: Q7K4Q5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	October 3, 2006
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project