P53550 (DCP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-decapping enzyme subunit 2
EC=3.-.-.-

Alternative name(s):
Protein PSU1

Gene names

Name:	DCP2
Synonyms:	PSU1
Ordered Locus Names:	YNL118C
ORF Names:	N1917

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	970 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. Ref.8 Ref.10 Ref.11 Ref.13
Cofactor	Manganese By similarity.
Subunit structure	Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNA, LSM2, LSM4 and LSM8. Interacts with EDC3. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.15
Subcellular location	Cytoplasm › P-body. Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. Ref.14
Miscellaneous	Present with 8530 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the Nudix hydrolase family. DCP2 subfamily. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay mRNA processing
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding RNA-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	deadenylation-dependent decapping of nuclear-transcribed mRNA Inferred from direct assay Ref.10. Source: SGD deadenylation-independent decapping of nuclear-transcribed mRNA Inferred from mutant phenotype PubMed 15225544. Source: SGD mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW stress granule assembly Inferred from mutant phenotype PubMed 20513766. Source: SGD
Cellular_component	cytoplasmic mRNA processing body Inferred from direct assay Ref.14. Source: SGD nucleus Inferred from direct assay PubMed 11914276. Source: SGD
Molecular_function	m7G(5')pppN diphosphatase activity Inferred from direct assay PubMed 16341225. Source: SGD mRNA binding Inferred from physical interaction Ref.10. Source: SGD manganese ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DCP1	Q12517	5	EBI-270,EBI-38519
EDC3	P39998	6	EBI-270,EBI-22300

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 970

970

mRNA-decapping enzyme subunit 2

PRO_0000057054

Regions

Domain

101 – 228

128

Nudix hydrolase

Motif

134 – 155

22

Nudix box

Compositional bias

345 – 430

86

Pro-rich

Compositional bias

436 – 439

4

Poly-Ser

Sites

Metal binding

149

1

Manganese By similarity

Metal binding

153

1

Manganese By similarity

Amino acid modifications

Modified residue

116

1

Phosphoserine Ref.19

Modified residue

319

1

Phosphoserine Ref.19

Modified residue

320

1

Phosphoserine Ref.19

Modified residue

438

1

Phosphoserine Ref.19

Modified residue

577

1

Phosphoserine Ref.19

Modified residue

584

1

Phosphoserine Ref.19

Modified residue

598

1

Phosphoserine Ref.19

Modified residue

607

1

Phosphoserine Ref.16

Modified residue

608

1

Phosphoserine Ref.16

Modified residue

679

1

Phosphoserine Ref.17

Modified residue

682

1

Phosphoserine Ref.16 Ref.19

Modified residue

686

1

Phosphothreonine Ref.19

Modified residue

691

1

Phosphoserine Ref.19

Modified residue

710

1

Phosphothreonine Ref.18 Ref.19

Modified residue

713

1

Phosphoserine Ref.18

Modified residue

728

1

Phosphoserine Ref.19

Modified residue

729

1

Phosphoserine Ref.18 Ref.19

Modified residue

730

1

Phosphoserine Ref.19

Modified residue

747

1

Phosphoserine Ref.19

Modified residue

751

1

Phosphoserine Ref.17 Ref.19

Modified residue

778

1

Phosphoserine Ref.16

Modified residue

783

1

Phosphoserine Ref.19

Modified residue

784

1

Phosphothreonine Ref.19

Modified residue

786

1

Phosphoserine Ref.19

Modified residue

836

1

Phosphoserine Ref.19

Modified residue

942

1

Phosphoserine Ref.19

Modified residue

958

1

Phosphoserine Ref.18

Natural variations

Natural variant

188

1

V → A in strain: YJM339. Ref.3

Natural variant

288

1

Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. Ref.3

Natural variant

301

1

L → H in strain: YJM280, YJM 20 and YJM339. Ref.3

Natural variant

319

1

S → P in strain: YJM627. Ref.3

Natural variant

494

1

D → N in strain: YJM339. Ref.3

Natural variant

505

1

I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. Ref.3

Natural variant

522

1

G → D in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3

Natural variant

547

1

N → T in strain: YJM280 and YJM320. Ref.3

Natural variant

567

1

S → R in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3

Natural variant

574

1

N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. Ref.3

Natural variant

577

1

S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. Ref.3

Natural variant

622

1

G → S in strain: V1-09 and YJM339. Ref.3

Natural variant

650

1

D → G in strain: YJM280 and YJM320. Ref.3

Natural variant

740

1

P → S in strain: YJM269 and YJM270. Ref.3

Natural variant

807

1

T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. Ref.3

Natural variant

823

1

S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. Ref.3

Natural variant

835

1

D → N in strain: YJM280 and YJM320. Ref.3

Natural variant

844

1

G → V in strain: V1-09. Ref.3

Natural variant

851

1

S → P in strain: YJM280, YJM320 and YJM627. Ref.3

Natural variant

854

1

M → I in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3

Natural variant

864

1

E → Q in strain: YJM269 and YJM270. Ref.3

Natural variant

865

1

L → S in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3

Natural variant

866

1

D → A in strain: YJM627.

Natural variant

909

1

A → T in strain: YJM280 and YJM320. Ref.3

Natural variant

945

1

I → L in strain: YJM627. Ref.3

Natural variant

951

1

D → E in strain: V1-09. Ref.3

Experimental info

Mutagenesis

60

1

N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. Ref.10

Mutagenesis

68

1

I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. Ref.10

Mutagenesis

142

1

D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. Ref.10

Sequence conflict

425

1

P → L in AAA68866. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

970

Helix Strand Turn

Details...

Beta strand

106 – 111

6

Beta strand

115 – 121

7

Beta strand

124 – 127

4

Beta strand

138 – 140

3

Helix

142 – 153

12

Beta strand

159 – 162

4

Beta strand

167 – 172

6

Beta strand

175 – 182

8

Beta strand

187 – 189

3

Beta strand

196 – 198

3

Beta strand

202 – 206

5

Helix

207 – 211

5

Helix

212 – 215

4

Helix

222 – 241

20

Sequences

	Sequence		Length	Mass (Da)
	P53550 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D53CA2C5A546FA4A	FASTA	970	108,667
	10 20 30 40 50 60 MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW FYTDFIKLMN 70 80 90 100 110 120 PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK KSIPVRGAAI FNENLSKILL 130 140 150 160 170 180 VQGTESDSWS FPRGKISKDE NDIDCCIREV KEEIGFDLTD YIDDNQFIER NIQGKNYKIF 190 200 210 220 230 240 LISGVSEVFN FKPQVRNEID KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ 250 260 270 280 290 300 IKNEDQLKSY AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE 310 320 330 340 350 360 LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM ANVFMSNPQL 370 380 390 400 410 420 FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP NPMAFGVPNM HNLSGPAVSQ 430 440 450 460 470 480 PFSLPPAPLP RDSGYSSSSP GQLLDILNSK KPDSNVQSSK KPKLKILQRG TDLNSIKQNN 490 500 510 520 530 540 NDETAHSNSQ ALLDLLKKPT SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE 550 560 570 580 590 600 TARDERNSLN VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS 610 620 630 640 650 660 TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD NSKLISQDIL 670 680 690 700 710 720 KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP KVKILKRGET FASLANDKKA 730 740 750 760 770 780 FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE 790 800 810 820 830 840 NASTSSINDA NASELLGMLK QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP 850 860 870 880 890 900 RTEGGPSSEM STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI 910 920 930 940 950 960 LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF DVRSNGTSGS 970 NELLSILHRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen." He F., Jacobson A. Genes Dev. 9:437-454(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Tzagoloff A.A. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24657 / D273-10B.
[3]	"Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast." Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M. Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-188; ASN-288 DEL; HIS-301; PRO-319; ASN-494; THR-505; ASP-522; THR-547; ARG-567; SER-574; ASN-577; SER-622; GLY-650; SER-740; ALA-807; PRO-823; ASN-835; VAL-844; PRO-851; ILE-854; GLN-864; SER-865; THR-909; LEU-945 AND GLU-951. Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230.
[4]	"The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames." de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G. Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Crystal structure of human Edc3 and its functional implications." Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H. Mol. Cell. Biol. 28:5965-5976(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EDC3.
[7]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[8]	"The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif." Dunckley T., Parker R. EMBO J. 18:5411-5422(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCP1.
[9]	"Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins." Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A., Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P. Yeast 17:95-110(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LSM2; LSM4 AND LSM8.
[10]	"Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae." Dunckley T., Tucker M., Parker R. Genetics 157:27-37(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASN-60; ILE-68 AND ASP-142, INTERACTION WITH EDC1.
[11]	"Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs." Tharun S., Parker R. Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MRNA, FUNCTION OF THE DCP1-DCP2 COMPLEX.
[12]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]	"Analysis of recombinant yeast decapping enzyme." Steiger M., Carr-Schmid A., Schwartz D.C., Kiledjian M., Parker R. RNA 9:231-238(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE DCP1-DCP2 COMPLEX.
[14]	"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies." Sheth U., Parker R. Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"Crystal structure of Dcp1p and its functional implications in mRNA decapping." She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H. Nat. Struct. Mol. Biol. 11:249-256(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCP1.
[16]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-608; SER-682 AND SER-778, MASS SPECTROMETRY. Strain: YAL6B.
[17]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679 AND SER-751, MASS SPECTROMETRY. Strain: ADR376.
[18]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-710; SER-713; SER-729 AND SER-958, MASS SPECTROMETRY.
[19]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-319; SER-320; SER-438; SER-577; SER-584; SER-598; SER-682; THR-686; SER-691; THR-710; SER-728; SER-729; SER-730; SER-747; SER-751; SER-783; THR-784; SER-786; SER-836 AND SER-942, MASS SPECTROMETRY.
[20]	"mRNA decapping is promoted by an RNA-binding channel in Dcp2." Deshmukh M.V., Jones B.N., Quang-Dang D.U., Flinders J., Floor S.N., Kim C., Jemielity J., Kalek M., Darzynkiewicz E., Gross J.D. Mol. Cell 29:324-336(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 100-245.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31377 Genomic DNA. Translation: AAC99860.1.
L43065 Genomic DNA. Translation: AAA68866.1.
EF125216 Genomic DNA. Translation: ABN58539.1.
EF125217 Genomic DNA. Translation: ABN58548.1.
EF125218 Genomic DNA. Translation: ABN58557.1.
EF125219 Genomic DNA. Translation: ABN58566.1.
EF125220 Genomic DNA. Translation: ABN58578.1.
EF125221 Genomic DNA. Translation: ABN58584.1.
EF125222 Genomic DNA. Translation: ABN58593.1.
EF125223 Genomic DNA. Translation: ABN58602.1.
EF125224 Genomic DNA. Translation: ABN58611.1.
EF125225 Genomic DNA. Translation: ABN58620.1.
EF125226 Genomic DNA. Translation: ABN58629.1.
EF125228 Genomic DNA. Translation: ABN58647.1.
Z69382 Genomic DNA. Translation: CAA93389.1.
Z71394 Genomic DNA. Translation: CAA95998.1.
BK006947 Genomic DNA. Translation: DAA10430.1.

PIR

S63059.

RefSeq

NP_014281.1. NM_001182956.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JVB	NMR	-	A	100-245	[»]

ProteinModelPortal

P53550.

SMR

P53550. Positions 14-244.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-969N.

IntAct

P53550. 21 interactions.

MINT

MINT-385102.

Proteomic databases

PeptideAtlas

P53550.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL118C; YNL118C; YNL118C.

GeneID

855605.

KEGG

sce:YNL118C.

Organism-specific databases

CYGD

YNL118c.

SGD

S000005062. DCP2.

Phylogenomic databases

GeneTree

ENSGT00390000018878.

KO

K12613.

OrthoDB

EOG4MD187.

Gene expression databases

Genevestigator

P53550.

GermOnline

YNL118C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.90.79.10. 1 hit.

InterPro

IPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]

Pfam

PF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

PROSITE

PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P53550.

NextBio

979774.

Entry information

Entry name

DCP2_YEAST

Accession

Primary (citable) accession number: P53550
Secondary accession number(s): B0KZS6 , B0KZU4, B0KZW2, B0KZY0, B0KZY9, B0KZZ8, B0L007, D6W164, Q6LCS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program