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Protein

mRNA decapping complex subunit 2

Gene

dcp2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671ATP
Binding sitei220 – 2201ATP

GO - Molecular functioni

  • ATP binding Source: PomBase
  • m7G(5')pppN diphosphatase activity Source: PomBase
  • magnesium ion binding Source: PomBase
  • manganese ion binding Source: InterPro
  • RNA 7-methylguanosine cap binding Source: PomBase
  • single-stranded RNA binding Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-SPO-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA decapping complex subunit 2 (EC:3.-.-.-)
Gene namesi
Name:dcp2
ORF Names:SPAC19A8.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC19A8.12.
PomBaseiSPAC19A8.12. dcp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytoplasmic mRNA processing body Source: PomBase
  • cytoplasmic stress granule Source: PomBase
  • cytosol Source: PomBase
  • Dcp1-Dcp2 complex Source: PomBase
  • mRNA cap binding complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181R → A: Abolishes interaction with dcp1. 1 Publication
Mutagenesisi19 – 191F → A: Decreases interaction with dcp1. 1 Publication
Mutagenesisi44 – 441F → A: Decreases interaction with dcp1. 1 Publication
Mutagenesisi143 – 1431E → A: Abolishes the decapping activity in vitro. 1 Publication
Mutagenesisi192 – 1921E → A: Abolishes the decapping activity in vitro. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741mRNA decapping complex subunit 2PRO_0000373871Add
BLAST

Proteomic databases

MaxQBiO13828.

Interactioni

Subunit structurei

Component of the decapping complex composed of dcp1 and dcp2 (By similarity). Interacts with edc3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
edc3O947525EBI-3647323,EBI-7556871
sum2Q9HGL34EBI-3647323,EBI-1117052

Protein-protein interaction databases

BioGridi278961. 16 interactions.
DIPiDIP-29009N.
IntActiO13828. 4 interactions.
MINTiMINT-4668291.

Structurei

Secondary structure

1
741
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi8 – 1912Combined sources
Turni20 – 223Combined sources
Helixi25 – 273Combined sources
Helixi31 – 4717Combined sources
Turni48 – 525Combined sources
Beta strandi54 – 563Combined sources
Helixi61 – 7111Combined sources
Helixi74 – 796Combined sources
Helixi83 – 908Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi106 – 11813Combined sources
Beta strandi126 – 1294Combined sources
Helixi136 – 14813Combined sources
Turni153 – 1553Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi169 – 1768Combined sources
Beta strandi193 – 2008Combined sources
Helixi201 – 2033Combined sources
Helixi217 – 2193Combined sources
Turni220 – 2223Combined sources
Helixi223 – 2253Combined sources
Helixi226 – 24015Combined sources
Beta strandi245 – 2473Combined sources
Helixi255 – 26511Combined sources
Beta strandi272 – 2743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A6TX-ray2.50A/B1-266[»]
2QKLX-ray2.33B1-95[»]
2QKMX-ray2.80B/D/F/H1-266[»]
4A54NMR-B242-291[»]
5J3TX-ray1.60B1-242[»]
5J3YX-ray3.29B/D1-242[»]
ProteinModelPortaliO13828.
SMRiO13828. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO13828.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini94 – 227134Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi128 – 14922Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family. DCP2 subfamily.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO13828.
KOiK12613.
OrthoDBiEOG7P5TBG.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR007722. DCP2_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SMARTiSM01125. DCP2. 1 hit.
[Graphical view]
SUPFAMiSSF140586. SSF140586. 1 hit.
SSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFTNATFSQ VLDDLSARFI LNLPAEEQSS VERLCFQIEQ AHWFYEDFIR
60 70 80 90 100
AQNDQLPSLG LRVFSAKLFA HCPLLWKWSK VHEEAFDDFL RYKTRIPVRG
110 120 130 140 150
AIMLDMSMQQ CVLVKGWKAS SGWGFPKGKI DKDESDVDCA IREVYEETGF
160 170 180 190 200
DCSSRINPNE FIDMTIRGQN VRLYIIPGIS LDTRFESRTR KEISKIEWHN
210 220 230 240 250
LMDLPTFKKN KPQTMKNKFY MVIPFLAPLK KWIKKRNIAN NTTKEKNISV
260 270 280 290 300
DVDADASSQL LSLLKSSTAP SDLATPQPST FPQPPVESHS SFDIKQKILH
310 320 330 340 350
LLNEGNEPKS PIQLPPVSNL PLNPPIQSSN SRLSHDNNSF DPFAYLGLDP
360 370 380 390 400
KNPSASFPRV VSQNNMLTNK PVLNNHFQQS MYSNLLKDQN SVQHLFAASD
410 420 430 440 450
MPSPMELPSP STVYHQVFYP PTSTSVSSYG LGKTPQPAYG SSSPYVNGHQ
460 470 480 490 500
TQQISSLPPF QSQTQFLARN SDNSGQSYNS EGDSNSKRLL SMLSQQDTTP
510 520 530 540 550
SSSTLSKEAN VQLANLFLTP NSLETKKFSD NSQGEEISDN LHGESCNNPN
560 570 580 590 600
ANSVHSAQLL QALLHPSATE TKEETPKKTS DSLSLLTLLK SGLPTPANDL
610 620 630 640 650
QNKSQNNERK ASSQVKELEV KNYSKSTDLL KKTLRIPRND EPLEAANQFD
660 670 680 690 700
LLKVSPQQKS EVPPKRNELS QSKLKNRKKK ENSETNKNHV DMSPGFVKIL
710 720 730 740
KRSPLADQKK EDTQESDFKG SDDHFLSYLQ SVVSSNSNGL H
Length:741
Mass (Da):83,234
Last modified:January 1, 1998 - v1
Checksum:iB405257B706BC5C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11648.1.
PIRiT37949.
RefSeqiNP_593780.1. NM_001019209.2.

Genome annotation databases

EnsemblFungiiSPAC19A8.12.1; SPAC19A8.12.1:pep; SPAC19A8.12.
GeneIDi2542503.
KEGGispo:SPAC19A8.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11648.1.
PIRiT37949.
RefSeqiNP_593780.1. NM_001019209.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A6TX-ray2.50A/B1-266[»]
2QKLX-ray2.33B1-95[»]
2QKMX-ray2.80B/D/F/H1-266[»]
4A54NMR-B242-291[»]
5J3TX-ray1.60B1-242[»]
5J3YX-ray3.29B/D1-242[»]
ProteinModelPortaliO13828.
SMRiO13828. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278961. 16 interactions.
DIPiDIP-29009N.
IntActiO13828. 4 interactions.
MINTiMINT-4668291.

Proteomic databases

MaxQBiO13828.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC19A8.12.1; SPAC19A8.12.1:pep; SPAC19A8.12.
GeneIDi2542503.
KEGGispo:SPAC19A8.12.

Organism-specific databases

EuPathDBiFungiDB:SPAC19A8.12.
PomBaseiSPAC19A8.12. dcp2.

Phylogenomic databases

InParanoidiO13828.
KOiK12613.
OrthoDBiEOG7P5TBG.

Enzyme and pathway databases

ReactomeiR-SPO-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.

Miscellaneous databases

EvolutionaryTraceiO13828.
PROiO13828.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR007722. DCP2_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SMARTiSM01125. DCP2. 1 hit.
[Graphical view]
SUPFAMiSSF140586. SSF140586. 1 hit.
SSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human."
    Sakuno T., Araki Y., Ohya Y., Kofuji S., Takahashi S., Hoshino S., Katada T.
    J. Biochem. 136:805-812(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. "Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe."
    She M., Decker C.J., Chen N., Tumati S., Parker R., Song H.
    Nat. Struct. Mol. Biol. 13:63-70(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-266, INTERACTION WITH DCP1, MUTAGENESIS OF ARG-18; PHE-19; PHE-44; GLU-143 AND GLU-192.
  5. "Structural basis of dcp2 recognition and activation by dcp1."
    She M., Decker C.J., Svergun D.I., Round A., Chen N., Muhlrad D., Parker R., Song H.
    Mol. Cell 29:337-349(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1-266 IN COMPLEX WITH DCP1.
  6. "The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex."
    Fromm S.A., Truffault V., Kamenz J., Braun J.E., Hoffmann N.A., Izaurralde E., Sprangers R.
    EMBO J. 31:279-290(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 242-291 IN COMPLEX WITH EDC3.

Entry informationi

Entry nameiDCP2_SCHPO
AccessioniPrimary (citable) accession number: O13828
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.