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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)DescriptionActionsGraphical viewLength
Binding sitei167ATP1
Binding sitei220ATP1

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)DescriptionActionsGraphical viewLength
Mutagenesisi18R → A: Abolishes interaction with dcp1. 1 Publication1
Mutagenesisi19F → A: Decreases interaction with dcp1. 1 Publication1
Mutagenesisi44F → A: Decreases interaction with dcp1. 1 Publication1
Mutagenesisi143E → A: Abolishes the decapping activity in vitro. 1 Publication1
Mutagenesisi192E → A: Abolishes the decapping activity in vitro. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003738711 – 741mRNA decapping complex subunit 2Add BLAST741

Proteomic databases

MaxQBiO13828.
PRIDEiO13828.

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 interactors.
DIPiDIP-29009N.
IntActiO13828. 4 interactors.
MINTiMINT-4668291.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 4Combined sources3
Helixi8 – 19Combined sources12
Turni20 – 22Combined sources3
Helixi25 – 28Combined sources4
Helixi31 – 47Combined sources17
Helixi49 – 52Combined sources4
Beta strandi54 – 56Combined sources3
Helixi61 – 69Combined sources9
Helixi73 – 75Combined sources3
Helixi76 – 81Combined sources6
Helixi83 – 90Combined sources8
Beta strandi98 – 104Combined sources7
Beta strandi110 – 115Combined sources6
Beta strandi117 – 120Combined sources4
Beta strandi126 – 129Combined sources4
Beta strandi132 – 134Combined sources3
Helixi136 – 148Combined sources13
Turni153 – 155Combined sources3
Beta strandi161 – 166Combined sources6
Beta strandi169 – 176Combined sources8
Beta strandi195 – 200Combined sources6
Helixi201 – 203Combined sources3
Helixi205 – 207Combined sources3
Beta strandi209 – 211Combined sources3
Turni218 – 222Combined sources5
Helixi223 – 240Combined sources18
Beta strandi245 – 247Combined sources3
Helixi255 – 265Combined sources11
Beta strandi272 – 274Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KQ1X-ray3.00B/E1-244[»]
5KQ4X-ray2.56B/E1-244[»]
ProteinModelPortaliO13828.
SMRiO13828.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO13828.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini94 – 227Nudix hydrolasePROSITE-ProRule annotationAdd BLAST134

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi128 – 149Nudix boxAdd BLAST22

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiO13828.
KOiK12613.
OrthoDBiEOG092C10K0.

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
PDB 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[»]
5KQ1X-ray3.00B/E1-244[»]
5KQ4X-ray2.56B/E1-244[»]
ProteinModelPortaliO13828.
SMRiO13828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiO13828.
PRIDEiO13828.

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.
OrthoDBiEOG092C10K0.

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...

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: November 30, 2016
This is version 114 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.