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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: -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
  • single-stranded RNA binding Source: PomBase

GO - Biological processi

Keywordsi

Molecular functionHydrolase, RNA-binding
Biological processmRNA processing
LigandATP-binding, Manganese, Metal-binding, Nucleotide-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiO13828
PRIDEiO13828

PTM databases

iPTMnetiO13828

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi278961, 17 interactors
DIPiDIP-29009N
IntActiO13828, 4 interactors
MINTiO13828
STRINGi4896.SPAC19A8.12.1

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 5Combined sources4
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 strandi189 – 192Combined sources4
Beta strandi195 – 200Combined sources6
Helixi201 – 203Combined sources3
Turni205 – 207Combined sources3
Beta strandi208 – 210Combined 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[»]
5N2VX-ray3.10B/E1-243[»]
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

Phylogenomic databases

InParanoidiO13828
KOiK12613
OrthoDBiEOG092C10K0

Family and domain databases

Gene3Di1.10.10.1050, 1 hit
InterProiView protein in InterPro
IPR007722 DCP2_BoxA
IPR036189 DCP2_BoxA_sf
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF05026 DCP2, 1 hit
PF00293 NUDIX, 1 hit
SMARTiView protein in SMART
SM01125 DCP2, 1 hit
SUPFAMiSSF140586 SSF140586, 1 hit
SSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462 NUDIX, 1 hit
PS00893 NUDIX_BOX, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiDCP2_SCHPO
AccessioniPrimary (citable) accession number: O13828
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 125 of the entry and version 1 of the sequence. See 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

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