DCP2_SCHPO
ID DCP2_SCHPO Reviewed; 741 AA.
AC O13828;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=mRNA decapping complex subunit 2;
DE EC=3.-.-.-;
GN Name=dcp2; ORFNames=SPAC19A8.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=15671491; DOI=10.1093/jb/mvh190;
RA Sakuno T., Araki Y., Ohya Y., Kofuji S., Takahashi S., Hoshino S.,
RA Katada T.;
RT "Decapping reaction of mRNA requires Dcp1 in fission yeast: its
RT characterization in different species from yeast to human.";
RL J. Biochem. 136:805-812(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-266, INTERACTION WITH DCP1, AND
RP MUTAGENESIS OF ARG-18; PHE-19; PHE-44; GLU-143 AND GLU-192.
RX PubMed=16341225; DOI=10.1038/nsmb1033;
RA She M., Decker C.J., Chen N., Tumati S., Parker R., Song H.;
RT "Crystal structure and functional analysis of Dcp2p from
RT Schizosaccharomyces pombe.";
RL Nat. Struct. Mol. Biol. 13:63-70(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1-266 IN COMPLEX WITH DCP1.
RX PubMed=18280239; DOI=10.1016/j.molcel.2008.01.002;
RA She M., Decker C.J., Svergun D.I., Round A., Chen N., Muhlrad D.,
RA Parker R., Song H.;
RT "Structural basis of dcp2 recognition and activation by dcp1.";
RL Mol. Cell 29:337-349(2008).
RN [6]
RP STRUCTURE BY NMR OF 242-291 IN COMPLEX WITH EDC3.
RX PubMed=22085934; DOI=10.1038/emboj.2011.408;
RA Fromm S.A., Truffault V., Kamenz J., Braun J.E., Hoffmann N.A.,
RA Izaurralde E., Sprangers R.;
RT "The structural basis of Edc3- and Scd6-mediated activation of the
RT Dcp1:Dcp2 mRNA decapping complex.";
RL EMBO J. 31:279-290(2012).
CC -!- FUNCTION: Catalytic component of the decapping complex necessary for
CC the degradation of mRNAs, both in normal mRNA turnover and in nonsense-
CC mediated mRNA decay. Removes the 7-methyl guanine cap structure from
CC mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.
CC Decapping is the major pathway of mRNA degradation in yeast. It occurs
CC through deadenylation, decapping and subsequent 5' to 3' exonucleolytic
CC decay of the transcript body. {ECO:0000269|PubMed:15671491}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the decapping complex composed of dcp1 and dcp2
CC (By similarity). Interacts with edc3. {ECO:0000250,
CC ECO:0000269|PubMed:16341225, ECO:0000269|PubMed:18280239,
CC ECO:0000269|PubMed:22085934}.
CC -!- INTERACTION:
CC O13828; Q9P805: dcp1; NbExp=7; IntAct=EBI-3647323, EBI-7557105;
CC O13828; O94752: edc3; NbExp=5; IntAct=EBI-3647323, EBI-7556871;
CC O13828; Q9HGL3: sum2; NbExp=4; IntAct=EBI-3647323, EBI-1117052;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16823372}.
CC Note=Is concentrated in several cytoplasmic foci called P bodies (or
CC cytoplasmic processing bodies) which represent sites of mRNA decapping
CC and 5' to 3' exonucleotidic decay.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11648.1; -; Genomic_DNA.
DR PIR; T37949; T37949.
DR RefSeq; NP_593780.1; NM_001019209.2.
DR PDB; 2A6T; X-ray; 2.50 A; A/B=1-266.
DR PDB; 2QKL; X-ray; 2.33 A; B=1-95.
DR PDB; 2QKM; X-ray; 2.80 A; B/D/F/H=1-266.
DR PDB; 4A54; NMR; -; B=242-291.
DR PDB; 5J3T; X-ray; 1.60 A; B=1-242.
DR PDB; 5J3Y; X-ray; 3.29 A; B/D=1-242.
DR PDB; 5KQ1; X-ray; 3.00 A; B/E=1-244.
DR PDB; 5KQ4; X-ray; 2.56 A; B/E=1-244.
DR PDB; 5N2V; X-ray; 3.10 A; B/E=1-243.
DR PDBsum; 2A6T; -.
DR PDBsum; 2QKL; -.
DR PDBsum; 2QKM; -.
DR PDBsum; 4A54; -.
DR PDBsum; 5J3T; -.
DR PDBsum; 5J3Y; -.
DR PDBsum; 5KQ1; -.
DR PDBsum; 5KQ4; -.
DR PDBsum; 5N2V; -.
DR AlphaFoldDB; O13828; -.
DR BMRB; O13828; -.
DR SMR; O13828; -.
DR BioGRID; 278961; 18.
DR DIP; DIP-29009N; -.
DR IntAct; O13828; 4.
DR MINT; O13828; -.
DR STRING; 4896.SPAC19A8.12.1; -.
DR iPTMnet; O13828; -.
DR MaxQB; O13828; -.
DR PaxDb; O13828; -.
DR PRIDE; O13828; -.
DR EnsemblFungi; SPAC19A8.12.1; SPAC19A8.12.1:pep; SPAC19A8.12.
DR GeneID; 2542503; -.
DR KEGG; spo:SPAC19A8.12; -.
DR PomBase; SPAC19A8.12; dcp2.
DR VEuPathDB; FungiDB:SPAC19A8.12; -.
DR eggNOG; KOG2937; Eukaryota.
DR HOGENOM; CLU_384097_0_0_1; -.
DR InParanoid; O13828; -.
DR BRENDA; 3.6.1.62; 5613.
DR EvolutionaryTrace; O13828; -.
DR PRO; PR:O13828; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0098745; C:Dcp1-Dcp2 complex; IDA:PomBase.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000932; C:P-body; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; TAS:PomBase.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:PomBase.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:PomBase.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IC:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034428; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3'; NAS:PomBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; Dcp2p; 1.
DR DisProt; DP01482; -.
DR Gene3D; 1.10.10.1050; -; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; SSF140586; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Reference proteome; RNA-binding.
FT CHAIN 1..741
FT /note="mRNA decapping complex subunit 2"
FT /id="PRO_0000373871"
FT DOMAIN 94..227
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 268..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 128..149
FT /note="Nudix box"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 18
FT /note="R->A: Abolishes interaction with dcp1."
FT /evidence="ECO:0000269|PubMed:16341225"
FT MUTAGEN 19
FT /note="F->A: Decreases interaction with dcp1."
FT /evidence="ECO:0000269|PubMed:16341225"
FT MUTAGEN 44
FT /note="F->A: Decreases interaction with dcp1."
FT /evidence="ECO:0000269|PubMed:16341225"
FT MUTAGEN 143
FT /note="E->A: Abolishes the decapping activity in vitro."
FT /evidence="ECO:0000269|PubMed:16341225"
FT MUTAGEN 192
FT /note="E->A: Abolishes the decapping activity in vitro."
FT /evidence="ECO:0000269|PubMed:16341225"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:5KQ4"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:5J3T"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2A6T"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:5J3T"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5N2V"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5J3T"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5KQ4"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5KQ1"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2QKM"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:2QKM"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4A54"
SQ SEQUENCE 741 AA; 83234 MW; B405257B706BC5C0 CRC64;
MSFTNATFSQ VLDDLSARFI LNLPAEEQSS VERLCFQIEQ AHWFYEDFIR AQNDQLPSLG
LRVFSAKLFA HCPLLWKWSK VHEEAFDDFL RYKTRIPVRG AIMLDMSMQQ CVLVKGWKAS
SGWGFPKGKI DKDESDVDCA IREVYEETGF DCSSRINPNE FIDMTIRGQN VRLYIIPGIS
LDTRFESRTR KEISKIEWHN LMDLPTFKKN KPQTMKNKFY MVIPFLAPLK KWIKKRNIAN
NTTKEKNISV DVDADASSQL LSLLKSSTAP SDLATPQPST FPQPPVESHS SFDIKQKILH
LLNEGNEPKS PIQLPPVSNL PLNPPIQSSN SRLSHDNNSF DPFAYLGLDP KNPSASFPRV
VSQNNMLTNK PVLNNHFQQS MYSNLLKDQN SVQHLFAASD MPSPMELPSP STVYHQVFYP
PTSTSVSSYG LGKTPQPAYG SSSPYVNGHQ TQQISSLPPF QSQTQFLARN SDNSGQSYNS
EGDSNSKRLL SMLSQQDTTP SSSTLSKEAN VQLANLFLTP NSLETKKFSD NSQGEEISDN
LHGESCNNPN ANSVHSAQLL QALLHPSATE TKEETPKKTS DSLSLLTLLK SGLPTPANDL
QNKSQNNERK ASSQVKELEV KNYSKSTDLL KKTLRIPRND EPLEAANQFD LLKVSPQQKS
EVPPKRNELS QSKLKNRKKK ENSETNKNHV DMSPGFVKIL KRSPLADQKK EDTQESDFKG
SDDHFLSYLQ SVVSSNSNGL H
