DCP2_ASHGO
ID DCP2_ASHGO Reviewed; 880 AA.
AC Q75BK1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=mRNA-decapping enzyme subunit 2;
DE EC=3.-.-.-;
GN Name=DCP2; OrderedLocusNames=ACR270W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the decapping complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=Is
CC 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016816; AAS51496.1; -; Genomic_DNA.
DR RefSeq; NP_983672.1; NM_209025.1.
DR AlphaFoldDB; Q75BK1; -.
DR SMR; Q75BK1; -.
DR STRING; 33169.AAS51496; -.
DR EnsemblFungi; AAS51496; AAS51496; AGOS_ACR270W.
DR GeneID; 4619807; -.
DR KEGG; ago:AGOS_ACR270W; -.
DR eggNOG; KOG2937; Eukaryota.
DR HOGENOM; CLU_009571_0_0_1; -.
DR InParanoid; Q75BK1; -.
DR OMA; FEEAQWF; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IEA:EnsemblFungi.
DR GO; GO:0098745; C:Dcp1-Dcp2 complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IEA:EnsemblFungi.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
DR CDD; cd03672; Dcp2p; 1.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; mRNA processing;
KW Nonsense-mediated mRNA decay; Reference proteome; RNA-binding.
FT CHAIN 1..880
FT /note="mRNA-decapping enzyme subunit 2"
FT /id="PRO_0000232999"
FT DOMAIN 101..227
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 293..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..155
FT /note="Nudix box"
FT COMPBIAS 449..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 880 AA; 97262 MW; 2F3F2CC740818F0E CRC64;
MSLPLRNPLD SVSLERALED LIVRFIINVP PEDLATVERE LFHFEEAQWF YTDFVKLTNP
HLPNMKFKTF ASYVISLCPL VWKWQDVNPE EALQKFSKYK KSIPVRGAAI FNETLNKILL
VKGTESDSWS FPRGKISKDE DDVDCCIREV MEEIGFDLTN YVLEDQYIER NIGGKNYKIY
LVKGVPQDFA FKPQVRNEIE KIEWRDFWKL SRSIHKSNNK FYLVSSMVKP LSLWVKKQKQ
IQGEEQLKQY AEEQLKLLLG IGTQEEAADP GRDLLNMLQS SVGQKKPLVF SDDESQASIS
TSAPTTVPPA PSTANSQSVQ PIAAGAYAGY PFPFPQYPIP GMQTINPFQF VQSSHQGVFA
THSTFTTSHQ YPQAQAPQTQ QPVPGAVVYP VQSQLQQAYQ PPHTPVVKPS VIEDRAPHSK
QLLELLKNPR KPEVEDESTA KTLLKLLKNP TKENRTSANT VPSSKGAVSG PSGGRSISGQ
SIDTANLPSG MASSMGAKST AIPLYSPRSS LSEMTLPDEP LGGYEEFESS SEEEQGEELA
YMNLQEPTSS VMESNAKVEN NTLDNISHVD TSGNLSTRSL QSEKTEKSKP TAKPKIKLLK
RGETLTPLTP SISSQTATSE SSAAGPTVPS EKDVSSRIQN SQGNELLDVL KSKAQPEPSV
ASTSPAKELL NTLNKPQGSV YQNLLFGANH RKSDDESSPR HSPVSQQART HEFLNLLKRP
QAKAENEELQ SVLLTPPANS GMVQNSSTLP NIPYGNLHQD QAAALLFPQQ PPQFQQPYAA
TNTNSKELLA ILRKPASNQQ KQLHEQTPAN PVDQPTTLAS EQQNLVKQQI SNPSQSLQQG
TPLQQPQPQH TQSPSNLHVT GNTAAAQELL GMLRKSRVVP
