DCP2_YEAS7
ID DCP2_YEAS7 Reviewed; 970 AA.
AC A6ZRW5; B0KZW2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=mRNA-decapping enzyme subunit 2;
DE EC=3.-.-.-;
DE AltName: Full=Protein PSU1;
GN Name=DCP2; Synonyms=PSU1; ORFNames=SCY_4676;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 composed of DCP1 and DCP2.
CC Interacts with mRNA, LSM2, LSM4 and LSM8. {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; AAFW02000067; EDN62697.1; -; Genomic_DNA.
DR EMBL; EF125227; ABN58638.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRW5; -.
DR BMRB; A6ZRW5; -.
DR SMR; A6ZRW5; -.
DR PRIDE; A6ZRW5; -.
DR EnsemblFungi; EDN62697; EDN62697; SCY_4676.
DR HOGENOM; CLU_009571_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
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 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; Phosphoprotein; RNA-binding.
FT CHAIN 1..970
FT /note="mRNA-decapping enzyme subunit 2"
FT /id="PRO_0000378320"
FT DOMAIN 101..228
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 287..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..155
FT /note="Nudix box"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..679
FT /note="Basic and acidic 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"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 677
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53550"
SQ SEQUENCE 970 AA; 108657 MW; 0FA59DF06D5ED970 CRC64;
MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW FYTDFIKLMN
PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK KSIPVRGAAI FNENLSKILL
VQGTESDSWS FPRGKISKDE NDIDCCIREV KEEIGFDLTD YIDDNQFIER NIQGKNYKIF
LISGVSEVFN FKPQVRNEID KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ
IKNEDQLKSY AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE
HQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM ANVFMSNPQL
FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP NPMAFGVPNM HNLSGPAVSQ
PFSLPPAPLP RDSGYSSSSP GQLLDILNSK KPDSNVQSSK KPKLKILQRG TDLNSIKQNN
NDETAHSNSQ ALLDLLKKPT SSQKTHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE
TARDERTSLN VDIGVNVMPS EKDSRRSQKE KPRSDANKTN LNASAESNSV EWGPGKSSPS
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQG NSKLISQDIL
KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP KVKILKRGET FASLANDKKA
FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE
NASTSSINDA NASELLGMLK QKEKDITAPK QPYNVDSYSQ KNPAKGLLNI LKKNNSTGYP
RTEGGPSSEM PTSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI
LHGNKNSSTF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF DVRSNGTSGS
NELLSILHRK
