DCP2_YEAST
ID DCP2_YEAST Reviewed; 970 AA.
AC P53550; B0KZS6; B0KZU4; B0KZW2; B0KZY0; B0KZY9; B0KZZ8; B0L007; D6W164;
AC Q6LCS6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=m7GpppN-mRNA hydrolase {ECO:0000305};
DE EC=3.6.1.62 {ECO:0000269|PubMed:12554866};
DE AltName: Full=Protein PSU1;
DE AltName: Full=mRNA-decapping enzyme subunit 2 {ECO:0000303|PubMed:10508173};
GN Name=DCP2 {ECO:0000303|PubMed:10508173}; Synonyms=PSU1;
GN OrderedLocusNames=YNL118C {ECO:0000312|SGD:S000005062}; ORFNames=N1917;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7883168; DOI=10.1101/gad.9.4.437;
RA He F., Jacobson A.;
RT "Identification of a novel component of the nonsense-mediated mRNA decay
RT pathway by use of an interacting protein screen.";
RL Genes Dev. 9:437-454(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24657 / D273-10B;
RA Tzagoloff A.A.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-188; ASN-288 DEL;
RP HIS-301; PRO-319; ASN-494; THR-505; ASP-522; THR-547; ARG-567; SER-574;
RP ASN-577; SER-622; GLY-650; SER-740; ALA-807; PRO-823; ASN-835; VAL-844;
RP PRO-851; ILE-854; GLN-864; SER-865; THR-909; LEU-945 AND GLU-951.
RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270,
RC YJM 320, YJM 326, YJM 339, YJM 627, and YJM230;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP INTERACTION WITH EDC3.
RX PubMed=18678652; DOI=10.1128/mcb.00761-08;
RA Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.;
RT "Crystal structure of human Edc3 and its functional implications.";
RL Mol. Cell. Biol. 28:5965-5976(2008).
RN [8]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [9]
RP FUNCTION, AND INTERACTION WITH DCP1.
RX PubMed=10508173; DOI=10.1093/emboj/18.19.5411;
RA Dunckley T., Parker R.;
RT "The DCP2 protein is required for mRNA decapping in Saccharomyces
RT cerevisiae and contains a functional MutT motif.";
RL EMBO J. 18:5411-5422(1999).
RN [10]
RP INTERACTION WITH LSM2; LSM4 AND LSM8.
RX PubMed=10900456;
RX DOI=10.1002/1097-0061(20000630)17:2<95::aid-yea16>3.0.co;2-h;
RA Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A.,
RA Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P.;
RT "Genome-wide protein interaction screens reveal functional networks
RT involving Sm-like proteins.";
RL Yeast 17:95-110(2000).
RN [11]
RP FUNCTION, MUTAGENESIS OF ASN-60; ILE-68 AND ASP-142, AND INTERACTION WITH
RP EDC1.
RX PubMed=11139489; DOI=10.1093/genetics/157.1.27;
RA Dunckley T., Tucker M., Parker R.;
RT "Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in
RT Saccharomyces cerevisiae.";
RL Genetics 157:27-37(2001).
RN [12]
RP INTERACTION WITH MRNA, AND FUNCTION OF THE DCP1-DCP2 COMPLEX.
RX PubMed=11741542; DOI=10.1016/s1097-2765(01)00395-1;
RA Tharun S., Parker R.;
RT "Targeting an mRNA for decapping: displacement of translation factors and
RT association of the Lsm1p-7p complex on deadenylated yeast mRNAs.";
RL Mol. Cell 8:1075-1083(2001).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP FUNCTION OF THE DCP1-DCP2 COMPLEX, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=12554866; DOI=10.1261/rna.2151403;
RA Steiger M., Carr-Schmid A., Schwartz D.C., Kiledjian M., Parker R.;
RT "Analysis of recombinant yeast decapping enzyme.";
RL RNA 9:231-238(2003).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=12730603; DOI=10.1126/science.1082320;
RA Sheth U., Parker R.;
RT "Decapping and decay of messenger RNA occur in cytoplasmic processing
RT bodies.";
RL Science 300:805-808(2003).
RN [16]
RP INTERACTION WITH DCP1.
RX PubMed=14758354; DOI=10.1038/nsmb730;
RA She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H.;
RT "Crystal structure of Dcp1p and its functional implications in mRNA
RT decapping.";
RL Nat. Struct. Mol. Biol. 11:249-256(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-682 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; THR-677; SER-679;
RP SER-682; SER-751; SER-771; SER-773 AND SER-778, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26098573; DOI=10.1038/ncb3189;
RA Hu G., McQuiston T., Bernard A., Park Y.D., Qiu J., Vural A., Zhang N.,
RA Waterman S.R., Blewett N.H., Myers T.G., Maraia R.J., Kehrl J.H., Uzel G.,
RA Klionsky D.J., Williamson P.R.;
RT "A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation
RT regulates autophagy.";
RL Nat. Cell Biol. 17:930-942(2015).
RN [20]
RP STRUCTURE BY NMR OF 100-245.
RX PubMed=18280238; DOI=10.1016/j.molcel.2007.11.027;
RA Deshmukh M.V., Jones B.N., Quang-Dang D.U., Flinders J., Floor S.N.,
RA Kim C., Jemielity J., Kalek M., Darzynkiewicz E., Gross J.D.;
RT "mRNA decapping is promoted by an RNA-binding channel in Dcp2.";
RL Mol. Cell 29:324-336(2008).
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 (PubMed:10508173, PubMed:11139489,
CC PubMed:11741542). Removes the 7-methyl guanine cap structure from mRNA
CC molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP
CC (PubMed:12554866). Decapping is the major pathway of mRNA degradation
CC in yeast and occurs through deadenylation, decapping and subsequent 5'
CC to 3' exonucleolytic decay of the transcript body (PubMed:10508173,
CC PubMed:11139489, PubMed:11741542). Blocks autophagy in nutrient-rich
CC conditions by repressing the expression of ATG-related genes through
CC degradation of their transcripts (PubMed:19779198).
CC {ECO:0000269|PubMed:10508173, ECO:0000269|PubMed:11139489,
CC ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:12554866}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000269|PubMed:12554866};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000269|PubMed:12554866};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12554866};
CC -!- SUBUNIT: Component of the decapping complex composed of DCP1 and DCP2
CC (PubMed:10508173, PubMed:11741542, PubMed:14758354). Interacts with
CC mRNA, LSM2, LSM4 and LSM8 (PubMed:10900456). Interacts with EDC3
CC (PubMed:18678652). {ECO:0000269|PubMed:10508173,
CC ECO:0000269|PubMed:10900456, ECO:0000269|PubMed:11139489,
CC ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:14758354,
CC ECO:0000269|PubMed:18678652}.
CC -!- INTERACTION:
CC P53550; Q12517: DCP1; NbExp=5; IntAct=EBI-270, EBI-38519;
CC P53550; P39998: EDC3; NbExp=6; IntAct=EBI-270, EBI-22300;
CC P53550; P25644: PAT1; NbExp=3; IntAct=EBI-270, EBI-204;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:12730603}.
CC -!- DISRUPTION PHENOTYPE: Increases autophagy activity through accumulation
CC of autophagy-related proteins in nutrient-replete conditions
CC (PubMed:19779198).
CC -!- MISCELLANEOUS: Present with 8530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; U31377; AAC99860.1; -; Genomic_DNA.
DR EMBL; L43065; AAA68866.1; -; Genomic_DNA.
DR EMBL; EF125216; ABN58539.1; -; Genomic_DNA.
DR EMBL; EF125217; ABN58548.1; -; Genomic_DNA.
DR EMBL; EF125218; ABN58557.1; -; Genomic_DNA.
DR EMBL; EF125219; ABN58566.1; -; Genomic_DNA.
DR EMBL; EF125220; ABN58578.1; -; Genomic_DNA.
DR EMBL; EF125221; ABN58584.1; -; Genomic_DNA.
DR EMBL; EF125222; ABN58593.1; -; Genomic_DNA.
DR EMBL; EF125223; ABN58602.1; -; Genomic_DNA.
DR EMBL; EF125224; ABN58611.1; -; Genomic_DNA.
DR EMBL; EF125225; ABN58620.1; -; Genomic_DNA.
DR EMBL; EF125226; ABN58629.1; -; Genomic_DNA.
DR EMBL; EF125228; ABN58647.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93389.1; -; Genomic_DNA.
DR EMBL; Z71394; CAA95998.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10430.1; -; Genomic_DNA.
DR PIR; S63059; S63059.
DR RefSeq; NP_014281.1; NM_001182956.1.
DR PDB; 2JVB; NMR; -; A=100-245.
DR PDB; 4K6E; X-ray; 2.10 A; A=102-245.
DR PDB; 4KG3; X-ray; 1.70 A; A/B/C=100-245.
DR PDB; 4KG4; X-ray; 1.80 A; A/B=100-245.
DR PDB; 5LM5; X-ray; 2.60 A; C/D=437-450.
DR PDB; 5LMF; X-ray; 2.15 A; C/D=484-500.
DR PDB; 5LMG; X-ray; 1.89 A; C/D=957-970.
DR PDB; 6Y3Z; X-ray; 3.49 A; A=1-271.
DR PDBsum; 2JVB; -.
DR PDBsum; 4K6E; -.
DR PDBsum; 4KG3; -.
DR PDBsum; 4KG4; -.
DR PDBsum; 5LM5; -.
DR PDBsum; 5LMF; -.
DR PDBsum; 5LMG; -.
DR PDBsum; 6Y3Z; -.
DR AlphaFoldDB; P53550; -.
DR BMRB; P53550; -.
DR SMR; P53550; -.
DR BioGRID; 35708; 662.
DR ComplexPortal; CPX-1628; RNA decapping complex, DCP1-DCP2.
DR DIP; DIP-969N; -.
DR IntAct; P53550; 45.
DR MINT; P53550; -.
DR STRING; 4932.YNL118C; -.
DR iPTMnet; P53550; -.
DR MaxQB; P53550; -.
DR PaxDb; P53550; -.
DR PRIDE; P53550; -.
DR EnsemblFungi; YNL118C_mRNA; YNL118C; YNL118C.
DR GeneID; 855605; -.
DR KEGG; sce:YNL118C; -.
DR SGD; S000005062; DCP2.
DR VEuPathDB; FungiDB:YNL118C; -.
DR eggNOG; KOG2937; Eukaryota.
DR GeneTree; ENSGT00390000018878; -.
DR HOGENOM; CLU_009571_0_0_1; -.
DR InParanoid; P53550; -.
DR OMA; EPFANNK; -.
DR BioCyc; YEAST:G3O-33140-MON; -.
DR BRENDA; 3.6.1.62; 984.
DR Reactome; R-SCE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR ChiTaRS; DCP2; yeast.
DR EvolutionaryTrace; P53550; -.
DR PRO; PR:P53550; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53550; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IDA:SGD.
DR GO; GO:0098745; C:Dcp1-Dcp2 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0016787; F:hydrolase activity; IDA:SGD.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:SGD.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:SGD.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IDA:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW mRNA processing; Nonsense-mediated mRNA decay; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..970
FT /note="m7GpppN-mRNA hydrolase"
FT /id="PRO_0000057054"
FT DOMAIN 101..228
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 302..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 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..155
FT /note="Nudix box"
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 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..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..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 COMPBIAS 840..867
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"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 677
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 188
FT /note="V -> A (in strain: YJM339)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 288
FT /note="Missing (in strain: V1-09, YJM269, YJM270, YJM326,
FT YJM339, YJM627 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 301
FT /note="L -> H (in strain: YJM280, YJM 20 and YJM339)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 319
FT /note="S -> P (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 494
FT /note="D -> N (in strain: YJM339)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 505
FT /note="I -> T (in strain: SK1, V1-09, YJM269, YJM270,
FT YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 522
FT /note="G -> D (in strain: YJM269, YJM270, YJM326 and
FT YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 547
FT /note="N -> T (in strain: YJM280 and YJM320)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 567
FT /note="S -> R (in strain: YJM269, YJM270, YJM326 and
FT YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 574
FT /note="N -> S (in strain: YJM269, YJM270, YJM280, YJM320,
FT YJM326 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 577
FT /note="S -> N (in strain: V1-09, YJM269, YJM270, YJM280,
FT YJM320, YJM326, YJM339 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 622
FT /note="G -> S (in strain: V1-09 and YJM339)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 650
FT /note="D -> G (in strain: YJM280 and YJM320)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 740
FT /note="P -> S (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 807
FT /note="T -> A (in strain: YJM 69, YJM270, YJM326 and
FT YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 823
FT /note="S -> P (in strain: YJM269, YJM270, YJM280, YJM320,
FT YJM326 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 835
FT /note="D -> N (in strain: YJM280 and YJM320)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 844
FT /note="G -> V (in strain: V1-09)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 851
FT /note="S -> P (in strain: YJM280, YJM320 and YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 854
FT /note="M -> I (in strain: YJM269, YJM270, YJM326 and
FT YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 864
FT /note="E -> Q (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 865
FT /note="L -> S (in strain: YJM269, YJM270, YJM326 and
FT YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 866
FT /note="D -> A (in strain: YJM627)"
FT VARIANT 909
FT /note="A -> T (in strain: YJM280 and YJM320)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 945
FT /note="I -> L (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 951
FT /note="D -> E (in strain: V1-09)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT MUTAGEN 60
FT /note="N->D: In DCP2-7; impairs mRNA decay at 37 degrees
FT Celsius; when associated with V-68 and V-142."
FT /evidence="ECO:0000269|PubMed:11139489"
FT MUTAGEN 68
FT /note="I->V: In DCP2-7; impairs mRNA decay at 37 degrees
FT Celsius; when associated with D-60 and V-142."
FT /evidence="ECO:0000269|PubMed:11139489"
FT MUTAGEN 142
FT /note="D->V: In DCP2-7; impairs mRNA decay at 37 degrees
FT Celsius; when associated with D-60 and V-68."
FT /evidence="ECO:0000269|PubMed:11139489"
FT CONFLICT 425
FT /note="P -> L (in Ref. 2; AAA68866)"
FT /evidence="ECO:0000305"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2JVB"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:4KG3"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2JVB"
FT STRAND 194..206
FT /evidence="ECO:0007829|PDB:4KG3"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:4KG3"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4KG3"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4KG3"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:4KG3"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4KG3"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 440..449
FT /evidence="ECO:0007829|PDB:5LM5"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:5LMF"
FT HELIX 958..967
FT /evidence="ECO:0007829|PDB:5LMG"
SQ SEQUENCE 970 AA; 108667 MW; D53CA2C5A546FA4A 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
LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM ANVFMSNPQL
FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP NPMAFGVPNM HNLSGPAVSQ
PFSLPPAPLP RDSGYSSSSP GQLLDILNSK KPDSNVQSSK KPKLKILQRG TDLNSIKQNN
NDETAHSNSQ ALLDLLKKPT SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE
TARDERNSLN VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD NSKLISQDIL
KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP KVKILKRGET FASLANDKKA
FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE
NASTSSINDA NASELLGMLK QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP
RTEGGPSSEM STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI
LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF DVRSNGTSGS
NELLSILHRK
