DCP1_YEAST
ID DCP1_YEAST Reviewed; 231 AA.
AC Q12517; D6W1S0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=mRNA-decapping enzyme subunit 1;
GN Name=DCP1; OrderedLocusNames=YOL149W;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553699; DOI=10.1002/yea.320111308;
RA Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J.,
RA Gancedo C., Arino J.;
RT "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT chromosome XV containing seven new open reading frames.";
RL Yeast 11:1281-1288(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 1-14, FUNCTION, AND MUTAGENESIS OF TRP-56.
RX PubMed=8757137; DOI=10.1038/382642a0;
RA Beelman C.A., Stevens A., Caponigro G., LaGrandeur T.E., Hatfield L.,
RA Fortner D.M., Parker R.;
RT "An essential component of the decapping enzyme required for normal rates
RT of mRNA turnover.";
RL Nature 382:642-646(1996).
RN [6]
RP FUNCTION.
RX PubMed=8816497; DOI=10.1128/mcb.16.10.5830;
RA Hatfield L., Beelman C.A., Stevens A., Parker R.;
RT "Mutations in trans-acting factors affecting mRNA decapping in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:5830-5838(1996).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=9482745; DOI=10.1093/emboj/17.5.1487;
RA LaGrandeur T.E., Parker R.;
RT "Isolation and characterization of Dcp1p, the yeast mRNA decapping
RT enzyme.";
RL EMBO J. 17:1487-1496(1998).
RN [8]
RP FUNCTION.
RX PubMed=9482746; DOI=10.1093/emboj/17.5.1497;
RA Anderson J.S.J., Parker R.P.;
RT "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA
RT turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases
RT of the exosome complex.";
RL EMBO J. 17:1497-1506(1998).
RN [9]
RP FUNCTION, AND INTERACTION WITH DCP2.
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 FUNCTION, AND MUTAGENESIS OF 16-GLU--LYS-20; 29-ARG--ASP-31; TYR-47;
RP 48-LYS--ASP-50; TRP-56; ARG-70; GLY-156; 187-LYS-ASP-188; TRP-204 AND
RP 216-GLU--LYS-219.
RX PubMed=10101156; DOI=10.1093/genetics/151.4.1273;
RA Tharun S., Parker R.;
RT "Analysis of mutations in the yeast mRNA decapping enzyme.";
RL Genetics 151:1273-1285(1999).
RN [11]
RP FUNCTION.
RX PubMed=10075882; DOI=10.1006/meth.1998.0706;
RA Zhang S., Williams C.J., Wormington M., Stevens A., Peltz S.W.;
RT "Monitoring mRNA decapping activity.";
RL Methods 17:46-51(1999).
RN [12]
RP FUNCTION.
RX PubMed=10564284; DOI=10.1091/mbc.10.11.3971;
RA Muhlrad D., Parker R.;
RT "Recognition of yeast mRNAs as 'nonsense containing' leads to both
RT inhibition of mRNA translation and mRNA degradation: implications for the
RT control of mRNA decapping.";
RL Mol. Biol. Cell 10:3971-3978(1999).
RN [13]
RP FUNCTION.
RX PubMed=10409716; DOI=10.1128/mcb.19.8.5247;
RA Schwartz D.C., Parker R.;
RT "Mutations in translation initiation factors lead to increased rates of
RT deadenylation and decapping of mRNAs in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:5247-5256(1999).
RN [14]
RP FUNCTION, AND INTERACTION WITH PAB1 AND TIF4632.
RX PubMed=10944120; DOI=10.1093/emboj/19.16.4372;
RA Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.;
RT "The eukaryotic mRNA decapping protein Dcp1 interacts physically and
RT functionally with the eIF4F translation initiation complex.";
RL EMBO J. 19:4372-4382(2000).
RN [15]
RP INTERACTION WITH LSM1; LSM2; LSM3; LSM4; LSM5; LSM6 AND LSM7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10761922; DOI=10.1038/35006676;
RA Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R.;
RT "Yeast Sm-like proteins function in mRNA decapping and decay.";
RL Nature 404:515-518(2000).
RN [16]
RP INTERACTION WITH LSM4.
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 [17]
RP FUNCTION, AND INTERACTION WITH 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 [18]
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 [19]
RP INTERACTION WITH DHH1.
RX PubMed=11780629; DOI=10.1017/s135583820101994x;
RA Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R.;
RT "The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts
RT with both the decapping and deadenylase complexes.";
RL RNA 7:1717-1727(2001).
RN [20]
RP FUNCTION, AND ACTIVATION BY DHH1.
RX PubMed=12032091; DOI=10.1093/emboj/21.11.2788;
RA Fischer N., Weis K.;
RT "The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1.";
RL EMBO J. 21:2788-2797(2002).
RN [21]
RP FUNCTION.
RX PubMed=12054793; DOI=10.1016/s0022-2836(02)00162-6;
RA Ramirez C.V., Vilela C., Berthelot K., McCarthy J.E.G.;
RT "Modulation of eukaryotic mRNA stability via the cap-binding translation
RT complex eIF4F.";
RL J. Mol. Biol. 318:951-962(2002).
RN [22]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [23]
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 [24]
RP FUNCTION OF THE DCP1-DCP2 COMPLEX.
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 [25]
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 [26]
RP FUNCTION.
RX PubMed=15024087; DOI=10.1128/mcb.24.7.2998-3010.2004;
RA Holmes L.E.A., Campbell S.G., De Long S.K., Sachs A.B., Ashe M.P.;
RT "Loss of translational control in yeast compromised for the major mRNA
RT decay pathway.";
RL Mol. Cell. Biol. 24:2998-3010(2004).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), INTERACTION WITH DCP2, AND
RP MUTAGENESIS OF 29-ARG--ASP-31; 32-PRO--ILE-34; 37-LEU-LEU-38; TRP-56;
RP ARG-70; LEU-217 AND LEU-221.
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).
CC -!- FUNCTION: Component of the decapping complex necessary for the
CC 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. DCP1 is activated by the DEAD-box
CC helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the
CC mRNA. {ECO:0000269|PubMed:10075882, ECO:0000269|PubMed:10101156,
CC ECO:0000269|PubMed:10409716, ECO:0000269|PubMed:10508173,
CC ECO:0000269|PubMed:10564284, ECO:0000269|PubMed:10944120,
CC ECO:0000269|PubMed:11139489, ECO:0000269|PubMed:11741542,
CC ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:12054793,
CC ECO:0000269|PubMed:12554866, ECO:0000269|PubMed:15024087,
CC ECO:0000269|PubMed:8757137, ECO:0000269|PubMed:8816497,
CC ECO:0000269|PubMed:9482745, ECO:0000269|PubMed:9482746}.
CC -!- SUBUNIT: Component of the decapping complex composed of DCP1 and DCP2.
CC Interacts with mRNAs, DHH1, LSM1, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7,
CC and the cap-binding proteins PAB1 and TIF4632/eIF-4G.
CC {ECO:0000269|PubMed:10508173, ECO:0000269|PubMed:10761922,
CC ECO:0000269|PubMed:10900456, ECO:0000269|PubMed:10944120,
CC ECO:0000269|PubMed:11139489, ECO:0000269|PubMed:11741542,
CC ECO:0000269|PubMed:11780629, ECO:0000269|PubMed:14758354}.
CC -!- INTERACTION:
CC Q12517; P53550: DCP2; NbExp=5; IntAct=EBI-38519, EBI-270;
CC Q12517; P39517: DHH1; NbExp=3; IntAct=EBI-38519, EBI-158;
CC Q12517; P39998: EDC3; NbExp=4; IntAct=EBI-38519, EBI-22300;
CC Q12517; F4HZB2: SPI; Xeno; NbExp=2; IntAct=EBI-38519, EBI-3386960;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:10761922,
CC ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:14562095}. 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.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9482745}.
CC -!- MISCELLANEOUS: Present with 2880 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; Z48239; CAA88278.1; -; Genomic_DNA.
DR EMBL; Z74891; CAA99170.1; -; Genomic_DNA.
DR EMBL; AY558431; AAS56757.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10636.1; -; Genomic_DNA.
DR PIR; S60387; S60387.
DR RefSeq; NP_014492.1; NM_001183403.1.
DR PDB; 1Q67; X-ray; 2.30 A; A/B=1-231.
DR PDB; 6Y3Z; X-ray; 3.49 A; B=1-231.
DR PDBsum; 1Q67; -.
DR PDBsum; 6Y3Z; -.
DR AlphaFoldDB; Q12517; -.
DR SMR; Q12517; -.
DR BioGRID; 34268; 409.
DR ComplexPortal; CPX-1628; RNA decapping complex, DCP1-DCP2.
DR DIP; DIP-1288N; -.
DR IntAct; Q12517; 25.
DR MINT; Q12517; -.
DR STRING; 4932.YOL149W; -.
DR iPTMnet; Q12517; -.
DR MaxQB; Q12517; -.
DR PaxDb; Q12517; -.
DR PRIDE; Q12517; -.
DR EnsemblFungi; YOL149W_mRNA; YOL149W; YOL149W.
DR GeneID; 854016; -.
DR KEGG; sce:YOL149W; -.
DR SGD; S000005509; DCP1.
DR VEuPathDB; FungiDB:YOL149W; -.
DR eggNOG; KOG2868; Eukaryota.
DR HOGENOM; CLU_113008_0_0_1; -.
DR InParanoid; Q12517; -.
DR OMA; IWIHTVA; -.
DR BioCyc; YEAST:G3O-33539-MON; -.
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 EvolutionaryTrace; Q12517; -.
DR PRO; PR:Q12517; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12517; 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:0008047; F:enzyme activator activity; IDA:SGD.
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:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; mRNA processing;
KW Nonsense-mediated mRNA decay; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..231
FT /note="mRNA-decapping enzyme subunit 1"
FT /id="PRO_0000232998"
FT REGION 92..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 16..20
FT /note="EFYRK->AFYAA: In DCP1-17; partial loss of mRNA-
FT decapping activity."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 29..31
FT /note="RYD->AYA: In DCP1-2; strong loss of mRNA decapping
FT activity at 36 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10101156,
FT ECO:0000269|PubMed:14758354"
FT MUTAGEN 32..34
FT /note="PKI->AKA: Partial loss of mRNA-decapping activity."
FT /evidence="ECO:0000269|PubMed:14758354"
FT MUTAGEN 37..38
FT /note="LL->AA: Strong loss of mRNA-decapping activity; when
FT associated with A-217 and A-221."
FT /evidence="ECO:0000269|PubMed:14758354"
FT MUTAGEN 47
FT /note="Y->A: In DCP1-32; partial loss of mRNA decapping
FT activity."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 47
FT /note="Y->F: In DCP1-35; partial loss of mRNA decapping
FT activity."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 48..50
FT /note="KWD->AWA: In DCP1-4; partial loss of mRNA decapping
FT activity. In DCP1-43; strong loss of mRNA-decapping
FT activity; when associated with A-187 and A-188. In DCP1-44;
FT strong loss of mRNA-decapping activity; when associated
FT with A-216 and A-219."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 56
FT /note="W->A: In DCP1-31; partial loss of mRNA decapping
FT activity."
FT /evidence="ECO:0000269|PubMed:10101156,
FT ECO:0000269|PubMed:14758354, ECO:0000269|PubMed:8757137"
FT MUTAGEN 70
FT /note="R->A: In DCP1-33; strong loss of mRNA decapping
FT activity."
FT /evidence="ECO:0000269|PubMed:10101156,
FT ECO:0000269|PubMed:14758354"
FT MUTAGEN 156
FT /note="G->D: In DCP1-1; strong loss of mRNA decapping
FT activity."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 187..188
FT /note="KD->AA: In DCP1-19; partial loss of mRNA decapping
FT activity. In DCP1-43; strong loss of mRNA-decapping
FT activity; when associated with A-48 and A-50."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 204
FT /note="W->A: In DCP1-33; partial loss of mRNA decapping
FT activity."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 216..219
FT /note="ELIK->ALIA: In DCP1-25; partial loss of mRNA-
FT decapping activity. In DCP1-44; strong loss of mRNA-
FT decapping activity; when associated with A-48 and A-50."
FT /evidence="ECO:0000269|PubMed:10101156"
FT MUTAGEN 217
FT /note="L->A: Strong loss of mRNA-decapping activity; when
FT associated with A-37; A-38 and A-221."
FT /evidence="ECO:0000269|PubMed:14758354"
FT MUTAGEN 221
FT /note="L->A: Strong loss of mRNA-decapping activity; when
FT associated with A-37; A-38 and A-217."
FT /evidence="ECO:0000269|PubMed:14758354"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 34..50
FT /evidence="ECO:0007829|PDB:1Q67"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 55..70
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 139..150
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:1Q67"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:1Q67"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1Q67"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1Q67"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:1Q67"
SQ SEQUENCE 231 AA; 26266 MW; 8456B1C96C121C4D CRC64;
MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD FKKDEWNKLE
YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV NNGSDNSNRN SSGNGNSYKS
NDSLTYNCGK TLSGKDIYNY GLIILNRINP DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE
CMGVEVKDEL VIIKNLKHEV YGIWIHTVSD RQNIYELIKY LLENEPKDSF A
