DED1_SCHPO
ID DED1_SCHPO Reviewed; 636 AA.
AC O13370; O59857; Q9UU14;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP-dependent RNA helicase ded1;
DE EC=3.6.4.13;
DE AltName: Full=Multicopy suppressor of overexpressed cyr1 protein 2;
GN Name=ded1; Synonyms=dep1, moc2, sum3; ORFNames=SPCC1795.11;
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 [MRNA], FUNCTION, AND ALTERNATIVE FORMS.
RX PubMed=11711540; DOI=10.1074/jbc.m109016200;
RA Liu H.-Y., Nefsky B.S., Walworth N.C.;
RT "The ded1 DEAD box helicase interacts with Chk1 and Cdc2.";
RL J. Biol. Chem. 277:2637-2643(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10725227; DOI=10.1242/jcs.113.8.1447;
RA Grallert B., Kearsey S.E., Lenhard M., Carlson C.R., Nurse P., Boye E.,
RA Labib K.;
RT "A fission yeast general translation factor reveals links between protein
RT synthesis and cell cycle controls.";
RL J. Cell Sci. 113:1447-1458(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10395922; DOI=10.1016/s0167-4781(99)00071-8;
RA Kawamukai M.;
RT "Isolation of a novel gene, moc2, encoding a putative RNA helicase as a
RT suppressor of sterile strains in Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1446:93-101(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9832516; DOI=10.1093/genetics/150.4.1361;
RA Forbes K.C., Humphrey T., Enoch T.;
RT "Suppressors of cdc25p overexpression identify two pathways that influence
RT the G2/M checkpoint in fission yeast.";
RL Genetics 150:1361-1375(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=16273369; DOI=10.1007/s00294-005-0028-z;
RA Goldar M.M., Jeong H.T., Tanaka K., Matsuda H., Kawamukai M.;
RT "Moc3, a novel Zn finger type protein involved in sexual development, ascus
RT formation, and stress response of Schizosaccharomyces pombe.";
RL Curr. Genet. 48:345-355(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 115-339, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-54; SER-55; SER-58;
RP SER-59; THR-63; THR-128 AND THR-312, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes (By similarity).
CC Inactivation of ded1 blocks mitotic cell cycle progression at G1 and
CC G2/M. Induces sexual development and ascus formation. {ECO:0000250,
CC ECO:0000269|PubMed:10725227, ECO:0000269|PubMed:11711540,
CC ECO:0000269|PubMed:16273369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Interacts with chk1, which is required for cell cycle arrest
CC following DNA damage.
CC -!- INTERACTION:
CC O13370; Q10281: rkp1; NbExp=3; IntAct=EBI-2478405, EBI-696304;
CC O13370; P79015: rpl3202; NbExp=3; IntAct=EBI-2478405, EBI-7169357;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- MISCELLANEOUS: A different form of ded1 has been identified via SDS-
CC PAGE studies. It is uncertain how this form arises in vivo.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF025536; AAC04893.1; -; mRNA.
DR EMBL; AF084222; AAC34121.1; -; Genomic_DNA.
DR EMBL; AB012389; BAA25324.1; -; mRNA.
DR EMBL; AJ237697; CAB40192.1; -; mRNA.
DR EMBL; CU329672; CAA18646.1; -; Genomic_DNA.
DR EMBL; AB027871; BAA87175.1; -; Genomic_DNA.
DR PIR; T43543; T43543.
DR RefSeq; NP_588033.1; NM_001023025.2.
DR AlphaFoldDB; O13370; -.
DR SMR; O13370; -.
DR BioGRID; 275274; 42.
DR IntAct; O13370; 11.
DR MINT; O13370; -.
DR STRING; 4896.SPCC1795.11.1; -.
DR iPTMnet; O13370; -.
DR MaxQB; O13370; -.
DR PaxDb; O13370; -.
DR PRIDE; O13370; -.
DR EnsemblFungi; SPCC1795.11.1; SPCC1795.11.1:pep; SPCC1795.11.
DR GeneID; 2538689; -.
DR KEGG; spo:SPCC1795.11; -.
DR PomBase; SPCC1795.11; -.
DR VEuPathDB; FungiDB:SPCC1795.11; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; O13370; -.
DR OMA; CYRSWVR; -.
DR PhylomeDB; O13370; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:O13370; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IMP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IMP:PomBase.
DR GO; GO:0031047; P:gene silencing by RNA; IDA:UniProtKB.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IDA:PomBase.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Helicase; Hydrolase;
KW Initiation factor; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..636
FT /note="ATP-dependent RNA helicase ded1"
FT /id="PRO_0000055042"
FT DOMAIN 200..392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 403..564
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..197
FT /note="Q motif"
FT MOTIF 336..339
FT /note="DEAD box"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 41
FT /note="A -> R (in Ref. 3; BAA25324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 69759 MW; 094630A41A3C26F1 CRC64;
MSDNVQQQVD SVGSVTEKLQ KTNISRPRKY IPPFARDKPS AGAAPAVGDD ESVSSRGSSR
SQTPSEFSSN YGGRREYNRG GHYGGGEGRQ NNYRGGREGG YSNGGGYRNN RGFGQWRDGQ
HVIGARNTLL ERQLFGAVAD GTKVSTGINF EKYDDIPVEV SGGDIEPVNE FTSPPLNSHL
LQNIKLSGYT QPTPVQKNSI PIVTSGRDLM ACAQTGSGKT AGFLFPILSL AFDKGPAAVP
VDQDAGMGYR PRKAYPTTLI LAPTRELVCQ IHEESRKFCY RSWVRPCAVY GGADIRAQIR
QIDQGCDLLS ATPGRLVDLI DRGRISLANI KFLVLDEADR MLDMGFEPQI RHIVEGADMT
SVEERQTLMF SATFPRDIQL LARDFLKDYV FLSVGRVGST SENITQKVVH VEDSEKRSYL
LDILHTLPPE GLTLIFVETK RMADTLTDYL LNSNFPATSI HGDRTQRERE RALELFRSGR
TSIMVATAVA SRGLDIPNVT HVINYDLPTD IDDYVHRIGR TGRAGNTGQA VAFFNRNNKG
IAKELIELLQ EANQECPSFL IAMARESSFG GNGRGGRYSG RGGRGGNAYG ARDFRRPTNS
SSGYSSGPSY SGYGGFESRT PHHGNTYNSG SAQSWW
