DEAD_KLEPN
ID DEAD_KLEPN Reviewed; 643 AA.
AC P33906;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000255|HAMAP-Rule:MF_00964};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00964};
DE AltName: Full=Cold-shock DEAD box protein A {ECO:0000255|HAMAP-Rule:MF_00964};
GN Name=deaD {ECO:0000255|HAMAP-Rule:MF_00964};
GN Synonyms=csdA {ECO:0000255|HAMAP-Rule:MF_00964};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CG43;
RX PubMed=8056751; DOI=10.1093/oxfordjournals.jbchem.a124352;
RA Peng H.L., Hsieh M.J., Zao C.L., Chang H.-Y.;
RT "Nucleotide sequence and expression in Escherichia coli of the Klebsiella
RT pneumoniae deaD gene.";
RL J. Biochem. 115:409-414(1994).
CC -!- FUNCTION: DEAD-box RNA helicase involved in various cellular processes
CC at low temperature, including ribosome biogenesis, mRNA degradation and
CC translation initiation. {ECO:0000255|HAMAP-Rule:MF_00964}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00964};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00964}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61345.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L08387; AAA61345.1; ALT_INIT; Genomic_DNA.
DR PIR; JX0314; JX0314.
DR AlphaFoldDB; P33906; -.
DR SMR; P33906; -.
DR PRIDE; P33906; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070417; P:cellular response to cold; IEA:InterPro.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd12499; RRM_EcCsdA_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00964; DEAD_helicase_DeaD; 1.
DR InterPro; IPR021046; Cold-shock_DEAD_Abox_C.
DR InterPro; IPR034415; CsdA_RRM.
DR InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028618; DEAD_helicase_DeaD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF03880; DbpA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF12343; DeaD_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW RNA-binding; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..643
FT /note="ATP-dependent RNA helicase DeaD"
FT /id="PRO_0000055105"
FT DOMAIN 37..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT DOMAIN 232..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT REGION 440..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..34
FT /note="Q motif"
FT MOTIF 156..159
FT /note="DEAD box"
FT COMPBIAS 447..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
SQ SEQUENCE 643 AA; 71944 MW; 8D388CA5BC047ABD CRC64;
MAEFETTFAD LGLKAPILEA LTDLGYEKPS PIQAECIPHL LDGRDVLGMA QTGSGKTAAF
SLPLLNNIDP ELRAPQILVL APTRELAVQV AEAMTEFSKH MRGVNVVALY GGQRYDVQLR
ALRQGPQIVV GTPGRLLDHL KRGTLDLSKL SGLVLDEADE MLRMGFIEDV ETIMAQIPEG
HQTALFSATM PEAIRRITRR FMKEPQEVRI QSSVTTRPDI SQSYWTAYGM RKNEALVRFL
EAEDFDAAII FVRTKNATLE VAEALERNGY NSAALNGDMN QALREQALER LKDGRLDILI
ATDVAARGLD VERISLVVNY DIPMDSESYV HRIGRTGRAG RAGRALLFVE NRERRLLRNI
ERTMKLTIPE VELPNAELLS KRRLEKFAAK VQQQLESSDL DQYRALLAKI HATAEGEELD
VETLAAALLK MAQGERSLIV PPVAPMRPRR EFRDRDDSFD RRGDRNDRGP RGDREDRPKR
ERRDVGDMEL YRIEVGRDDG VEVRHIVGAI ANEGDISSRY IGNIKLFASH STIELPKGMP
GEVLQHFTRT RILNKPMNMQ LLGDAQPRTE RRGGGERREG GRGFGGERRE GGRGFGGERR
EGGRGEGRRF SGERREGRAP GRDDASAPRR DDSAGRRRFG GDA
