ID   DEAD_BUCAP              Reviewed;         601 AA.
AC   Q8K9H6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
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};
GN   OrderedLocusNames=BUsg_360;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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}.
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DR   EMBL; AE013218; AAM67913.1; -; Genomic_DNA.
DR   RefSeq; WP_011053880.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9H6; -.
DR   SMR; Q8K9H6; -.
DR   STRING; 198804.BUsg_360; -.
DR   EnsemblBacteria; AAM67913; AAM67913; BUsg_360.
DR   KEGG; bas:BUsg_360; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_6; -.
DR   OMA; LPQGMPK; -.
DR   OrthoDB; 626183at2; -.
DR   Proteomes; UP000000416; Chromosome.
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; 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; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   RNA-binding; Stress response.
FT   CHAIN           1..601
FT                   /note="ATP-dependent RNA helicase DeaD"
FT                   /id="PRO_0000055099"
FT   DOMAIN          37..208
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT   DOMAIN          231..378
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT   REGION          564..601
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        564..581
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   601 AA;  68827 MW;  A6A6F0E207F27DBB CRC64;
     MTHTESTFSF LGLNPFIIKS LSKMGYVKPS PIQAACIPLL LEGRDVLGMA QTGSGKTAAF
     SLPLLHNLNI NLKAPQILVL APTRELAVQV AEAFSDFSKY IMGIHVLPLY GGQRYEVQLR
     ALRQGPQIVV GTPGRLLDHL KRGTLNLSNL YALVLDEADE MLRMGFIEDV ETIMSQIPKE
     HQTALFSATM PEAIRRISKR FMKNPQEIKI QSNITTRPDI KQSYWMVYGR KTDALIRFLE
     VEDFSATIIF VKTKNATLEV SEALERNGYN SAALNGDMNQ ALREQTLERL KSGRLDILIA
     TDVAARGLDV DRISFVINYD IPMDSESYVH RIGRTGRAGR AGRALLFVEN RERRLLRNIE
     RTINQTIPEV QLPKIEVLCK RRLERFAKKV QEQLESRDLD EYSALLDKLY SPDDLDIKTL
     ASALLKMAQG GRPLIIKKDL LQRPSREFSF KDDRRREDNH RNNNRNRRER RELKDIDLYR
     IEAGRNDGVE VRHIVGAIAN EGNINSRNIG NIKLFSSYAI VELPKGLSKD LLQRLIKTKI
     LNKKINIKLL RDIKNYETRT HNRSIFNKDK NNKRRFSDNR LNKSSSIKNE TKSSFFRRKS
     V