ID   DEAD_BUCAI              Reviewed;         601 AA.
AC   P57453;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
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}; OrderedLocusNames=BU372;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13076.1; -; Genomic_DNA.
DR   RefSeq; NP_240190.1; NC_002528.1.
DR   RefSeq; WP_009874330.1; NC_002528.1.
DR   AlphaFoldDB; P57453; -.
DR   SMR; P57453; -.
DR   STRING; 107806.10039042; -.
DR   PRIDE; P57453; -.
DR   EnsemblBacteria; BAB13076; BAB13076; BAB13076.
DR   KEGG; buc:BU372; -.
DR   PATRIC; fig|107806.10.peg.386; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_6; -.
DR   OMA; LPQGMPK; -.
DR   Proteomes; UP000001806; 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; 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   Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..601
FT                   /note="ATP-dependent RNA helicase DeaD"
FT                   /id="PRO_0000055098"
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          552..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        552..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..590
FT                   /note="Polar 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;  68806 MW;  886C237AC5E61279 CRC64;
     MTHIESTFSF LGLNPFIIQS LNEMGYVKPS PIQASCIPLL LEGRDVLGMA QTGSGKTAAF
     SLPLLHNLNI NLKAPQILVL APTRELAVQV AEAFSDFSKY MIGIHVLPLY GGQRYELQLR
     ALRQGPQIVV GTPGRLLDHL KRGTLNLSNL HGLVLDEADE MLRMGFIEDV ETIMAQIPKE
     HQTALFSATM PEAIRRISKR FMRNPKEIKI QSNITTRPDI KQSYWMVYGR KTDALIRFLE
     AEDFSATIIF VRTKNATLEV SEALERNGYN SAALNGDMNQ ALREQTLERL KNGRLDILIA
     TDVAARGLDV DRISFVINYD IPMDSESYVH RIGRTGRAGR AGRALLFVEN RERRLLRNIE
     RTMKQSIPEV QLPKVELLCQ RRLEQFAKKV QQQLESRDLD EYSALLDKLY STDDLDIKTL
     AAALLKMAQG ERPLIIKPDV IKRQSRDLLF QDDRRREDNR NSRTRRDRRD INKDAELYRI
     EVGRNDGVEV RHIVGAIANE GNINSRNIGN IKLFSSYSTI ELPKGMSKDL LQTFNRTRIL
     NKPINMKLLR DSRHYENKTT HRSIFNKDKN SNRRVSDGSF NKSNSPKKTE FKSSFFRRRN
     V