DEAD_HAEIN
ID DEAD_HAEIN Reviewed; 613 AA.
AC P44586;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=HI_0231;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC21900.1; -; Genomic_DNA.
DR PIR; F64056; F64056.
DR RefSeq; NP_438403.1; NC_000907.1.
DR RefSeq; WP_005694061.1; NC_000907.1.
DR AlphaFoldDB; P44586; -.
DR SMR; P44586; -.
DR STRING; 71421.HI_0231; -.
DR PRIDE; P44586; -.
DR EnsemblBacteria; AAC21900; AAC21900; HI_0231.
DR KEGG; hin:HI_0231; -.
DR PATRIC; fig|71421.8.peg.245; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_1_6; -.
DR OMA; LPQGMPK; -.
DR PhylomeDB; P44586; -.
DR BioCyc; HINF71421:G1GJ1-248-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0070417; P:cellular response to cold; IEA:InterPro.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
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..613
FT /note="ATP-dependent RNA helicase DeaD"
FT /id="PRO_0000055104"
FT DOMAIN 36..207
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 434..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..33
FT /note="Q motif"
FT MOTIF 155..158
FT /note="DEAD box"
FT COMPBIAS 437..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
SQ SEQUENCE 613 AA; 69705 MW; 1B826CBDEB1704DF CRC64;
MTDKITFNDL GLPEFILKAV SDLGFETPSP IQQSCIPHLL NGNDVLGMAQ TGSGKTAAFA
LPLLAQIDPS EKHPQMLVMA PTRELAIQVA DACELFVKYA QGTRIVTLYG GQRYDIQLRA
LKQGAQVVVG TPGRILDHIR RGTLNLSELR FIVLDEADEM LRMGFIDDVE TVMAELPENH
QTALFSATMP EPIRRITKRF MNDPQEVKIK VNNENAPDID QSCWYVHGVR KNEALLRFLE
VEDFDAAIIF ARTKTGTLDI TELLEKNGFR SAALNGDMTQ QLREQTLDRL RNGSLDIVVA
TDVAARGIDI ERISLVVNYD IPLDAESYVH RIGRTGRAGR SGRALLFVEP RERRLLRNIE
HLMKKGINEV ELPNHLVLQE CRRKKFVAKI TKQLEHHDLE QYRSLLEDLF TADQDQENIA
AAMLMLLQGK QKLILPPDPP MEKRRRERND RGDRRENPRS AERRGERKGY GNPQPMDLYR
IEVGRADGVE VRHIVGAIAN EGDINSRYIG HIKLYDDYTT VELPQGMPKE LLQQFAKTRV
LNKQMQMSFL GAVKSDNSRG SDDFNGKRKG RGGDFRGERG RERGNDNRGN RKFNEKSNRT
FSDKPRRDRR SSF
