ID I2B4U5_SHIBC Unreviewed; 632 AA.
AC I2B4U5; K6UT93;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000256|HAMAP-Rule:MF_00964};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00964};
DE AltName: Full=Cold-shock DEAD box protein A {ECO:0000256|HAMAP-Rule:MF_00964};
GN Name=deaD {ECO:0000256|HAMAP-Rule:MF_00964,
GN ECO:0000313|EMBL:AFJ45549.1};
GN Synonyms=csdA {ECO:0000256|HAMAP-Rule:MF_00964};
GN OrderedLocusNames=EBL_c04230 {ECO:0000313|EMBL:AFJ45549.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45549.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ45549.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_00964};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00964}.
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DR EMBL; CP001560; AFJ45549.1; -; Genomic_DNA.
DR RefSeq; WP_002441966.1; NZ_BAHA01000014.1.
DR AlphaFoldDB; I2B4U5; -.
DR STRING; 630626.EBL_c04230; -.
DR KEGG; ebt:EBL_c04230; -.
DR PATRIC; fig|630626.3.peg.417; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_1_6; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000001955; 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:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12499; RRM_EcCsdA_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00964}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00964};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00964};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00964}; Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00964};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00964}.
FT DOMAIN 6..34
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 37..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 232..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 436..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..34
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 445..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 70764 MW; 2BE37E5EEAA2681E CRC64;
MAEFETTFSD LGLKAPILEA LNDLGYEKPS PIQAECIPHL LNGRDVLGMA QTGSGKTAAF
SLPLLNNLDP ELKAPQILVL APTRELAVQV AEAMTDFSKH MRGVNVVALY GGQRYDVQLR
ALRQGPQIVV GTPGRLLDHL KRGTLNLSSL HGLVLDEADE MLRMGFIEDV ETIMAQIPAE
HQTALFSATM PEAIRRITRR FMQDPQEVRI QSSVTTRPDI SQSYWTAWGM RKNEALVRFL
EAEDFDAAII FVRTKNATLE VAEALERSGY NSAALNGDMN QALREQTLER LKDGRLDILI
ATDVAARGLD VERISLVVNY DIPMDAESYV HRIGRTGRAG RAGRALLFVE NRERRLLRNI
ERTMKLTIPE VELPNAELLG KRRLEKFAAK VQQQLESSDL DQYRALLAKL QPEAEGELDV
ETLAAALLKM AQGERPLILP PDAPMRPRRE FRERDDRRGD RNDRGDRGER GDRPRRERRD
VGDMQLYRIE VGRDDGVEVR HIVGAIANEG DISSRYIGNI KLFGTHSTIE LPKGMPGDVL
QHFTRTRILN KPMNMQLIGD AQPRPDRGGR SFGGERREGG RRDGGRGFGG ERREGGRGDG
RRFSGERRDG NRGPRRDDSA PRPARRFGGD AS
//
