ID A0A1X7ANI9_9GAMM Unreviewed; 631 AA.
AC A0A1X7ANI9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:SMA49856.1};
GN Synonyms=csdA {ECO:0000256|HAMAP-Rule:MF_00964};
GN ORFNames=EHSB41UT_03646 {ECO:0000313|EMBL:SMA49856.1};
OS Parendozoicomonas haliclonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Parendozoicomonas.
OX NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA49856.1, ECO:0000313|Proteomes:UP000196573};
RN [1] {ECO:0000313|EMBL:SMA49856.1, ECO:0000313|Proteomes:UP000196573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA49856.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWPT01000009; SMA49856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7ANI9; -.
DR OrthoDB; 9808889at2; -.
DR Proteomes; UP000196573; Unassembled WGS sequence.
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; 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; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {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:UP000196573};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00964};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00964}.
FT DOMAIN 10..38
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 41..212
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 236..383
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 437..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 10..38
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 439..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 70410 MW; 2E32E4E0C1494ABC CRC64;
MPETQIETIT AFDQLPLSDA ILRAVSDVGY ETPSPIQARS IPHLLEGRDL LGLAQTGTGK
TAAFALPTLS RIDVTNSDTQ VLVLCPTREL AIQVAEACQT YAKYLPSFHV LPIYGGQDMR
GQLRGLHRGA QVVVGTPGRV MDHLRRGSLK LDSLKTVVLD EADEMLRMGF VDDIEWILDH
TPKSRQTALF SATMPPAIRR IADTYLQDPV SVEIRAKTTT VATITQKVWM ASGLHKLDAL
TRILEVEDFD AMIIFVRTRS ATVELAEKLE ARGFSAAALN GDMSQALREK MVDRLKKGSL
DILIATDVAA RGLDVERISH VVNYDIPNDT EAYVHRIGRT GRAGRQGTAI LFAAPRERRM
LRAIEHATRQ KIEPMRLPTQ RDVRDIRIKN FKEQLACILG NEDLSQYREV VNEMIQEQAI
EMEDAAAALC YMAQKERPFP DGNEPEPRQW EDRGDRGDRG ERGERRGRRG DDREDPRNIG
KKRYRIGVGR EHGVSPGEIV GALANEGGIS GRDIGHIRLF DKFSTVYLPE TLGQDVLSTM
SEISIRNQVI GLREWRENPE GGRGGRGGFG GERGDRGERR GGRGGFGGDR NDRGGERRRS
FSDRGERGGR DDRGDRPRRA PRRNDDNRGN E
//
