ID A0A2T5MJN6_9GAMM Unreviewed; 659 AA.
AC A0A2T5MJN6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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 Synonyms=csdA {ECO:0000256|HAMAP-Rule:MF_00964};
GN ORFNames=CJD38_01290 {ECO:0000313|EMBL:PTU32781.1};
OS Stenotrophobium rhamnosiphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stenotrophobium.
OX NCBI_TaxID=2029166 {ECO:0000313|EMBL:PTU32781.1, ECO:0000313|Proteomes:UP000244248};
RN [1] {ECO:0000313|EMBL:PTU32781.1, ECO:0000313|Proteomes:UP000244248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GT1R17 {ECO:0000313|EMBL:PTU32781.1,
RC ECO:0000313|Proteomes:UP000244248};
RA Liu Q., Xin Y.-H.;
RT "Novel species isolated from glacier.";
RL Submitted (APR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTU32781.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QANS01000001; PTU32781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5MJN6; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000244248; 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:UP000244248};
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 13..41
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 44..215
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 240..391
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 455..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..41
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 466..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 72681 MW; BC56EC040AE81762 CRC64;
MSADPSETTS VSPGFRDLAL SEPVQKALDD VGYESPSPIQ AATIPHLLEG KDVLGQAQTG
TGKTAAFALP ILSNINIGKA GPQALVLAPT RELAIQVAEA FQKYATHIKG FHVLPIYGGQ
SYEPQLKALK RGVHVVVGTP GRVMDHMKRG TLNLSNLSCL VLDEADEMLR MGFIDDVEFI
LQQTPKERQV ALFSATMPSV IRRIAQTYLH DPVEITIKSK TATATNIRQR YLMASGMEHK
LNSLTRILEA EPFEGMIIFA RTKSATTELA EKLEARGYSC AALNGDIVQA QRERTVNRLK
SGQLDIIVAT DVAARGLDVE RISHVVNFDI PTDTESYVHR IGRTGRAGRS GEAILFVASR
ERHLLATIER ATRQPVTLMQ LPSVSAVNDL RIVRFKQKIS ETIAAGGLDT LRAAVEQYEH
ENNVPMIEIA AALAQMAQGD KPLLLAEGPI ERRAAAVAGP ERSSHRENMF ASDRSERSER
RPTPDRRTPP VREARDFRDS PRATIEVAPR AERSERPAPA ERFERTERPV RTERPERTTA
ADRPERSTER PASRPRGASE EGMETYRIEV GHVHAVKPGN IVGAIANEAE IDSEFIGRIE
IFEDHSLIDL PEGMPKETFR GLQKVWVCGQ QLKITKAGEQ ATSAPVPRKY SKPSGPKRF
//
