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Database: UniProt
Entry: Q21G88_SACD2
LinkDB: Q21G88_SACD2
Original site: Q21G88_SACD2 
ID   Q21G88_SACD2            Unreviewed;       595 AA.
AC   Q21G88;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
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   OrderedLocusNames=Sde_3034 {ECO:0000313|EMBL:ABD82291.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD82291.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD82291.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD82291.1; -; Genomic_DNA.
DR   RefSeq; WP_011469507.1; NC_007912.1.
DR   AlphaFoldDB; Q21G88; -.
DR   STRING; 203122.Sde_3034; -.
DR   KEGG; sde:Sde_3034; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_6; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000001947; 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; 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:UP000001947};
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          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..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..595
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        439..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..595
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  66390 MW;  0195BFA1A9CC7FC5 CRC64;
     MTESSPNFAQ LGLNEHILKA LTDVGYETPS PIQAKSIPEL LAGRDILGQA QTGTGKTAAF
     ALPILNNLDL SQKAPQVLVL APTRELAIQV AEAFQSYAHH LPGFHILPIY GGQGYDQQIR
     ALKRGVHVIV GTPGRVMDHM RKGTLKLDQL KVLVLDEADE MLRMGFIDDV EWVLTQTPPT
     RQIALFSATM PKEIAKVANK YLNDPALIKI EVKTQTADTI RQRYWGVSGH HKLDATTRIL
     EAEEFDAMII FVRTKTTTIE LAEKLAARGY SSAALNGDIS QNLRERTVEK LKKGQIDILV
     ATDVAARGLD VDRISHVLNY DIPYDSEAYV HRIGRTGRAG RSGEAILFVA PREMRMLRTI
     EKATRKPIEL MKMPSTDDIN QIRVDRFKQK ILDAAKSPGL EFFRKLVTEM QHDNELDTAD
     IAAALALLYQ GDQPLLLEDR PQRQQREFKE RDGDFDKRGR GDRDGRGREG RDRGKGREKD
     ENMETYRIEV GRKDGVKPGD IVGAIANEAN ISSKFIGHIK LHDDFSTVDL PSGMPKEVFE
     TLSKTWVCQK QLRITRAEGN AGGGRGRGGD DFKRKKRPAN KDGAPRKPRA KKADS
//
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