ID F5Z509_ALTNA Unreviewed; 588 AA.
AC F5Z509;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=ambt_15330 {ECO:0000313|EMBL:AEF04576.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF04576.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF04576.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
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; CP002339; AEF04576.1; -; Genomic_DNA.
DR RefSeq; WP_013785500.1; NC_015554.1.
DR AlphaFoldDB; F5Z509; -.
DR KEGG; alt:ambt_15330; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_1_6; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000000683; 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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00964};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00964}.
FT DOMAIN 7..35
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 38..209
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 233..380
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 437..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..35
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 561..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 65847 MW; 353103F9A303478E CRC64;
MTTTVDMTFK DLKLPEPILQ ALEKVGYEKP SPIQAESIPL LLEGHDLLGQ AQTGTGKTAA
FALPMLANID PEQRKPQLLV LAPTRELAIQ VAEAFQVYAS FSHKIKVLPV YGGQSYDNQI
RQLKRGVQVV VGTPGRVIDH IKRKTLDLSE LKFLVLDEAD EMLRMGFIDD VELILSHAPA
ERQTALFSAT MPGPIKKITQ RYLKDPKHVK IASKVSTAST IRQRYCQVAP HHKLEALTRI
MEVERFDGMI IFVRTKTATV ELADKLSARG YDVEPLNGDI PQNARERTVD KLKQGNIDIL
VATDVVARGL DVERVSHVIN YDVPYDSESY VHRIGRTGRA GRTGDAILFI SHREKRMLFS
IEKTTKQPIE VMPIPSISEI NETRLSRFKQ SVIDATQDDS IETLIPLVEM IKEEAEASPE
VLMAALLKIA QGDEPLILKE SDRPDLHSKP PRDSREPRGD RRDGGRDGRE RKPRAPRTGR
KPEAGMQRFR IDVGHTHGAK PGNIVGAIAN EGNMDSKHIG AIEIYDNFST VDLPEGMPKE
TKDKLQGTRV AGQRLSIREW SDTPPAKRER GDNRGENRSR DNRARRKS
//
