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Database: UniProt
Entry: S7VNH8_9BACT
LinkDB: S7VNH8_9BACT
Original site: S7VNH8_9BACT 
ID   S7VNH8_9BACT            Unreviewed;       455 AA.
AC   S7VNH8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Cold-shock DEAD-box protein A {ECO:0000313|EMBL:EPR71541.1};
GN   ORFNames=ADICYQ_0209 {ECO:0000313|EMBL:EPR71541.1};
OS   Cyclobacterium qasimii M12-11B.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR71541.1, ECO:0000313|Proteomes:UP000014974};
RN   [1] {ECO:0000313|EMBL:EPR71541.1, ECO:0000313|Proteomes:UP000014974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12-11B {ECO:0000313|EMBL:EPR71541.1,
RC   ECO:0000313|Proteomes:UP000014974};
RX   PubMed=23950138;
RA   Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT   from Arctic Marine Sediment.";
RL   Genome Announc. 1:e00642-13(2013).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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:EPR71541.1}.
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DR   EMBL; ATNM01000013; EPR71541.1; -; Genomic_DNA.
DR   RefSeq; WP_020890994.1; NZ_ATNM01000013.1.
DR   AlphaFoldDB; S7VNH8; -.
DR   STRING; 641524.ADICYQ_0209; -.
DR   PATRIC; fig|641524.5.peg.205; -.
DR   eggNOG; COG0513; Bacteria.
DR   OrthoDB; 9785240at2; -.
DR   Proteomes; UP000014974; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 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|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}.
FT   DOMAIN          1..29
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          32..206
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          228..375
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          369..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        381..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  50339 MW;  B5E92AFC4732D265 CRC64;
     MIFSEFNFVP ELQEGLDAMG FEKATPIQEQ AIPIILEGKD LIATAQTGTG KTAAFILPVL
     NEISKGDRKG VKVLIIAPTR ELAIQIDQQI QGLAYFLGIS SIPIYGGGDG KVWEQQRKAL
     EMGADIVVAT PGRLIALLAG GKVNFDSLEN LILDEADRML DMGFSEDILT IVNYLPKSRQ
     TLLFSATMPP KIRKFSQQIL QDPEQISIAL GKTAKGVSQY VYHVYDGQKE ALVNSILKSQ
     DFQAVIIFCS TKDKVKSLFK VLKKNFKVEA FHADLDQNER ELIMSSFKNK SLKILVATDI
     LSRGIDVEDI EMVINFDTPN DPEDYVHRVG RTARAEKKGK AVTFVNEKDR YKYKNIENLI
     GMEIEVLPNP EEIGTGPDLK KSHSGKSSGG NRPGGNRNSP GNKRPAKPYK KQARPVDKKS
     ATESVNAKPE AKPKTESTSD KGKFRERKNI KGGLE
//
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