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Database: UniProt
Entry: A0A0P7C6Z8_9BACT
LinkDB: A0A0P7C6Z8_9BACT
Original site: A0A0P7C6Z8_9BACT 
ID   A0A0P7C6Z8_9BACT        Unreviewed;       411 AA.
AC   A0A0P7C6Z8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=AFM12_12005 {ECO:0000313|EMBL:KPM48147.1};
OS   Jiulongibacter sediminis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Jiulongibacter.
OX   NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM48147.1, ECO:0000313|Proteomes:UP000050454};
RN   [1] {ECO:0000313|EMBL:KPM48147.1, ECO:0000313|Proteomes:UP000050454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN14-9 {ECO:0000313|EMBL:KPM48147.1,
RC   ECO:0000313|Proteomes:UP000050454};
RA   Liu Y., Du J., Shao Z.;
RT   "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001556};
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:KPM48147.1}.
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DR   EMBL; LGTQ01000009; KPM48147.1; -; Genomic_DNA.
DR   RefSeq; WP_055148916.1; NZ_LGTQ01000009.1.
DR   AlphaFoldDB; A0A0P7C6Z8; -.
DR   STRING; 1605367.AFM12_12005; -.
DR   PATRIC; fig|1605367.3.peg.3803; -.
DR   OrthoDB; 974172at2; -.
DR   Proteomes; UP000050454; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050454}.
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          229..377
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          375..411
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..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  45679 MW;  50892821192EFFFB CRC64;
     MSFKELGLSD VLLKGIEEKG YTTPTLIQEK AIPAVLQGKD VLASAQTGTG KTAGFALPLI
     QLLSEKPITK RRPIRALVLT PTRELAAQVY DETREYARHT GLEAAVIFGG VKQHSQVARL
     KQGVDILVAT PGRLLDLQQQ KLLQLTQVEY LVLDEADRML DMGFIRDIRK VISLMPDRKQ
     NLLFSATFSP EIKKLAATFL DNPVTVAAAP ENTTAELVNQ KVYRVDKAQK TELIIKLIWE
     GNWHQVLVFT RTKHGANRLA QKFQKQKITA AAIHGNKTQN ARTKALEGFK TGEISVLVAT
     DIAARGLDIP QLPHVINFEL PNVPEDYVHR IGRTGRAGAS GEAISLVSAD EVAYLRGIEK
     LLEMKIETEI LEGFEPTEAF NEPQPKSNQK PQQRGGGNRS RHAKNRFRKK H
//
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