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Database: UniProt
Entry: A0A924IA58_9BACT
LinkDB: A0A924IA58_9BACT
Original site: A0A924IA58_9BACT 
ID   A0A924IA58_9BACT        Unreviewed;       570 AA.
AC   A0A924IA58;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 12.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=H7308_02705 {ECO:0000313|EMBL:MBC7526436.1};
OS   Chthonomonadaceae bacterium.
OC   Bacteria; Bacillati; Armatimonadota; Chthonomonadia; Chthonomonadales;
OC   Chthonomonadaceae.
OX   NCBI_TaxID=2739509 {ECO:0000313|EMBL:MBC7526436.1, ECO:0000313|Proteomes:UP000601118};
RN   [1] {ECO:0000313|EMBL:MBC7526436.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FL-bin-356 {ECO:0000313|EMBL:MBC7526436.1};
RA   Zeng Y.;
RT   "Metagenome-assembled genomes from the Lille Firn glacier at the Villum
RT   Research Station in northeast Greenland.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00047984};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|ARBA:ARBA00038437}.
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:MBC7526436.1}.
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DR   EMBL; JACMPS010000088; MBC7526436.1; -; Genomic_DNA.
DR   Proteomes; UP000601118; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; cd12252; RRM_DbpA; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   FunFam; 3.40.50.300:FF:000108; ATP-dependent RNA helicase RhlE; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR050079; DEAD_box_RNA_helicase.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF1; ATP-DEPENDENT RNA HELICASE DBPA; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF03880; DbpA; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF25399; DeaD_dimer; 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; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:MBC7526436.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          43..71
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          74..244
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          255..416
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..71
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  63071 MW;  0A473425DE388715 CRC64;
     MAKKEKSVAT VEERPESAAL TTPVAEPEID LEIETPLASG LPAAFAALGL GEPLLRAIAE
     SGFTQPTPIQ SEAIPFFLTG RDLIGQAQTG TGKTAAFALP LAQLIDPDKR KPQAIVLLPT
     RELCLQVSAE TRHLSKFCRI RVVAVYGGQP IDRQFRALEA GAHIVVGTPG RVLDHIRRGT
     LDLSDIQYVA LDEADEMLQM GFIEDVEEIL KSAPKQRQTA LFSATMPPRI AALANETMKN
     PYHIKIQPKE RTVARITQTY YEVPNSRKQE ALLRILDMEE PKSAIIFCKT KKDVDDLGEA
     LQNKGFNAET LHGDMNQTLR DRVMGRFRSG KAEILVATDV AARGLDIDQV THVFNFDLPW
     DTESYIHRIG RTGRAGRSGD AITLVTPRDR HQIKMLEKQI KAPIGQAQVP TPADIARRHR
     ERFQKEVEAA LELGDFDREA LIVEAITEKT DWTTGEIAAA AMNLLWKSRR LTDFDLDAAR
     ETDARAEVGM VRIFLQIGRF DNVRPGDIVG AIANEAGLSG KSVGAIEIFD RSSYVEVPER
     DASRVISALN NTKLRGRKVR ADVARPKDDR
//
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