ID A0A0T6AYC6_9SCAR Unreviewed; 293 AA.
AC A0A0T6AYC6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
DE Flags: Fragment;
GN ORFNames=AMK59_7239 {ECO:0000313|EMBL:KRT80004.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT80004.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT80004.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT80004.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT80004.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
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:KRT80004.1}.
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DR EMBL; LJIG01022545; KRT80004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AYC6; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:KRT80004.1};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 1..109
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 208..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 293
FT /evidence="ECO:0000313|EMBL:KRT80004.1"
SQ SEQUENCE 293 AA; 33967 MW; 181811E21A003F14 CRC64;
MKEKRHKMLE SFRTSSEGLL LCTDVMARGI DIPEVDWVIQ WDPPSNASAF VHRVGRTARQ
GHEGSALIML LESEETYVTF IEKNQKVQLI ERNDPCNEEQ ITKSMETLRK IQLKDRAIME
KATRAFVSHI RAYSKHECSL LLRIKDLSIG AMAVTYGLLQ LPKMPEVKNR DVSEFPIIEN
FDCNSIPYKD KNKESARQLK LKQYQNTGVW PGIKQKNRPK MKSTEPWSKS KQKKEEKKEK
RLKRKKGNEA KAACDEPVKK KKRKGKVSQE DIDELSKDIA LLKKLKKKKI TEE
//
