ID A0A182H449_AEDAL Unreviewed; 718 AA.
AC A0A182H449;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=RP20_CCG021334 {ECO:0000313|EMBL:KXJ71160.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF021334-PA.1, ECO:0000313|Proteomes:UP000069940};
RN [1] {ECO:0000313|EMBL:KXJ71160.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ71160.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ71160.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ71160.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ71160.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ71160.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AALF021334-PA.1}
RP IDENTIFICATION.
RC STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF021334-PA.1};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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. DDX10/DBP4
CC subfamily. {ECO:0000256|ARBA:ARBA00038084}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXUM01108787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KQ565264; KXJ71160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182H449; -.
DR STRING; 7160.A0A182H449; -.
DR EnsemblMetazoa; AALF021334-RA; AALF021334-PA; AALF021334.
DR VEuPathDB; VectorBase:AALC636_004558; -.
DR VEuPathDB; VectorBase:AALF021334; -.
DR VEuPathDB; VectorBase:AALFPA_055366; -.
DR Proteomes; UP000069940; Unplaced.
DR Proteomes; UP000249989; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17941; DEADc_DDX10; 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; IPR025313; DUF4217.
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; PTHR24031:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000249989};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 55..83
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 86..260
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 273..435
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 55..83
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..23
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 81598 MW; 0D80245D3268CB1B CRC64;
MKHPNSGKRV KDKFKRKPKQ QNGGKSKFKF SMKDEESEIG RLTESYPTAT IEETSSFSDF
PLSKKTLRGL AQGQYRKPTA IQRESILPAL QGKDILAAAK TGSGKTLAFL IPVFEKLYTN
QWTRLDGLGA LIITPTRELA LQIFETVAKI GKLHDFTTGL IIGGQNLKVE KSRLHQLNII
ICTPGRLLQH MDQNPLFDCT NLKILVLDEA DRCLDLGFES AMNAIIENLP SERQTLLFSA
TQTKSVKDLA RLNLRNPLYI APHEKEQYTT PAKLQQNYVA VELGQKLTML WSFLKAHSKQ
KIIVFFATCK QVKYFYEVFR KLRPSTLLLP LYGGMNQERR NKIYTEFCSK SNVCLLATDV
ASRGLDFPKV NWVVQLDCPE DANQYIHRAG RTARLNTSGE SLLVLLPQEE EGVVKMLEKT
KVPINKIHID DKQLFSPLIK IQSFLAQSPE LKETAKRAFV AYVKSVALMK DKSIFDASKL
DLEAYAKSLG LLVTPRVRFL SRKENKSKKS NVKTDVKVAL DENDEDESDE EFFTVKKSER
FSTMHQPEEE PNEPEVVTES KKKITKVKLL KKALVTNKKI CFDDSGNAVD EEVRDEVYDI
EKARAQLKLA DAEDKERYKN LQKAKRVARK EKLKRKADEE NEEEDDFGSD DDEHSVDLNW
LPDPDKVYNG DDREVGSDAS SAEELKPAKK TPKKRKIADK ISDITLTEAE QLAMNLLK
//
