ID A0A2U1KZ02_ARTAN Unreviewed; 603 AA.
AC A0A2U1KZ02;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=CTI12_AA549310 {ECO:0000313|EMBL:PWA41959.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA41959.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA41959.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA41959.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
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|ARBA:ARBA00001556,
CC 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. DDX18/HAS1
CC subfamily. {ECO:0000256|ARBA:ARBA00024357}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769}.
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:PWA41959.1}.
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DR EMBL; PKPP01012720; PWA41959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1KZ02; -.
DR STRING; 35608.A0A2U1KZ02; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17942; DEADc_DDX18; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
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; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR029014; NiFe-Hase_large.
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:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00346; Complex1_49kDa; 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; SSF56762; HydB/Nqo4-like; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 113..141
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 144..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 346..503
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 92..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 113..141
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 92..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 68545 MW; E789B78D9A0AD4B5 CRC64;
MPLGASENDS SRVCWDSRRA APYDVHDQSD PDVPVGTRGD RYDRYCIRIE EMRQSVRIIV
QCPNQMPSGM IKADDRLIGR EDDQFFRDIP EMMENKEERK GDEDLKRRRG RSDPFTALPL
SEPTKKAILE LGFQYMTQIQ ARGIPPLLEG KDVLGAARTG SGKTLAFLVP AVELLYQLRF
SPRNGTGVVV ICPTRELAIQ THKVATDLLK YHSQTLGLVI GGAARKTEAE RIVKGVNILV
ATPGRLLDHL QNTKGFIYKN LKCFVIDEAD RILEANFEEE MKQIIRILPK TRQTALFSAT
QTKKVEDLAR LSFQNTPVYI DVDIGRSRVT NEGLQQGYCV VPSAKRFLLL YSFLKRNLSK
KVMVFFSSCN SVKFHSELLT YIHVDCFDIH GKQKQNKRTS TFFDFCKAEK GILLCTDVAA
RGLDIPAVDW IVQYDPPDEP KEYIHRVGRT ARGEGAKGNA LLFLIPEELL FLSYLKQAKV
PVKEYEFDEK KIANVQSHLE KLVSTNFYLN KSAKDAYRSY LLAYNSHSMK EIFNVHRLDM
QAVAASFCFS DPPKVALNID SNASKFRQKS RRPEGRSRNG FSENNPYGRN RGGGDDRTQI
VRY
//
