ID A0A2U1LKC8_ARTAN Unreviewed; 987 AA.
AC A0A2U1LKC8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=RNA helicase, ATP-dependent, SK12/DOB1 protein {ECO:0000313|EMBL:PWA49449.1};
GN ORFNames=CTI12_AA481650 {ECO:0000313|EMBL:PWA49449.1};
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:PWA49449.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA49449.1, 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:PWA49449.1};
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 -!- 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:PWA49449.1}.
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; PKPP01008922; PWA49449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1LKC8; -.
DR Proteomes; UP000245207; 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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 1.20.1500.20; -; 1.
DR Gene3D; 2.40.30.300; -; 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; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PWA49449.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT DOMAIN 76..232
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 304..506
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..552
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 112531 MW; CB0CB560D8334BB9 CRC64;
MGSVKRKSIE QDPSTSSSSS PPLKQPRNLI TDEVGVACVH DVSYPENYVG RSDSEKDTKP
AKEFPFSLDP FQSEAIHCLN AGESVMVSAH TSAGKTVVAS YAIAMSLQNK QRVIYTSPIK
ALSNQKYREF KEEFSDVGLM TGDVTIEPNA SCLVMTTEIW RSMQYKGSEL TREVAWIIFD
EVHYMRDRER GVVWEESIVM APKNARFVFL SATVPNAKEF ADWVAKVHQQ PCHIVYTDYR
PTPLQHYLFP TGGDGLYLVV DEKGKFREDS FQKALNALVS TNDKKDNGKW QKGMVNGRAG
EDSDIFKMVK MIIQRQYDPV IIFSFSKREC EFLAMQMAKM DLNEDDEKVN IETIFWSAMD
MLSDDDKKLP QVSNMLPLLK RGIGVHHSGL LPILKEVIEI LFQEGLIKCL FATETFSIGL
NMPAKTVVFS NVRKFDGDKF RWLSSGEYIQ MSGRAGRRGI DDRGVCILML DEKLEPSTAK
MMVKGSADCL NSAFHLSYNM LLNQLRSEDG DPENLLRNSF YQFQADRAIP DLERQMKDLQ
EERDSIHIEE EDSLENYYSL LQQFKSLKKD VRDIIFAPRY CLPFLQPGRL VCIRCVNDDD
STLPLSIEDH ITWGVIVNFQ KVKGLSEDDA NKSPEDANYT IDILTRCSVS KDELSKKTIK
IVPLKERGEP VVVSVPISQI DNLSSVRLVI EKDLLPLENR ENTLKKVSEV LSRFSKQGIP
YLDPEEDMKV QSGSYRKAVR RIEALENLFE KHEVAKSPLI EQKLKVLHKK KEITAQIKAI
KKSMRSTSAL AFKDELKARK RVLRRLGYVT RDDVVELKGK VACEISSADE LVLTELMFNG
VFKDIKIEEM VSLLSCFVWQ EKLQDAQKPR EELEMLFTQL QDTARRVAKV QLDSKVQIDI
ESFVSSFRPD IMEAVYSWAK GSKFYEIMEI TQVFEGSLIR GIRRMEEILQ QLILAAKSVG
EVELEAKFED AVSKIKRDIV FAASLYL
//