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Database: UniProt
Entry: A0A200R8N7_9MAGN
LinkDB: A0A200R8N7_9MAGN
Original site: A0A200R8N7_9MAGN 
ID   A0A200R8N7_9MAGN        Unreviewed;       442 AA.
AC   A0A200R8N7;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Helicase {ECO:0000313|EMBL:OVA19104.1};
GN   ORFNames=BVC80_7599g4 {ECO:0000313|EMBL:OVA19104.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA19104.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA19104.1, ECO:0000313|Proteomes:UP000195402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC   TISSUE=Root {ECO:0000313|EMBL:OVA19104.1};
RX   PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA   Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA   Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA   Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA   Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT   "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT   Benzylisoquinoline Alkaloids Metabolism.";
RL   Mol. Plant 10:975-989(2017).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000256|ARBA:ARBA00024350}.
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:OVA19104.1}.
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DR   EMBL; MVGT01000266; OVA19104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200R8N7; -.
DR   STRING; 56857.A0A200R8N7; -.
DR   InParanoid; A0A200R8N7; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000195402; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd17954; DEADc_DDX47; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR044765; DDX47/Rrp3_DEADc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF21; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 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; 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:UP000195402}.
FT   DOMAIN          14..42
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          45..216
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          227..387
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          404..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           14..42
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        404..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  48865 MW;  3B042050D7C3EC86 CRC64;
     MTSIAAEVED EEVKTFKGLG ICEQLAEACE NLGWKNPSKI QAEAIPHALE GKDLIGLAQT
     GSGKTGAFAL PILNALLDSP QAFFACVLSP TRELAIQIAE QFEALGSGVG VKCAVVVGGI
     DMMQQAIALA KRPHIVVGTP GRLVDHLSNT KGFSLRTLKY LVLDEADRLL NEDFEKTIDD
     ILKAIPRERK TYLFSATMTK KVRKLQRACL RNPVKIEAAS KYSTVDTLKQ QYRFVPAKYK
     DCYLVFILSE MSGSTSMVFT RTCEATRLLA LLLRNLGLRA IPISGQMSQA KRLGAMNKFK
     AGECNILLCT DVASRGLDIP SVDMVINYDI PTNSKDYIHR VGRTARAGRS GVAISLVNQY
     ELEWYIQIEK LIGKKLPEFP AQEEEVLLLL ERVTEAKRLS LTKLKESGKR KRRGGEEDGE
     EVDRYLTHKK GGGKSSKKAK NR
//
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