ID A0A2I0AS78_9ASPA Unreviewed; 1344 AA.
AC A0A2I0AS78;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AXF42_Ash013909 {ECO:0000313|EMBL:PKA58403.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA58403.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA58403.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA58403.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; KZ451953; PKA58403.1; -; Genomic_DNA.
DR STRING; 1088818.A0A2I0AS78; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:PKA58403.1};
KW Helicase {ECO:0000313|EMBL:PKA58403.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PKA58403.1};
KW Nucleotide-binding {ECO:0000313|EMBL:PKA58403.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161}.
FT DOMAIN 320..512
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 645..848
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 46..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 150836 MW; 44FB11927E39836A CRC64;
MGKNFKGGEQ VSTTTSELLG SGEIQDGFVT NGVGSNAFIL PGKKRRKTKG IGKVSKIKAK
EAQSHRKSKQ RKLQKLQEEK EKKLILSKSI SVLQKYKIKD ESYSILQSSG TIGQPETARE
KRRLALQYSK AGLEVPEGMT LFKTEKTPCG KDVIEHFDQD YLPINNGDSR GSMKELKKED
CSSSYLEKTV KESNEGESIV KSLELNKCSL FPPGKAMNNS GSSQQHSFQK NSNDANLIPN
DKVLSEDNKS FISTPSVSDT CLEGKSSQGT HVSPKPFKVS DPHTIPGPSK TAIVVPVSRP
QEVEEERRDL PIIMMEQEIM EAINDHPILI LCGETGCGKT TQVPQFLYEA GYGTSGYGDR
KGIIGITQPR RVAVLATAKR VSYELGFYLG KEVGFQVRHD RMIGSNCSIK FMTDGILLRE
TQSDILLKRY SIIILDEAHE RSLNTDILIG MLSRIVKLRQ DLYENQQKQM HARDKISPHD
LIFPLKLVIM SATLRVEDFT SNRKLFHQTP PVLEVPIRQF PVTVHFSRKT PEDYLGQAYK
KILSIHKKLP PGAILAFVTG QREVEFLCKK LRRASQKFCE NGLRKENASG GNLEQDIQPI
DEAFGMQSSP NLPTNMFGSY EEEDIQGNNQ NSSDSDTESE VDEDSEDDDS LKTENLEGGS
SVIDFLRNPG CLSSLKAAFE ALAENSSIKS SAEKPEPQLA LQSQEATAKP AAAVGPLYVL
PLYAMLPASA QLRVFEQVPE GERLVVVATN VAETSLTIPG IKYVVDTGKE KVKSYNYGNG
IATYEVQWIS KASASQRAGR AGRTGPGHCY RLYSSAAFSK DDIFPEFSCP EISKVPVESV
VLLLKFMNID KVENFPFPTP PKASALEEAE RCLMTIEALD MKSKLTPTGR AMAQYPMSPR
HSRLILTVIE ILRNQPVFGR ANLVLGYAIA AAAALSFPSP FLFQLEWYKE TQENDYGQED
KIHENERTKD HGEEQRKKRL KAIAKECRAR FCNPSSDALT VAYALQLFEL TDNAFQFCRN
NYLHLKTMEE MSKLRKQILQ LTFHSGKLCR EFSWVHGGID DVEAAWRKNS AKHPLQLIEE
QLLGQAICAG WADRIAKRMR ISPDSSDKVR KAHSMQYQSC AMDDVVYLHR RSSVSQTAPE
FLVYSELLCT TKPYMHGVTT VKPDWLVRYA SSLCSFSPPL MDPKPYYEPL SDRSFCWVST
TFGRHNWQLP LHSLPIKDEI LRVSVFAYAL LAGNVLPCLK NARDFLAASP SIILRPEALG
HRRVGDLLSA LRTRSSVIDS RKMLREAWNE NPMFLHLEVG NWFQAKFGQQ FELSWKQMLQ
EATLEGCELF PKRMKKDRNF ARHG
//
