ID A0A420JBE8_9PEZI Unreviewed; 1199 AA.
AC A0A420JBE8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=GcM3_000008 {ECO:0000313|EMBL:RKF84145.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF84145.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF84145.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF84145.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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 -!- 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:RKF84145.1}.
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DR EMBL; MCBQ01000093; RKF84145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420JBE8; -.
DR STRING; 62708.A0A420JBE8; -.
DR Proteomes; UP000283383; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; 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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR Pfam; PF00270; DEAD; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:RKF84145.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383}.
FT DOMAIN 232..303
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 545..708
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 726..906
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 141..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 135619 MW; 2B9FE68B09694111 CRC64;
MEDLESLEIL SLVSKVTSEL QNHLGICDKT LAEFVIAQNV QCKSLQDFQE TLEKMGADFP
QSLIESIDRL VKTIHPKYQD KDAREESGRT VEEKTKVFKG LALPDKEIPW TEESTDVNRN
FNEKTERDAI DDTLALLEDL EPKIKRENPE NSGWKRSRSP EEDYNREGKK KKMNKFTSRS
KNDTHYRDNG VEEKDEFGRS RRLNQDCLYS QERDDKYRRS SNFELDEKPI ELKIYDGHVT
GMKDFGCFVR LHGVQGKVDG LVHVSALVEG QRVSHPSDLV VKGQSVKVKV VRIEGKRIGL
SMKEVDQETG QDLAPRASIQ SGANTERLGG GRDEGLSLDE KKSAIMGDSN ESRQFKKRMT
SPERWEIRQL IASGVVKASE YPDLDEDYNA TLNGEGGMEL EEEVDIELRE EEPPFLAGQT
KQSLELSPIR VVKAPDGSMN RAAMAGTSLA RDRRELRQQE AQDKAAEESS KVDLSSQWND
PMVQAEERVF ASDLRATKPN PASEIVPEWK RATQNKNQSF GRRTDMTIKQ QRENLPVYRF
RSELIKAVHE NQLLIVVGDT GSGKTTQLTQ YLAEAGFANE YIIGCTQPRR VAAMSVAKRV
AEEVGCQLGQ EVGYTIRFED VTSLATKIKY MTDGMLQREI LMDPDLKRYS VIMLDEAHER
TIATDVLFAL LKKTIKRRPD LKVIVTSATL DADKFSAYFN ECPIFSIPGR TFPVEIMYSR
EPEPDYLDAA LVTVMQIHLT EPPGDILLFL TGQEEIDTSC EILFERMKAL GQGVPELIIL
PVYSALPSEM QSKIFEPAPP GSRKVVIATN IAETSITIDH IYYVIDPGFV KQNAYDPKLG
MDSLVVTPIS QAQAKQRAGR AGRTGPGKCF RLYTEAAFQS EMLPTSIPEI QRQNLSNTIL
MLKAMGINDL LHFDFMDPPP TNTMLTALEE LYALSALDDE GLLTRLGRKM ADFPMDPSMA
KVVIAAVDMG CCEEILSIVA MLSLPTVFYR PKEKQNQADQ KKSKFHDQHG DHLTLLNVYN
SWKQNKYANA WCFENFIQAR SMRRAKDVRD QLVKIMERYK HPIVSCGRDT QKVRQAFCSG
FFRNSARKDP QEGYKTLIEG TPVYLHPSSA LFGKQAEWVI YHTLVLTSKE YMHCTTSIDP
KWLVEAAPSF FKVAPTDKLS KRKKSERIQP LYNKFAAEDD WRLSAQKRQG RGGGGGTWG
//
