ID A0A150V7V6_9PEZI Unreviewed; 1194 AA.
AC A0A150V7V6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=M433DRAFT_192602 {ECO:0000313|EMBL:KYG46628.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46628.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG46628.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG46628.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG46628.1}.
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DR EMBL; JPDO01000108; KYG46628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V7V6; -.
DR STRING; 766039.A0A150V7V6; -.
DR Proteomes; UP000075602; 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: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; 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; 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 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:UP000075602}.
FT DOMAIN 230..300
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 538..701
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 719..899
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 133849 MW; 97E5C80BC6E5E0BB CRC64;
MDALEELEFL GLVGKVSDEI NNHMGVADTT IAEFVIAEHA KCADKADFYE KATKEFDFPQ
TLAESIDRLI RALHPKYKAQ DRVREAPRQN DGGDGGKSKK FKGLALPDKE PAFADESDKN
AMDDTFALLE SMAGPPKSNG RKRSMSPIES RETDGERGNK RYRRSRSRSQ SPQSRIRNDE
YLFEDEFGRT RPHRPVEGDR DTERRKYRKS RRDSYDQAPR QELDNQPVLY KVYDGRVTGV
KDFGVFVNLK GVKGKVDGLV HISAMADHKV NHPSDLVARD QEVKVKVMKI QDKRISLSMA
EVDQQTGQDL NPGRRLQTGA TGANAIGLNG ATNLVNPVPV IEGATGGGGR QRKRMTSPER
WEIRQLIASG VIKASEYPDI NEDYNAAMNG EQIEEEEDVD IEVREDEPPF LAGQTKRSLE
LSPIRVIKAP DGSMNRAAMQ GDVLAKERRE LRQQEAQDKA AQEASRTDLG QEWNDPMVAP
GERRFASDLR QPKPHPAAEV PEWKKIASGK GELGKRTNLS IKQQRESLPA FKMRKQFLDA
VKQYQLLIVV GDTGSGKTTQ LTQYLAEEGY ANEGMIGCTQ PRRVAAMSVA ARVSDEVGCR
VGEEVGYTVR FDDKTSDRTR IKYLTDGIMQ REILLDPTLS RYSVIMLDEA HERTIATDVL
FGLLKKTLKK RPDMKLIVTS ATLDAEKFSA YFNECPILSI PGRTFPVEIL YSREPESDYL
DAALTTVMQI HLTEPPGDIL LFLTGKEEID TSCEILYERM KALGPSVPEL IILPIYGALP
SEIASRIFEP TPPGSRKVVI ATNIAETSIT IDGIYFVVDP GFVKQTAYDA KLGMDRLQVT
PISQAQAKQR AGRAGRTGPG KCFRLYTESA FQNEMLPTTI PEIQRQNLAN TILMLKAMGI
NDLLGFDFMD PPPTNTMLTA LEELYALSAL DDEGLLTRLG RRMADFPMEP ALAKSLIMSV
ELGCSQEVLS IVAMISATQT VFHRPKEKQQ QADQKKARFH DPAGDHLTLL NVYNGWNSSG
KSDPWCYENF IQPRSMRRVE DVRKQLVQIL ERHRLKIISC GRDTTRVRQA LCSGFFRNSA
RKDPQEGYKT LVEGTPVYMH PSSALFGKGV EHVIYHSLVE TTREYMHNVT AIEPKWLVEA
APTFFKVAGK DGMGMSKRKR QERIQPLHNR FAGEDDWRLS AQRRQGRGGG GTWG
//
