ID A0A0C9M1J4_9FUNG Unreviewed; 1912 AA.
AC A0A0C9M1J4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=ATP-dependent RNA helicase Dbp8 {ECO:0000313|EMBL:GAN02281.1};
GN ORFNames=MAM1_0019c01723 {ECO:0000313|EMBL:GAN02281.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02281.1};
RN [1] {ECO:0000313|EMBL:GAN02281.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02281.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF836308; GAN02281.1; -; Genomic_DNA.
DR STRING; 91626.A0A0C9M1J4; -.
DR OrthoDB; 2027807at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 CDD; cd17955; DEADc_DDX49; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR031968; VASt.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF21; RNA HELICASE; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS51778; VAST; 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:GAN02281.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 299..399
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1047..1220
FT /note="VASt"
FT /evidence="ECO:0000259|PROSITE:PS51778"
FT DOMAIN 1494..1522
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 1525..1697
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1711..1873
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 466..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1844..1871
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 1494..1522
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 469..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1912 AA; 212261 MW; CBDE197E48FBC5BD CRC64;
MQLPVDNPQS TLLTLHDAIT DSPVYRSTTL HFDDQLELLE KWLESLSKYM KLYVNQLNKF
NLETNTLCKK VIPVGIDDSM IDPNFTGAVI KSFSDALQTG LAFKTKLVSD LEDSFIQPLQ
LFVKTHLKDF KDFRKQHEKT LERYDAQLYK YTAQSKTKEA SAVREEAFRL YEARKSYVRM
SGQHVVRILH FRSLLEHFLV ERFALASSFH LKDFEGGSDS WSKLQSKLIS WKQWLLDDKE
TCNYQLDQLQ SSRITLETKF LNVVRPARDL EKYNINANQQ ANSRHSLDYS SVINSANQPS
HKWGYLFARG ARNYWNRKWF FLYDGCFGSC NVNASNRLKG TITMGERVSV LLCDIKPLND
VDRRYCFEVM CAHQPSFVLQ AETEEDMREW MAAFEKSKRL MLQTEQLDYK SGTSTATTTA
INASSATDTD ATLLNNSPPM ANSTALIAKA KPTTMLDELP AVSANSPLID TGLEGSSEQQ
QQQQQQASQK PSIVMLSTSP ENDQQSLTQS TSLTPLLVWE ASRASLNTSS TLPTSVPSSP
ATQSFSAAAL SLDAALTDSD EANPNANGTN GNSTVSGNAT GTSSSWGIPW ALVPSMFQGG
STDDITSELP PTPGSPNVPA VTDAEGHQII WPTRVDDSNV PKVELSGYPS DLDARNRELR
HLFGGVSPSE VVLTTFIGLL KRKPLHDPNE LKDVETPASP TSASNPVDTL EQEFNSQLST
TIKEPSSSYG YSYTGRGFIT QETFWFYSCV LMNCVNTVAI RLCDIKTIRL IRDPSVANIG
TSSNLALAID LASSSGTNDA QSPLIFTTLM DDIEVIAEKL KFAVSNAKSA EPEPLQTAYD
VIHSLSAVVN KSKSSNQVRT IIKSATDPVR STSDVTSNNS STVSLNSLSS AGSTLLDPNV
SPLPSRSSDP KKKTSKTPRK YSAPVQPKSG ALAAAMMAAT VAGGSGFLDA RKGIQEESRG
LLRSKRSKAT LHSEESDIPP VPVPSSSLSS SASSMVNVPS KLADSTTLKD VAETEIPEVP
KAKDPHAVPD DFSHPSGPVS CGCENHLDKL EAEIEVPISA KHLYYIMFAE ENPHAIDIWE
KKTVENKSKD LTMTPWQTVD GKKERTLKYI IPVNNAMVKL KEAEVVEKQV IEKKDDYLRY
IVLTSTKTAQ LPYADAFVPY VKYCITWVTH DRCKLACHTG VKFLKNILVK GMVSKAASKG
MAENLSVFMP IVKQEASKHT HRKRSGSKEK ADQVSLKRMG TIKRPTAKDA SDLTEKGNKE
EAAAAGGWYG ELEKLVNMVQ DLTEVVPFAV KVGIAVVILL WFMFSWLRAG SRQQLMVPKS
SSEQTPQVVS RAVYLRDINE GLLNVEYEPA YGHSESFRSF LESKSGNRTS GAHPHRWYSS
HHHQFAIELL FSRERLAMLR HDTMVLFQLV NEVDAQLLEN EYTNWLMDTR LQCRASDADY
DGLHCDDHLL LFSSIQHYSL TFMAAAPSRT LSRVAASQKK AAEKKQQTIA PEGSSFIDIG
VEAWLSDTLK SMSIKEPTEI QRACIPPILA GKDVIGGAKT GSGKTAAFAL PILQKLSEDP
YGVFALVLTP TRELAFQIAE QFRVLGKGMG VKECVVVGGM DMMAQALELA KRPHVIIATP
GRLRDHIRSS SGAVDLRRCK FLVMDEADRM FTPTFVPELE VILPLLPKQR QTLLFTATMT
ESILALRDAE EDPKKQPFVH MCDMSTSTVN TLDQYYVFVP SQVRMVYLAH LLRTDDLKEK
SIIIFCGRCS TAELMTIMLK ELGIRCTALH SEMTQQQRLD SLGKFRAEVI KILISTDVGS
RGLDIPSVEC VLNYDIPRDP TDYIHRVGRT ARAGRDGKAI SIVAEKDIQL IQNIEERINK
KMEKYDVNEN EILEELSEVT AAKREASMQL HDKQFGAKTH IRKKKKMAKQ ED
//
