ID A0A1Y2GMB1_9FUNG Unreviewed; 774 AA.
AC A0A1Y2GMB1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=BCR41DRAFT_337471 {ECO:0000313|EMBL:ORZ13848.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ13848.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ13848.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ13848.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORZ13848.1}.
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DR EMBL; MCFF01000022; ORZ13848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GMB1; -.
DR STRING; 64571.A0A1Y2GMB1; -.
DR InParanoid; A0A1Y2GMB1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000193648; 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 CDD; cd17973; DEXHc_DHX15; 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; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
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:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 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 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:ORZ13848.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000193648}.
FT DOMAIN 108..273
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 295..477
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 87549 MW; A732905D85308E15 CRC64;
MSDSKSQKLV KAEKDAEAPQ ENPYLAHLPP SERLVGGAAA SGRKNPYGLA PNHPLANFVI
GATTAEQAEA AEEGDINPFT DKPFSDKYRK ILAGRRKLPV NKHRKEFLNL VQNNQVVILV
GETGSGKTTQ IPQFLVFDEL PGFKGKKIAC TQPRRLAAMS VAQRVAEEMD VVMGQEVGYN
IRFEDCTSAS TILQYMTDGM LLREAMNDPL LTRYSAIILD EAHDRTLSTD ILMGLMKEII
RKRSDLKVVV MSATLDAGKF QKYFDDAPLM SVPGRTFPVE IYYTPEPESD YLEAAIFTAL
QIHRSEDPGD ILLFLTGEEE IEDACKKIKM EADMMPDTGP VKVLPLYSTL PPQAQKRIYE
DAPPPRTPEG RPGRKIVVST NIAETSLTID GIVYVIDPGF SKQKVYNPRI RVESLLVSPI
SKASAQQRSG RAGRTRPGKC FRLYTENAFM KELIETTYPE ILRSNLGTVV LQLKKLGIDD
LVHFDFMDPP APETLMRALE LLNYLGALDD DGNLTPLGSI MADFPLDPQL AKMLIMSPQY
GCSNEIMTIV SLLNVPLVFV RPADQRKAAD EAKAQFAHPD GDHLTLLNVY HAYKTSGEDQ
KWCYDNYCNY RTLKSADNVR TQLKRYMERF DLDLVSLPFD ERPKGPYYTG IRKALVTGYF
MQVAHQERSG NYLTVKDNQV VRLHPSSCLD HAAEWVIYNE FVLTNQNFIR TVTEVKAEWL
LDIAPIYFDL DSFPNCEGKR VLEKLLRRRK DEEDMKKNRK SDRSDRDRDY KRRK
//
