ID A0A1X2G5T0_9FUNG Unreviewed; 852 AA.
AC A0A1X2G5T0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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=DM01DRAFT_1368666 {ECO:0000313|EMBL:ORX45715.1};
OS Hesseltinella vesiculosa.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX45715.1, ECO:0000313|Proteomes:UP000242146};
RN [1] {ECO:0000313|EMBL:ORX45715.1, ECO:0000313|Proteomes:UP000242146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX45715.1,
RC ECO:0000313|Proteomes:UP000242146};
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:ORX45715.1}.
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DR EMBL; MCGT01000041; ORX45715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2G5T0; -.
DR STRING; 101127.A0A1X2G5T0; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000242146; 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:0046872; F:metal ion binding; 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; cd17967; DEADc_DDX3_DDX4; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF2; DEAD BOX RNA HELICASE-PL10B; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242146};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 26..55
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 78..107
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 207..235
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 238..426
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 438..598
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..235
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 91624 MW; 7C09E7522287D103 CRC64;
MSWGNDNYDM NNDQSFDNDR PKFTPRPGDW DCPSCGKSNF ARRSSCFRCD TAKPGDADNQ
YGGGDSYGYQ SHAPSGPRPG DWDCTGCGQS NFARRTDCFK CGEARPEGAG ASGGYGQNQG
AYDSARRTTG PVTDDVDAFR SYKWASSRAR YEYNANNLDE NGMARRNADL EKELFDDNAE
QQTTLDFSRY ESIRVSVERG ERPEPLKSFD EGDINPVMKE NIRLCKFAQP TPVQQYSIPI
VTRGDDLMAC AQTGSGKTAA FLVPTLSALF GKPELVQPRP QPYEYRTFCV EPLVLILAPT
RELCSQIFDD CRRYTYRSNL RPCAIYGGAA SFAQLRELER GCDILAAAPG RLMDFIQRRK
ISLKRVKYLI LDEADRMLDM GFEGIIRNIV EKQGLSPERQ TLMFSATFPR AIRKLARDFL
RSQYTFLKVG RIGGTTNSIT QKVMYVPEEE KREAVHALLN SQPPSRTLIF VETKRSADSL
DQYLFDLSFP TTSIHGDRTQ MEREDALQAF KSGQCPILVA TAVAARGIDI RNVMHVINYD
MPNDMDEYIH RIGRTARVGK SGLATSFYNE RSEHLAPLLT KLLKENNQPI PDFLEQFYSE
NVEWEEDQDD ENVAAPSYAG QDWTPQDRQP VGGPGSFANN ASGNKGAADA AFNSGGDWNG
GGGDNNGGGD WNAGGSAPWD SGNAGGNDGG WGNDNTNQAS GGWDSSAPAP AQQQAPAPTN
ANWGASDQQA PASSDGGWGA STDAPAAAPS NDGWGASAPA PAAAPSNDGW GAPSGAPAEA
PSNNGWGAPT NAPASAPAPA PAPAPSNDSW GTSAGASADA PSNDGWGAPA DAPSNDSWGA
APSGGGWGSA AP
//
