ID A0A0C9SL21_PLICR Unreviewed; 763 AA.
AC A0A0C9SL21;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PLICRDRAFT_126611 {ECO:0000313|EMBL:KII84726.1};
OS Plicaturopsis crispa FD-325 SS-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX NCBI_TaxID=944288 {ECO:0000313|EMBL:KII84726.1, ECO:0000313|Proteomes:UP000053263};
RN [1] {ECO:0000313|EMBL:KII84726.1, ECO:0000313|Proteomes:UP000053263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII84726.1,
RC ECO:0000313|Proteomes:UP000053263};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JUN-2014) 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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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DR EMBL; KN832569; KII84726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9SL21; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000053263; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
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; 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; SM00382; AAA; 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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053263}.
FT DOMAIN 90..256
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 283..469
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 85623 MW; BDBD06B587D4CCE3 CRC64;
MSGARDNPYL AHLPPNQRGA GGPSGSGGND PAAREPLYGF MPRRVKADQV RKALDHDLNA
FTKQPHSAQY KKILEMRRKL PVYGQMDEFY EMFSKNQIIV MVGETGSGKT TQIPQFVAYS
DLPHTRGKLV ACTQPRRVAA MSVAKRVADE MDVQLGRQVG YSIRFEDMTE PGTTFLKYMT
DGMLLREAMN DPNLDRYSTI ILDEAHERTL ATDILMGLLK ALAKKRSDLK IIIMSATLDA
LKFQKYFGLT EEGAAPLFKV PGRTHPVEVF YTQEPEPDYV EAAIRTVLMI HRAEDPGDVL
LFLTGEEEIE DACRKIKLEA DDLVNQDPDS VGPLVCIPLY SSLPPQQQQR IFDAPPAARP
GGPPGRKVVV STNIAETSLT IDGIVYVVDP GFSKQKVYNP RIRVESLLVS PISKASAQQR
AGRAGRTRPG KCFRLYTEKD FMSELEEQTH PEILKSNLAN TVLELVKLGI KDLVRFDYVD
APAPETLMRA LELLNYLAAL DDEGNLTPLG AIMAEFPLDP QLAKMLIVSP EFKCSNEILT
ITAMLSVPNV WIRPNNQRRE ADAAKALLTV PDGDHLTLLN VYNNYVQNKH DKNWTWTHYL
SARALAQADN VRAQLQRSME RFDVDLVSMT DERKLYVNIR QALVCGFFMQ IAHKEGEKGN
YLTVKDNQVV ALHPSCGLDT QPEWVIFNEF VLTTRPYIRM VSDIRPEWLF EFAASYFDLA
SFPDGETKRA LQRIMNKRAG KAGGRVDAGS SDVRDAKKRK KNK
//
