ID A0A2I1H4Q3_9GLOM Unreviewed; 818 AA.
AC A0A2I1H4Q3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, 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=RhiirA4_327835 {ECO:0000313|EMBL:PKY53824.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY53824.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY53824.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY53824.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) 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}.
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:PKY53824.1}.
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DR EMBL; LLXI01001466; PKY53824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1H4Q3; -.
DR VEuPathDB; FungiDB:FUN_007366; -.
DR VEuPathDB; FungiDB:GLOIN_2v1529594; -.
DR VEuPathDB; FungiDB:RhiirA1_340307; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000234323; 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: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; 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; 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, ECO:0000313|EMBL:PKY53824.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000234323}.
FT DOMAIN 118..283
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 308..490
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 92749 MW; A20744E3A71CC529 CRC64;
MDNKKRNAES AVEVTDQRNN ETDQTNSTHE HLNKRQRIGE TPIEENPYLA HLNKPARLNQ
ANSALDGFIP GKTTATQARR AEEGIYNPFN SKKFSQKYRD ILAIRRKLPV HAQRQEFLDL
VHSSQFVVFV GETGSGKTTQ IPQFLCYDVL PHLKKKQIAC TQPRRVAAMS VAQRVSDEMD
VKLGEEVGYN IRFEDCSSPK TILKYLTDGM LLREAMNDPK LEKYSAIILD EAHERTLATD
ILMGLMKQIA KVRPDLKVIV MSATLDAEKF QKYFNDAPVL TVPGRTFPVE IFYTPEPERD
YLEAAIRTVM QIHACEDPGD ILLFLTGEEE IEGACQKIKV ESEELLSQTE LGPLKILPLY
SSLPPPQQQR IFEDAPPPRT KDGKPGRKVI VSTNIAETSL TIDGIVYVVD PGFSKQKVYN
PRIRVESLLV SPISKASAQQ RAGRAGRTRA GKCFRLYTER AFLKELQEQT HPEILRSNLG
SVVLQLKKLG IDDLVHFDFM DPPAPETLMR ALELLNYLGA LDDEGNLTGD GHLMAEFPLD
PQLSKMLIES PKYRCSNEIL SIAALLSVPN IFVRPNDMKK QAEEAKAKFA HDEGDHLTLL
NVYHAYKSES RDRDADWCYD NFLSIRSLKS ADNVRQQLKR IMERCDEELV STPFTDGNYY
INIRKALTAG FFMQVAHLEK SGHYLTCKDN QIVQLHPSSS LKHQPEWVLY NEFVLTTKNY
IRTVTEVKAE WLLDIAPVYY DLKNFPNCEG KRVLEKILMR KSSKRPVVAA RSVIAAMKAD
RDNDQSKRPV VAAMKADRDN DQSKRPVVAA MKANKNSK
//
