ID J4KMM8_BEAB2 Unreviewed; 895 AA.
AC J4KMM8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=BBA_06933 {ECO:0000313|EMBL:EJP64229.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP64229.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP64229.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP64229.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00003706}.
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. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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DR EMBL; JH725170; EJP64229.1; -; Genomic_DNA.
DR RefSeq; XP_008600252.1; XM_008602030.1.
DR AlphaFoldDB; J4KMM8; -.
DR STRING; 655819.J4KMM8; -.
DR GeneID; 19889945; -.
DR HOGENOM; CLU_003041_5_1_1; -.
DR InParanoid; J4KMM8; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EJP64229.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 85..113
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 116..288
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 333..495
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 85..113
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 328..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..668
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 99195 MW; 168CE633984DEE95 CRC64;
MSRRAVSPAA SEPEMDIFGS IYPGDDTNGK QNGAATADTD FDFDGLMNGH DQGNEDDDEA
FIALKQAASF RKTSNLKGRT VKKGGGFQAM GINATLLKAI ARKGFSVPTP IQRKTIPLVL
DRKDVVGMAR TGSGKTAAFV IPMIERLRAH SAKFGSRALI MSPSRELAIQ TLKVVKELSK
GTDLKAVLLV GGDSLEEQFG FMAANPDIVI ATPGRFLHLK VEMKLDISSI KYVVFDEADR
LFEMGFAAQL TEILHALPLS RQTLLFSATL PTSLVEFARA GLQDPSLVRL DADTKVSPDL
QSAYFSIKGD EKEGSLLHIL HDVIKVPVGE PENNDDTGKD SKKRKRGPDG PARPTQHSTI
VFTATKHHVE YIANLLQWAG FAVSHVYGSL DQTARRIQVE DFRHGKTNIL VVTDVAARGI
DIPVLANVIN YDFPSQPKIF VHRVGRTARA GQRGWSYSLV RDTDAPYLLD LQLFLGKQLV
IGQEKEKPSY ADDVVVGSLE RNSLEEHVEW FNRVIHDNDD ISALQKVSIK AERLYLKTRN
SASSQSAKRA REVVASGAWV QLHPLFGNDV DHDEKSRAEM MAKISGFRPN ETIFEIGRSD
KASNEAADVM KQLRKKITPR RRQEAEAEAE EEIDDDEVGA PAMNDFDDAT DDDTGLGAVD
EDSDEDLEVT VSNAGKSKKD RDDWRDSEIF MSYTPRTVNA AEERGYGVHS GGAGSSFVEA
ARDVTMDLGN DESAKSFGEA NKQRLRWDKK SKKYVSRHND EDGSKGAKLV TGESGVKIAA
SFQSGRYDKW RKAHRIGRTQ RVGEDEKAGA AALLSQGGVR YKHKQEKAPK AADKYRDDYQ
VRKKRVDEAR EKRVGRFRDG AGSKKEIKGV HDIRKAREEK QKRKEKNARP MRKRS
//
