ID A0A0D7BW78_9AGAR Unreviewed; 788 AA.
AC A0A0D7BW78;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=CYLTODRAFT_385346 {ECO:0000313|EMBL:KIY74454.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY74454.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY74454.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY74454.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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 ECO:0000256|RuleBase:RU365068};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000256|ARBA:ARBA00037933}.
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DR EMBL; KN880431; KIY74454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BW78; -.
DR STRING; 1314674.A0A0D7BW78; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17949; DEADc_DDX31; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 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, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 132..161
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 168..389
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 434..629
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..161
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 57..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 86237 MW; C23DB1957442D448 CRC64;
MDDIVLNLAS DDAGPSRVSS KKGGRWTDRA KAKRGLKRKS GPEESATLPT PKRSRVQKPG
KSHETALEKT VKPSRSTHTS HGQATAHTPQ PRPQGQIISS LFSYNPKVEL PSQPTPFKAP
AKPSNAPLTD SSSFDGLGVD PLIGAHLSKK MEIEKPTAIQ RAVLPAILRN PDVHRDIFIQ
SQTGSGKTLA FLIPIIQDLL PLSTLSYIDR SIGTLAIIIA PTRELAQQIS EILEALLKMR
LRPEDASADD PASARFTRWL VSGLLIGGNT RTHEKARLRK GLPIVVSTPG RLLDHLQHSE
SFNVGKCRWL VMDEADRLMD LGFEETITGI LKGLEARRNL AIKAAEQGAG HEVGGWDWER
RRRTILCSAT MKEGVQNLAG TALDNPLLVK ATESDAVDTK NPTVADADAQ ENYTPPAQLS
QRYIVAPLKQ RLVTLIALLR TLITSRTAEG TKIVVFFSCT DSVDFHWQLL GRAKMNDGEE
AEEAVSDDDD EEEEEGKAAS ADSQIAMESS LLPGTSIYRL HGSLATQTRN QSLKQFSNNA
AKSSILFSTS VASRGLDLPQ VRAVVQYDLP TEGGAAEYVH RVGRTARAGK AGEAWSILTP
SEQDWVKWVE GQMKPEKVGD TPPTLQGVTP ESILQRGFGG KGAEYEARAT DVQLTFERWA
LQKENLALAQ QAFLSHMRAY ATHPSTEKHI FHVRHLHLGH LAKAFALRDA PKSISGKGKS
KKATDSHPPA KKRVNDAFLK RNKDTEARME AVVRSQGRLT KKKGMMVSSG ADEFQLAGGY
NLEKMFNS
//
