DBP7_BOTFB
ID DBP7_BOTFB Reviewed; 877 AA.
AC A6RSH5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ATP-dependent RNA helicase dbp7;
DE EC=3.6.4.13;
GN Name=dbp7; ORFNames=BC1G_03202;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; CH476853; EDN19569.1; -; Genomic_DNA.
DR RefSeq; XP_001558170.1; XM_001558120.1.
DR AlphaFoldDB; A6RSH5; -.
DR SMR; A6RSH5; -.
DR GeneID; 5438779; -.
DR KEGG; bfu:BCIN_12g03020; -.
DR VEuPathDB; FungiDB:Bcin12g03020; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..877
FT /note="ATP-dependent RNA helicase dbp7"
FT /id="PRO_0000310217"
FT DOMAIN 288..484
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 512..719
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 34..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 255..284
FT /note="Q motif"
FT MOTIF 417..420
FT /note="DEAD box"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 877 AA; 96117 MW; 624AEEEF99ABFE8B CRC64;
MADDGMLMNF EIGDVPIVAK QAFKGGRWKD RLAAKKTAQH RVTKSTNKPS AREIFSEPQH
DTSAEEYIGR EASSRAPKRQ RVDDNYNSYG GRNENTAAYA SGKLPSGSIN VGGGRKTTFQ
EEPRTAFVAG KLPPGSINIG GKKATQIEDE GRAAYASGKL PPGSINSGAK KAISFQDETR
PAYVSGKLPH GSIDGMRNRE MAAVHREIAE GGRKPGQVVS SLFTFNPTSK KTFDEPEEQA
EPAKPSNAPL TEEMATFTNL GLSRRLAAHL STKLDMKAPT AIQKASVQQL VSDDSDAFIQ
AETGSGKTLA YLLPIVERIL ALSENGVQIH RDSGLFAIIL SPTRELCKQI AAVLEKVLRC
APWIVGTTVN GGESKQSEKA RLRKGVNILV ATPGRLADHL DNTEVLNVAT VRWLVLDEGD
RLMELGFEEE IKGIVEKIGR RSVAKANSDM GSLPKRRVTI LCSATMKMNV QRLGEISLKD
AVHIQADPSE QEKQDKENGV EAQDKAFSAP TQLKQSYAIV PAKLRLVTLT ALLKRAFARK
GSVMKAIVFI SCADSVDFHF SLFSRTPEAS AEVVDEEKVD LPALPKSELV KETIAHGTTI
SNNSNPVILH KLHGSLAQNI RTATLKAFSE SADPCVMICT DVASRGLDLP NVDFVIEYDP
PFSAEDHLHR VGRTARAGRE GRALIFLMPG VEEEYVSILA SGYREGKKAL TRHTAEDLIQ
KGFGGIGREW EERATNFQLE VERWSLDSPK YLEMARRGYQ SHIRAYATHV ANERHIFNMQ
ELHLGHLAKA FALRDKPGSI KVPGLRPAKM TKADRSVAAR KAKRGEKAED KAPEGERVRK
QKKMELDLPT VDGNEAAARM KRKMKEHMAA ASEFNIG
