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Database: UniProt
Entry: A7F8V8
LinkDB: A7F8V8
Original site: A7F8V8 
ID   DBP7_SCLS1              Reviewed;         877 AA.
AC   A7F8V8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   16-OCT-2019, entry version 65.
DE   RecName: Full=ATP-dependent RNA helicase dbp7;
DE            EC=3.6.4.13;
GN   Name=dbp7; ORFNames=SS1G_14039;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   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
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH476649; EDN99179.1; -; Genomic_DNA.
DR   RefSeq; XP_001584942.1; XM_001584892.1.
DR   SMR; A7F8V8; -.
DR   STRING; 5180.EDN99179; -.
DR   PRIDE; A7F8V8; -.
DR   EnsemblFungi; EDN99179; EDN99179; SS1G_14039.
DR   GeneID; 5481078; -.
DR   KEGG; ssl:SS1G_14039; -.
DR   EuPathDB; FungiDB:SS1G_14039; -.
DR   InParanoid; A7F8V8; -.
DR   KO; K14806; -.
DR   OMA; FSRIQWL; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    877       ATP-dependent RNA helicase dbp7.
FT                                /FTId=PRO_0000310218.
FT   DOMAIN      288    484       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      512    719       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     301    308       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       255    284       Q motif.
FT   MOTIF       417    420       DEAD box.
SQ   SEQUENCE   877 AA;  96640 MW;  1BDA4018C32FF3D3 CRC64;
     MADDGMLMNF EIGEVPIVTK QSFKGGRWKD RLAAKKTAQH RVSRSTSKPS TREIFSERQH
     DTGAEEYIGR EPSLRAPKRQ RVDDNYDSYG GRNESTAAYA SGKLPSGSIN LGRGRKTTFQ
     EETRPAFVAG KLPPGSINIS GKKATPIQEE TRPAFVSGKL PPGSINSGAR KAISFQEEKK
     PAYISGKLPH GSIDGMRNRE MAAVHREIAE GGRKPGQVVS SLFTFNPTSK KKFDEPEEES
     EPAKPSNAPL TEEMATFTNL GLSRRLAAHL STKLDMKAPT AIQKASVTQL ISDDSDAFIQ
     AETGSGKTLA YLLPIVERIL ALSDNGIQIH RDSGLFAIIL SPTRELCKQI AAVLEKVLRC
     APWIVGTTVN GGESKQSEKA RLRKGVNILV ATPGRLADHL DNTEVLNVAT VRWLVLDEGD
     RLMELGFEEE IKGIVEKIGR RSVASGSSEM MSLPKRRVTI LCSATMKMNV QRLGEISLKD
     AVHIQADPSE QEKQDKANGI EADDKAFSAP TQLKQSYAIV PAKLRLVTLT ALLKRAFARK
     GSVMKAIVFM SCADSVDFHF SLFSRSAEKS AEASEEGKVD PPTLPKSELI KETITHGATI
     SNNSNPVILH KLHGSLAQNI RTATLKAYSE SADPCVLICT DVASRGLDLP NVDFVIEYDP
     PFSAEDHLHR VGRTARAGRE GRALIFLMPG TEEEYVSILA SGYREGRKAL THHTAEDLIQ
     KGFGGTGREW EERATNFQLE VERWSLDSPR YLEMARRGFQ SHIRAYATHV ANERHIFNMQ
     ELHLGHLAKA FALRDKPGSI KVPGLRPAKM TKADRSVAAR KAKRGEKEEE KAPEGERVRK
     QRKMELDLPT VDSNEVAARM KRKMKEHMSA ASEFNIG
//
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