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DBP7_SCLS1
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   03-AUG-2022, entry version 76.
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 mold)
OS   (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., 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; CH476649; EDN99179.1; -; Genomic_DNA.
DR   RefSeq; XP_001584942.1; XM_001584892.1.
DR   AlphaFoldDB; A7F8V8; -.
DR   SMR; A7F8V8; -.
DR   STRING; 665079.A7F8V8; -.
DR   EnsemblFungi; EDN99179; EDN99179; SS1G_14039.
DR   GeneID; 5481078; -.
DR   KEGG; ssl:SS1G_14039; -.
DR   VEuPathDB; FungiDB:sscle_10g079110; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   InParanoid; A7F8V8; -.
DR   OMA; AVHIKAD; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
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   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..877
FT                   /note="ATP-dependent RNA helicase dbp7"
FT                   /id="PRO_0000310218"
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..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..851
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        51..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..849
FT                   /note="Basic and acidic 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;  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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