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DBP9_SCLS1
ID   DBP9_SCLS1              Reviewed;         607 AA.
AC   A7EM78;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=ATP-dependent RNA helicase dbp9;
DE            EC=3.6.4.13;
GN   Name=dbp9; ORFNames=SS1G_06425;
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. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476628; EDO03944.1; -; Genomic_DNA.
DR   RefSeq; XP_001592186.1; XM_001592136.1.
DR   AlphaFoldDB; A7EM78; -.
DR   SMR; A7EM78; -.
DR   STRING; 665079.A7EM78; -.
DR   GeneID; 5488646; -.
DR   KEGG; ssl:SS1G_06425; -.
DR   VEuPathDB; FungiDB:sscle_13g092700; -.
DR   InParanoid; A7EM78; -.
DR   OMA; GYEKDFK; -.
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: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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 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..607
FT                   /note="ATP-dependent RNA helicase dbp9"
FT                   /id="PRO_0000310256"
FT   DOMAIN          55..232
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          243..475
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          332..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..52
FT                   /note="Q motif"
FT   MOTIF           180..183
FT                   /note="DEAD box"
FT   COMPBIAS        335..352
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   607 AA;  67588 MW;  490FC03B7F5F0E35 CRC64;
     MKRKLDVNDV PVPTEEAEAA NGKATFASLG LDARLLQGIA KQNFQSPTLV QSKAIPLTLE
     GRDILARAKT GSGKTAAYLL PILHSILKRK ELSPTQCTSA LILVPTRELA DQVYKTVESF
     TAFCAKDVRA VNLTQRVSDA VQRSLLADSP DIVIATPARA SLNANTSALL LTNLTHMVID
     EADLVLSYGY DEDLQNVAKI MPKGVQTVLM SATLTSEVET LKGLFCRNPE VLKLEEAEDE
     GKGVSQFVVK CAEDEKFLLV YVIFKLKLIK GKCIIFVGDI DRCYRLKLFL EQFGTRSCIL
     NSQLPVNSRI HVVEEFNKNV YDIIIASDEH EVLGDEDEPK PEETEEVEAD DASGEKEDAK
     DAKKETKQPS KKKQKTGKKD KEYGVSRGID FKNVACVLNF DLPTSSKSYT HRIGRTARAG
     QTGMALSFVI PSALYRKHKP TSIESAKDDE KVLAKIIKHQ AKKGKEVKPY NFDMKQVDAF
     RYRMGDALRA VTSIAVQEAK AREIRQELMK SEKLKRHFEE NPSDLYHLRH DGELRPARVQ
     AHLKHVPDYL LPKEGKKGIT GGDIGFVGMH KTTENRIRKA RAANKAKGRG KGRKSDPLKT
     FKAKSRK
 
 
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