GenomeNet

Database: UniProt
Entry: A6RW56
LinkDB: A6RW56
Original site: A6RW56 
ID   RRP3_BOTFB              Reviewed;         486 AA.
AC   A6RW56;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   31-JUL-2019, entry version 68.
DE   RecName: Full=ATP-dependent rRNA helicase rrp3 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P38712};
GN   Name=rrp3 {ECO:0000250|UniProtKB:P38712}; ORFNames=BC1G_04843;
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.,
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-dependent rRNA helicase required for pre-ribosomal
CC       RNA processing. Involved in the maturation of the 35S-pre-rRNA and
CC       to its cleavage to mature 18S rRNA.
CC       {ECO:0000250|UniProtKB:P38712}.
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:0000250|UniProtKB:P38712};
CC   -!- SUBUNIT: Interacts with the SSU processome.
CC       {ECO:0000250|UniProtKB:P38712}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH476861; EDN23574.1; -; Genomic_DNA.
DR   RefSeq; XP_001556825.1; XM_001556775.1.
DR   SMR; A6RW56; -.
DR   PRIDE; A6RW56; -.
DR   GeneID; 5437409; -.
DR   KEGG; bfu:BCIN_11g03140; -.
DR   EuPathDB; FungiDB:Bcin11g03140; -.
DR   KO; K14777; -.
DR   OMA; KAKNRSI; -.
DR   OrthoDB; 744428at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 1.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN         1    486       ATP-dependent rRNA helicase rrp3.
FT                                /FTId=PRO_0000310231.
FT   DOMAIN       91    262       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      286    434       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     104    111       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        60     88       Q motif. {ECO:0000305}.
FT   MOTIF       210    213       DEAD box. {ECO:0000305}.
SQ   SEQUENCE   486 AA;  53961 MW;  790584B86ADE963E CRC64;
     MSSVKRRKTD KNPSLEGLKS KKTKESKKES HTPSPEPIED TEDNRVIEET EEAEEDDAPK
     SFKDLGIVDS LCEACDTLGY KAPTPIQRES IPLALQGRDL IGLAETGSGK TAAFALPILQ
     ALLDKPQPLF GLVLAPTREL AYQISQQFEA LGSVIRVKCA VIVGGMDMVP QSIALGKKPH
     IIVATPGRLL DHLENTKGFS LRSLKYLVMD EADRLLDLDF GPILDKILKV LPRERRTYLF
     SATISSKVES LQRASLKDPL RVSISSNKYQ TVSTLIQNYI FIPLIHKDTY LIYLLNEFAG
     QSAIIFTRTV NETQRIAILL RTLGFGAIPL HGQLSQSSRL GALNKFRAGS REILVATDVA
     ARGLDIPSVD VVLNYDVPQD SKTYIHRVGR TARAGKSGHA ISVVTQYDLE IFMRIEAALG
     KKQVEYPTVK DEVMVFKPRV EEAQRHARNE MKNLHEDRGK KGAVLKGRRP ANGAKRGRDE
     MDREEG
//
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