GenomeNet

Database: UniProt
Entry: A1CR32
LinkDB: A1CR32
Original site: A1CR32 
ID   RRP3_ASPCL              Reviewed;         473 AA.
AC   A1CR32;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   31-JUL-2019, entry version 66.
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=ACLA_028280;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW08103.1; -; Genomic_DNA.
DR   RefSeq; XP_001269529.1; XM_001269528.1.
DR   SMR; A1CR32; -.
DR   STRING; 5057.CADACLAP00002065; -.
DR   PRIDE; A1CR32; -.
DR   EnsemblFungi; EAW08103; EAW08103; ACLA_028280.
DR   GeneID; 4701588; -.
DR   KEGG; act:ACLA_028280; -.
DR   EuPathDB; FungiDB:ACLA_028280; -.
DR   HOGENOM; HOG000268802; -.
DR   KO; K14777; -.
DR   OMA; KAKNRSI; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    473       ATP-dependent rRNA helicase rrp3.
FT                                /FTId=PRO_0000282694.
FT   DOMAIN       84    255       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      283    427       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      97    104       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        53     81       Q motif. {ECO:0000305}.
FT   MOTIF       203    206       DEAD box. {ECO:0000305}.
SQ   SEQUENCE   473 AA;  52198 MW;  88C660130956DBF3 CRC64;
     MSAVKKRKIA NKAPQYESDA ESSSSHESVA SKHSDNAEAQ DGPESSETKP APKSFKDLGI
     IDQLCEACAT MGYKAPTPIQ AESIPLALQD RDLIGLAETG SGKTAAFALP ILQALMDKPQ
     SFFGLVLAPT RELAFQISQS FEALGSTINV RCAVIVGGMD MVSQSIALGK KPHIIVATPG
     RLLDHLENTK GFSLRTLKYL VMDEADRLLD MDFGPLLDKI LKILPRERRT FLFSATMSSK
     VESLQRASLS NPLRVSVSSN KYQTVSTLLQ SYRFIPHKHK DIYLVYLLNE FVGQSAIIFT
     RTVHETQRIS FLLRALGFGA IPLHGQLSQS SRLGALGKFR SRSRDILVAT DVAARGLDIP
     SVDVVLNFDL PTDSKTYVHR VGRTARAGKS GVAISFVTQY DVEIWLRIEG ALGKKLDEYD
     LEKDEVMVLA ERVGEAQRQA IMEMKNFDEK KGTRAKKFGK GKRSRDEMDQ EEG
//
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