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Database: UniProt
Entry: Q0CQF3
LinkDB: Q0CQF3
Original site: Q0CQF3 
ID   SPB4_ASPTN              Reviewed;         639 AA.
AC   Q0CQF3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   31-JUL-2019, entry version 70.
DE   RecName: Full=ATP-dependent rRNA helicase spb4 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P25808};
GN   Name=spb4 {ECO:0000250|UniProtKB:P25808}; ORFNames=ATEG_04081;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of
CC       60S ribosomal subunits. Binds 90S pre-ribosomal particles and
CC       dissociates from pre-60S ribosomal particles after processing of
CC       27SB pre-rRNA. Required for the normal formation of 18S rRNA
CC       through the processing of pre-rRNAs at sites A0, A1 and A2, and
CC       the normal formation of 25S and 5.8S rRNAs through the processing
CC       of pre-rRNAs at sites C1 and C2. {ECO:0000250|UniProtKB:P25808}.
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:P25808};
CC   -!- SUBUNIT: Component of pre-60S ribosomal complexes.
CC       {ECO:0000250|UniProtKB:P25808}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P25808}.
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. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH476598; EAU35883.1; -; Genomic_DNA.
DR   RefSeq; XP_001213259.1; XM_001213259.1.
DR   SMR; Q0CQF3; -.
DR   STRING; 33178.CADATEAP00009227; -.
DR   PRIDE; Q0CQF3; -.
DR   EnsemblFungi; EAU35883; EAU35883; ATEG_04081.
DR   GeneID; 4318460; -.
DR   EuPathDB; FungiDB:ATEG_04081; -.
DR   HOGENOM; HOG000268803; -.
DR   OMA; RRHKETP; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; 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; IPR025313; DUF4217.
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; 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; 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; Coiled coil; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    639       ATP-dependent rRNA helicase spb4.
FT                                /FTId=PRO_0000282705.
FT   DOMAIN       45    249       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      283    437       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      58     65       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      521    624       {ECO:0000255}.
FT   MOTIF        14     42       Q motif. {ECO:0000305}.
FT   MOTIF       197    200       DEAD box. {ECO:0000305}.
SQ   SEQUENCE   639 AA;  71347 MW;  AC6C61FC3F56F644 CRC64;
     MAPKPPAGTS SRAWEAVSPS LSEWVLDAVA SWGFSKMTPV QASAIPLFMA HKDVVVEAVT
     GSGKTLSFLV PVVEKLLRLE EPIKKHHIGA IIISPTRELA SQIHQVLLSL LAFHPPSAAA
     IKPPGEDDAP REKFSASTLK VVPQLLLGGS TTPAEDLSYF LKHSPNVLIS TPGRLLELLS
     SPHVHCPQSS FEMLVLDEAD RLLDLGFKET LQNILRRLPK QRRTGLFSAS ISEAVDQIVR
     VGLRNPVKVL VKVKGTSGVQ DKRTPASLQM TYLTTPPAHK FLTLRPILTS LQPTPQKTIF
     FVSTCSGVDY LAAILPLLLG DDFQLIPLHG KHPANVRQKN FNRFINAHTP SILLTTDVAS
     RGLDIPSVDL VVQIDPPSDP KTFIHRCGRA GRAGRRGVSV VLLHPGREED YVSFLEVRKT
     PVTPFPHPIS ISDSDASTAT EAARKIIKQD RALHDRGQKA FVSWLRSYSK HQASSIFRVA
     DLDWEALGHA WGLLKLPKMP ELRNFTGDRT LGVDLDWENY AYKDKQREKR RKEVLQESAE
     AGAQQTSNKR RASESVAWSN KVDQKNKKQK RREQKHLQQE KRRWEKMTEE EKQKARETQK
     MLEEIRQKNE EARALRRAEK AAGKAADNDG DDDEFEGFD
//
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