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Database: UniProt
Entry: Q5B8F4
LinkDB: Q5B8F4
Original site: Q5B8F4 
ID   SPB4_EMENI              Reviewed;         638 AA.
AC   Q5B8F4; C8VID7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   16-OCT-2019, entry version 96.
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=AN3176;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000052; EAA62940.1; -; Genomic_DNA.
DR   EMBL; BN001306; CBF83255.1; -; Genomic_DNA.
DR   RefSeq; XP_660780.1; XM_655688.1.
DR   STRING; 162425.CADANIAP00009893; -.
DR   EnsemblFungi; CBF83255; CBF83255; ANIA_03176.
DR   EnsemblFungi; EAA62940; EAA62940; AN3176.2.
DR   GeneID; 2873958; -.
DR   KEGG; ani:AN3176.2; -.
DR   HOGENOM; HOG000268803; -.
DR   InParanoid; Q5B8F4; -.
DR   KO; K14809; -.
DR   OMA; RRHKETP; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; 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:0003723; F:RNA binding; IBA:GO_Central.
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; 2.
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    638       ATP-dependent rRNA helicase spb4.
FT                                /FTId=PRO_0000232328.
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    629       {ECO:0000255}.
FT   MOTIF        14     42       Q motif. {ECO:0000305}.
FT   MOTIF       197    200       DEAD box. {ECO:0000305}.
SQ   SEQUENCE   638 AA;  71063 MW;  2091AF2ED31C856F CRC64;
     MAPKPPSGTS SRAWDAVNPP LSEWVLDAVS SMGFTRMTPV QASAIPLFMA HKDVVVEAVT
     GSGKTLSFLI PVVEKLLRLE EPIKKHHVGA IIVSPTRELA SQIYNVLTSL LAFHPASAAV
     INTSETEDVP RPKHSSSVLR VVPQLLLGGS TSPAEDLSTF LKRSPNLLVA TPGRLLELLS
     SPHVYCPQSS FEMLVLDEAD RLLDLGFKET LQNILRRLPK QRRTGLFSAS VSEAVDQIVR
     VGLRNPVKVV VKVKGASGVD DKRTPASLQM TYLTQPPTGK FPALKHILNS VQPTPSKSIF
     FVSTCSGVDY LSVILPLILG NDFQLIPLHG KHPANVRQKN FNRFVNAHNP AILLTTDVAS
     RGLDIPSVDL VVQIDPPSDP KTFIHRCGRA GRAGRRGLSV VLLHPGREED YVSFLEVRKT
     PVAPFPHPIT VSDAEAAAAT ETARKVVKAD RAIHDRGQKA FVSWLRSYSK HQASSIFRVA
     DLDWEGLGKA WGLLKLPKMP ELKNFKGDKT LGVQMDWDTY AYKDKQREKR RLELLQEMAE
     SGQQQTTNKK RPNETVAWSN NAENRNKKAK RRDMKQVRQE RKRWEKMTEE EKKKALETEQ
     MLEQIRAKNE EQRRLKRAAA KADKDAEEGG DEEFTGFD
//
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