GenomeNet

Database: UniProt
Entry: Q4HVW2
LinkDB: Q4HVW2
Original site: Q4HVW2 
ID   SPB4_GIBZE              Reviewed;         637 AA.
AC   Q4HVW2; A0A0E0SIG5; V6RV17;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   31-JUL-2019, entry version 85.
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};
GN   ORFNames=FGRRES_10896, FGSG_10896;
OS   Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
OS   (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
RA   Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
RA   Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
RA   Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
RA   Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
RA   Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
RA   Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
RA   Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
RA   Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
RA   Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
RA   Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
RA   Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
RA   Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus
RT   Fusarium graminearum.";
RL   BMC Genomics 16:544-544(2015).
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; DS231670; ESU17862.1; -; Genomic_DNA.
DR   EMBL; HG970334; CEF86228.1; -; Genomic_DNA.
DR   RefSeq; XP_011325484.1; XM_011327182.1.
DR   SMR; Q4HVW2; -.
DR   STRING; 5518.FGSG_10896P0; -.
DR   EnsemblFungi; ESU17862; ESU17862; FGSG_10896.
DR   GeneID; 23557776; -.
DR   KEGG; fgr:FGSG_10896; -.
DR   EuPathDB; FungiDB:FGRAMPH1_01G20749; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   InParanoid; Q4HVW2; -.
DR   KO; K14809; -.
DR   Proteomes; UP000070720; Chromosome 3.
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; 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    637       ATP-dependent rRNA helicase SPB4.
FT                                /FTId=PRO_0000232329.
FT   DOMAIN       45    247       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      283    438       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      58     65       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      524    631       {ECO:0000255}.
FT   MOTIF        14     42       Q motif. {ECO:0000305}.
FT   MOTIF       195    198       DEAD box. {ECO:0000305}.
SQ   SEQUENCE   637 AA;  71628 MW;  C4D5441E291587A4 CRC64;
     MATEKPKKRS PRAWDTLNPP LSEWIRDAVA TMGFDQMTPV QAATLPHFMG NKDVVVEAVT
     GSGKTLAFLI PLVQKLLRLS EPTKKHHVAA IIVSPTRELA AQIHTVLMKL LQFHEASAEI
     LPHLKDDDEK RPFTTVPAIV PQLLVGGTTT TVQDLRFFLR HSPNVLISSP GRLVELMSSP
     HVHCPQSSFE VLVLDEADRL LDLGFKPDLQ KILSHLPKQR RTGLFSASVS EAVGEIIRVG
     LRNPVKIEVK VKIKGGGILE DRKTPASLQM TYMVKPASQK LPALAELLRQ LPVRPQRSIV
     FLSTCAAVDY FQHILPLILP EGFALVPLHG KHAAKVREKN FNKFLSSVSP TILLTTDLAA
     RGLDIPQVDL VVQIDAPSDP KVFIHRSGRA GRAGRKGLAV VMLHPGREED YVQFLEIRKT
     PIAPLEKPTI TTSEDDAAEF AKKTRDFVLT DRGLFDKAQK AFVSWARSYG AHQATSIFRA
     ADLDWADLGN AWGLLRMPRM PELKGWTGDK MCGLEIDWDN YAYKEKTREQ QRKVALEEEK
     SGVKKQDKSE EFKRKRKNNE AWSAKHEKED DRVERREKRR KRRDAEATSK MTDDEKVKQM
     ELNDLIAEVR RQNREKAAAE AAAAKQEKDG EFKGFDD
//
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