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SPB4_GIBZE
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   03-AUG-2022, entry version 95.
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 ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., 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=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., 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=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
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 Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates
CC       from pre-60S ribosomal particles after processing of 27SB pre-rRNA.
CC       Required for the normal formation of 18S rRNA through the processing of
CC       pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and
CC       5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
CC       {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 box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS231670; ESU17862.1; -; Genomic_DNA.
DR   EMBL; HG970334; CEF86228.1; -; Genomic_DNA.
DR   RefSeq; XP_011325484.1; XM_011327182.1.
DR   AlphaFoldDB; Q4HVW2; -.
DR   SMR; Q4HVW2; -.
DR   STRING; 5518.FGSG_10896P0; -.
DR   EnsemblFungi; ESU17862; ESU17862; FGSG_10896.
DR   GeneID; 23557776; -.
DR   KEGG; fgr:FGSG_10896; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G20749; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   HOGENOM; CLU_003041_26_4_1; -.
DR   InParanoid; Q4HVW2; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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   Gene3D; 3.40.50.300; -; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..637
FT                   /note="ATP-dependent rRNA helicase SPB4"
FT                   /id="PRO_0000232329"
FT   DOMAIN          45..247
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          283..438
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          535..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          524..631
FT                   /evidence="ECO:0000255"
FT   MOTIF           14..42
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           195..198
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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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