SPB4_PHANO
ID SPB4_PHANO Reviewed; 633 AA.
AC Q0UP45;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SNOG_06469;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445333; EAT86300.1; -; Genomic_DNA.
DR RefSeq; XP_001796839.1; XM_001796787.1.
DR AlphaFoldDB; Q0UP45; -.
DR SMR; Q0UP45; -.
DR STRING; 13684.SNOT_06469; -.
DR PRIDE; Q0UP45; -.
DR EnsemblFungi; SNOT_06469; SNOT_06469; SNOG_06469.
DR GeneID; 5973718; -.
DR KEGG; pno:SNOG_06469; -.
DR eggNOG; KOG0345; Eukaryota.
DR HOGENOM; CLU_003041_26_4_1; -.
DR InParanoid; Q0UP45; -.
DR OMA; DRAIHDK; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IEA:EnsemblFungi.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
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 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..633
FT /note="ATP-dependent rRNA helicase SPB4"
FT /id="PRO_0000282707"
FT DOMAIN 42..253
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 292..446
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 530..629
FT /evidence="ECO:0000255"
FT MOTIF 11..39
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 201..204
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 547..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 633 AA; 71204 MW; B82AA47631CAAF03 CRC64;
MAPQTKIDRS FSALTPALSE WIIDAVDAMG FVKTTPVQHA AIPMFMKNSD VVVEAVTGSG
KTLAFLIPIV ERLLREDAPT KKHHVGAIII SPTRELATQI HTVLSSLLKF HAPSAAMLEP
DDEDTDMEDA DTPPKPTFPP GTLKAVPQLL LGGSVTPAQD LSAFLKKSPN ILIGTPGRLL
ELLRSPHVHC PQSSFDALVM DEADRLLDLG FKEDLQKIIS RLPKQRRTGL FSASMSEAVD
QLIRVGLRNP VRIAVKVKAR ATGEDGKIED KRTPASLQMS YLVTPPSHKI PAMKKILSSL
QPQPQKSILY LSTCFSVDYF QHVLPEVLQG YDIVPLHGKH PDKVRRKNFN KFVDSVTPSI
LLTTDVAARG LDIPSVDLVF QLDPPSDPKT FIHRCGRAGR AGRRGLAVTF LNPGREEDYI
EFLQVRQTPI SPLTTPEITV TDEDAKAVTS KIRKKVREDR ALFDKAQRGF VSWVRAYSKH
TASSIFRIDD LDWTELGNAW GLLTLPGMPE LKKWQGDKRL GIELDLATYA YKDKAREKLR
LEELERDKEE GTKKKQHKKE DREKSAWTEQ KESKATKEVR REKKKSKREH ERLAKMTDEE
RKEEDRVQAM IEQMRKKVAK QEAEDADFEG FSD
