SPB4_ASPOR
ID SPB4_ASPOR Reviewed; 638 AA.
AC Q2UBZ5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, 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=AO090012000805;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007161; BAE60920.1; -; Genomic_DNA.
DR RefSeq; XP_001727759.1; XM_001727707.1.
DR AlphaFoldDB; Q2UBZ5; -.
DR SMR; Q2UBZ5; -.
DR STRING; 510516.Q2UBZ5; -.
DR PRIDE; Q2UBZ5; -.
DR EnsemblFungi; BAE60920; BAE60920; AO090012000805.
DR GeneID; 5988233; -.
DR KEGG; aor:AO090012000805; -.
DR VEuPathDB; FungiDB:AO090012000805; -.
DR HOGENOM; CLU_003041_26_4_1; -.
DR OMA; DRAIHDK; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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 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..638
FT /note="ATP-dependent rRNA helicase spb4"
FT /id="PRO_0000232322"
FT DOMAIN 45..249
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 283..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 534..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..619
FT /evidence="ECO:0000255"
FT MOTIF 14..42
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 197..200
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 534..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 638 AA; 71581 MW; 656868F86A185261 CRC64;
MAPKPPAGTS SRAWDGVSPS LSEWVLEAVS SMGFTRMTPV QASAIPLFMA HKDVVVEAVT
GSGKTLSFLI PIVEKLLRLE EPIKKHHVGA IIISPTRELA SQIYHVLLSL LAFHPPSASV
INPSEDDDVP RQKFPSSTLK VVPQLLLGGS TTPAEDLSKF LKQSPNLLVS TPGRLLELLS
SPHVHCPQSS FEMLVLDEAD RLLDLGFKET LQNIIRRLPK QRRTGLFSAS ISEAVDQIVR
VGLRNPVKVM VKVKGTSGAQ DKRTPASLQM TYLTTPTIHK FDALKHILHS VDPTPQKTIF
FASTCSGVDY LSAILPLILG DDFQLISLHG KHPANVREKN FNRFVNSYSP AILLTTDVAS
RGLDIPSVDL VVQIDPPSDP KTFIHRCGRA GRAGRRGLSV VLLHPGREED YVSFLEVRKT
PVAPFPHPIS FSESEATAAT KAVRKAVLAD RALHDRGQKA FVSWLRSYSK HQASSIFRVA
DLDWESLGKA WGLLKLPKMP ELRNFTGDRT LGVNLDWDDY KYKDKQREKR RIELLQESKE
GDGTQESSNK RKATETTAWS NKLDDRNKKQ KRREQKQRRQ EKNKWEKMTE EERQKIRETE
QMVESIRVKN EEERRLRRAG KAEAANAGKD EEEFEGFD
