SPB4_CHAGB
ID SPB4_CHAGB Reviewed; 646 AA.
AC Q2GV49;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=CHGG_08155;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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; CH408033; EAQ86902.1; -; Genomic_DNA.
DR RefSeq; XP_001225811.1; XM_001225810.1.
DR AlphaFoldDB; Q2GV49; -.
DR SMR; Q2GV49; -.
DR STRING; 38033.XP_001225811.1; -.
DR EnsemblFungi; EAQ86902; EAQ86902; CHGG_08155.
DR GeneID; 4393902; -.
DR eggNOG; KOG0345; Eukaryota.
DR HOGENOM; CLU_003041_26_4_1; -.
DR InParanoid; Q2GV49; -.
DR OMA; DRAIHDK; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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; 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..646
FT /note="ATP-dependent rRNA helicase SPB4"
FT /id="PRO_0000256048"
FT DOMAIN 46..247
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 284..434
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 539..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..623
FT /evidence="ECO:0000255"
FT MOTIF 15..43
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 195..198
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 558..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 646 AA; 71577 MW; 969A97452C531D85 CRC64;
MPPEQVRARK TPRSWGALTP SLAPWILDYL SSMGFEQPTP VQKSCFDIFR GNKDVVVEAV
TGSGKTLAFL IPVVERLLRS EDPAKRHHVQ AIIISPTREL ASQIYNVLVS FLKFHAPSAH
LLPHAKGDEK RPATTEPVVV PQLLVGGTTK AAEDLSTFLR LSPNILIGTP GRLAELLSTP
YVKAPSSSFE VLVMDEADRL LDLGFSQELT RILGYLPKQR RTGLFSASLS EAVERLITVG
LLYPHKITVR VKSLRDGGIV QERKTPMSLQ MSYIVTPASQ KIPALCQLLE RLEPRPSRSI
VFFSTCFAVK YFARVLHGIL PPGFSIVSLH GKLEPQVREK NFERFVNAAS PTVLLTTDIA
ARGLDIPQVD LVVQHDPPTD TKVFIHRCGR AGRAGRRGLA VVMLQPGREE GYVQLLDVRQ
TPISPLAKPP VSVTAADADL ASSRIRAQAR ADRDIYQLAQ RAFVSWARSY IEHQATSIFR
VADLDWADLA QGYGLLELPK MPEVRGLDRS LGLAIDTESI PFRDGAREKK RLAELEQWKK
EKAAREAQRA SGGGGDATDP LKRKKNEAWS GKHEHEDVKA ARREKKRRKR EAQRLGDMTE
PEREEQRKLD EMIAEVRRRN AEAPTPAAQA AGSGGGGGDE FEGFDD
