SPB4_AJECN
ID SPB4_AJECN Reviewed; 676 AA.
AC A6R918;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 66.
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=HCAG_06809;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=EDN09642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH476660; EDN09642.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001539204.1; XM_001539154.1.
DR AlphaFoldDB; A6R918; -.
DR SMR; A6R918; -.
DR STRING; 339724.A6R918; -.
DR EnsemblFungi; EDN09642; EDN09642; HCAG_06809.
DR GeneID; 5445260; -.
DR KEGG; aje:HCAG_06809; -.
DR HOGENOM; CLU_003041_26_4_1; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000009297; 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; 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..676
FT /note="ATP-dependent rRNA helicase SPB4"
FT /id="PRO_0000310249"
FT DOMAIN 52..262
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 295..452
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 610..664
FT /evidence="ECO:0000255"
FT MOTIF 21..49
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 210..213
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 676 AA; 75663 MW; 9A7EB1A0E076260E CRC64;
MATSASRIAP TTPQSSHSRA WDALTPPLSE WILDAISAMG FSRMTPVQAS TIPLFMAHKD
VVVEAVTGSG KTLAFLIPVV ERLLRLESPI KKHHIGAILI SPTRELATQI YNVLLSLLAF
HGPSAARLQR TENNSGEVDE SNPASSYPPS TLKIVPQLLL GGTTTPTQDL SAFLKQSPNV
LVSTPGRLLE LLSSPHAHCS QSSFEVLVLD EADRLLDLGF KEDLQKILQR LPKQRRTGLF
SASVSEAVDQ IIRVGLRNPV KIAVKVKGAG LEDKRTPASL QMTYLLTPPT HKLPAVKYIV
STLSPTPQRS ILYFSTCAAV DYYQHILPCI LPDRFTTIPL HGKHPPQVRQ KNFTRFVNSV
TSSILLTTDV AARGLDIPAV DLVIQIDPPT DPKAFLHRCG RAGRAGRRGL SVIFLHPGRE
EDYIAFLNVR KTPVTEFQST STSTPSQLYS SSHFSASSPK NPQTFHPIQI TTADATSTTE
KIRALVLRDR AIHDKAQRAF VSWLRSYSKH QASSIFRVAD LDWEELGRAW GLLRLPTMPE
LKGFTGDRNL GVSGVDWDNY AYKDRQREKH RRMEMEGRSS SNVNNNGDAT GSDKGPLKRP
ATSESIPWSQ NLERKSEKER RRERKKIRRY HEQWKKMTEE EKERVRETEQ MVNAVRKAVQ
EQDQTVTREE EFEGFD
