SPB4_CANAL
ID SPB4_CANAL Reviewed; 631 AA.
AC Q59N29; A0A1D8PNA5; Q59NP8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=ATP-dependent rRNA helicase SPB4 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P25808};
GN Name=SPB4; Synonyms=SPB41, SPB42; OrderedLocusNames=CAALFM_C501600CA;
GN ORFNames=CaO19.11631, CaO19.13677, CaO19.4154, CaO19.6298;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017627; AOW29593.1; -; Genomic_DNA.
DR RefSeq; XP_711358.2; XM_706266.2.
DR AlphaFoldDB; Q59N29; -.
DR SMR; Q59N29; -.
DR STRING; 237561.Q59N29; -.
DR PRIDE; Q59N29; -.
DR GeneID; 3647252; -.
DR KEGG; cal:CAALFM_C501600CA; -.
DR CGD; CAL0000185825; SPB4.
DR VEuPathDB; FungiDB:C5_01600C_A; -.
DR eggNOG; KOG0345; Eukaryota.
DR HOGENOM; CLU_003041_26_4_1; -.
DR InParanoid; Q59N29; -.
DR OMA; DRAIHDK; -.
DR OrthoDB; 973872at2759; -.
DR PRO; PR:Q59N29; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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..631
FT /note="ATP-dependent rRNA helicase SPB4"
FT /id="PRO_0000232323"
FT DOMAIN 41..235
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 265..429
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 583..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 525..594
FT /evidence="ECO:0000255"
FT MOTIF 10..38
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 183..186
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 631 AA; 72353 MW; 315908BEEA617889 CRC64;
MKSNTESLAW ENLRYDLHSW IKEAISSMGY PTMTPVQAST IPLLSGNKDV VVEAVTGSGK
TLSFVIPVLQ KISDRLYKPD SDGDLPEPVK RGHMLSIVLS PTRELANQIQ SVFNQVLQYL
PEDKGTRINT QLLVGSIGNV REDLNQFLTN QPQILIGTPG RILEFLGSSQ SIKTSSLEIV
ILDEADKLLD FSFEKDVINI LKKLPKQRRT GLFSATISSA GNTIFRTGMN NPVKVQVKSK
NYFGEQSNSP KSLQLSYMMI NPELKITTLL TILSKYQYKK AIVYFPTCTS VKHFYQIFNK
VYQQESSDEP LKFFSLHGQL NTKSRLKTLD NFTQGDINLY KHILMTTDVA ARGIDIPDVD
LVIQIDPPTD PNVFLHRCGR TGRANKVGRA IVMLNDNCQE EDYIGFMEVK GIFLTKQDIP
TSSATKNLHE NFQIKLRQYM LEDRARHELA VKSYVGFIRY YSKHIASSIF RLATLDYLGI
AKMYGLLRLP KMPETKYIDN SIMPTDGWLG EIIDMDKYSY ADKLQEKTRL ENLENDKLKK
IQDAKRRKEL KIKNEAWSSK SERKENKLDR KEKLKRKREA IEKQIMEEER LNDGGNKDEE
DEVVEDWKDM VRKNKKKQKK NNSIQGSFDD L
