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Database: UniProt
Entry: Q6FKS8
LinkDB: Q6FKS8
Original site: Q6FKS8 
ID   SPB4_CANGA              Reviewed;         617 AA.
AC   Q6FKS8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 100.
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}; OrderedLocusNames=CAGL0L08976g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
DR   EMBL; CR380958; CAG62136.1; -; Genomic_DNA.
DR   RefSeq; XP_449166.1; XM_449166.1.
DR   SMR; Q6FKS8; -.
DR   STRING; 5478.XP_449166.1; -.
DR   PRIDE; Q6FKS8; -.
DR   EnsemblFungi; CAG62136; CAG62136; CAGL0L08976g.
DR   GeneID; 2891097; -.
DR   KEGG; cgr:CAGL0L08976g; -.
DR   CGD; CAL0135944; CAGL0L08976g.
DR   EuPathDB; FungiDB:CAGL0L08976g; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   InParanoid; Q6FKS8; -.
DR   KO; K14809; -.
DR   OMA; RRHKETP; -.
DR   Proteomes; UP000002428; Chromosome L.
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: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   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..617
FT                   /note="ATP-dependent rRNA helicase SPB4"
FT                   /id="PRO_0000232325"
FT   DOMAIN          38..224
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          252..406
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         51..58
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           7..35
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           172..175
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   617 AA;  70790 MW;  1E33D196D4FCE603 CRC64;
     MGKSLEWADL DYELQPWIKK AINVSGFDSM TPVQASTIPM FAKNKDVVVE SVTGSGKTIA
     FVIPILEKII SEGINNSKFK KGHFYSLILA PTRELSMQIQ NVVSSFLEHY PEDQYPIRSQ
     LVVGTNEKSV RDDVNTLLDE RPQILIGTPG RVLDFLQSPS VKTSSCGMVV LDEADRLLDV
     SFFKDVEKIL NVLPKQRRTG LFSATISSAG TLIFKTGLRN PVKITVNSQG KNAPTTLNLF
     YSVMKPEEKL QNLIHIMNNI RFKKCIVYFS TCVSVTFFYQ YLKYLQQTDK TLREDLQVIS
     IHGKLTTQSR RKALSTFTES LSDCILLTTD VAARGIDIPD VDLVLQIDPP TDADIFLHRC
     GRTGRANKIG RAIVFLNEGR EEDYIPFMEV KNVDIEETDI NKNKISNDNN DEFYQRFTKW
     LLSDRANYDL SVKSYVAFIR YYSKHSATSI FRLQSLDYVS LGKMYGLFRL PRMPEITKYL
     QDKEKSGETV VGYYGEGWLM NPPPIDMDKY AYQDKKREKA RIEELKNLAQ INDKKKLKAE
     LKKKNMAWSS KTMTKEERQE RRKKLDLKRK AIELEIAAEA ERDESDTEIT QDWKDEILQK
     KKKKKVGSEM QGSFDDL
//
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