MAK5_KLULA
ID MAK5_KLULA Reviewed; 796 AA.
AC Q6CTN7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; OrderedLocusNames=KLLA0C11253g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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. DDX24/MAK5
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382123; CAH01553.1; -; Genomic_DNA.
DR RefSeq; XP_452702.1; XM_452702.1.
DR AlphaFoldDB; Q6CTN7; -.
DR SMR; Q6CTN7; -.
DR STRING; 28985.XP_452702.1; -.
DR PRIDE; Q6CTN7; -.
DR EnsemblFungi; CAH01553; CAH01553; KLLA0_C11253g.
DR GeneID; 2891940; -.
DR KEGG; kla:KLLA0_C11253g; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; Q6CTN7; -.
DR OMA; HYHVPRT; -.
DR Proteomes; UP000000598; Chromosome C.
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:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..796
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000232237"
FT DOMAIN 250..446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 501..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..247
FT /note="Q motif"
FT MOTIF 379..382
FT /note="DEAD box"
FT COMPBIAS 142..173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 796 AA; 90131 MW; DF44B968D091718C CRC64;
MVYGVSKMAN KNRKNLKPVK SDRKDRISKN HSKKKVNKNS LKKVATTDIT VNANELNWKS
VDIPDTLDDF GGFYGLEEID GVDVKVVDGK VQFITKDNKN VKKEPEQVEE KDNIVFQEDD
EDVNMDELIE FKNFDDIKEG ELSAASDDEE SEFHVSTEEE GEEGEEAEDQ EEERSEKENV
KGEAGTVVTE DQTNDDLLQS NVFSSNVDID DQEPPVLPEW SENMDLSFTV LKGLSGLGFT
RPTEIQLKSI PLALKGHNIM GKASTGSGKT LAYGIPIIEQ LIKDTSNDRS IGLIFTPTRE
LAHQVTDHLQ KVWTKMNKLN KYTILSLTGG LSIQKQERIL KYDGSGRIIV ATPGRFLELL
ERNPDLIPRF AKIDTLVLDE ADRLLQDGHF DEFEKILKLL GKARKIKTSI DGKPTGSGWQ
TMIFSATFSL DLFTKLDKTS WKILKTAGGE NNEMEQVLNH LMKKIQFKSK PVIIDTNPEH
KVTSQVKESL IECLPMERDL YVYYFIMMYP GTTLVFCNAI DSVKKLNAFL NNLKISSFQI
HSSMAQKNRL RNLEKFKEQS EKNSKVGKPT ILIASDVAAR GLDISGIKHV LHYHLPRSAD
VYIHRSGRTA RGDNEGVSVM ICSPQESMGP LRKLRKVLST KKSSNPRKTK WQNDVPMLPL
EPDIVSQLRE RSKIASELAD DEIATKSLHK DDNWLKKAAE ELDIELDSEE EEKDQFLARN
KTKKLNKQLE KNENKALKYQ LNELLKMPLR KDLRKSYLTG GLTNLADTLV KHKGHNSIIG
HDKVDALQTL KGKKHK
