MAK5_DEBHA
ID MAK5_DEBHA Reviewed; 790 AA.
AC Q6BV58;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; OrderedLocusNames=DEHA2C05170g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG85962.1; -; Genomic_DNA.
DR RefSeq; XP_457911.1; XM_457911.1.
DR AlphaFoldDB; Q6BV58; -.
DR SMR; Q6BV58; -.
DR STRING; 4959.XP_457911.1; -.
DR PRIDE; Q6BV58; -.
DR EnsemblFungi; CAG85962; CAG85962; DEHA2C05170g.
DR GeneID; 2900812; -.
DR KEGG; dha:DEHA2C05170g; -.
DR VEuPathDB; FungiDB:DEHA2C05170g; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; Q6BV58; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000599; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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..790
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000232234"
FT DOMAIN 230..427
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 483..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 199..227
FT /note="Q motif"
FT MOTIF 364..367
FT /note="DEAD box"
FT COMPBIAS 1..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 790 AA; 89112 MW; B69D00860CAE4879 CRC64;
MKVSKDKSKK GVKSKPKTSR KPLSLKQKLQ RESKIVKVDN LNWKAVDIPD NLDDYQGFYG
LEEIDGVDVK VTGGNVEFVV KDNSKVKDSD NEEDDDDVHD DDDNQDDGDD DQDDDDVDIE
DDEDEIIEGD NEDDFKGFDD DNAINEDDQM DIESAKTEKK SKKEVKPKNE KVAKKDSILE
SAFKNVDLTL PDDNEVNLPY WDDLSLSSFT LNGLSALEYE KPTAIQKRTI PLAIEGKDVI
GKAITGSGKT LAYGIPILER HLQKMAKANQ SKKVINPPTG IIFAPTRELA HQVVDHLNRI
AKFTPLSQHG IVSITGGLSI QKQERLLSHG PGIVVATPGR FLELLQKDMA LVQRLSCTDI
VVLDEADRLL QDGHFDEFVK ILELFGKHRP RDNKELEWKW QTLVFSATFS RDLFGKLDKH
LKSNKNKEEM GSSLIDNDEI LQLLNDKLKF KDSKPTLVDA NPKEMVAGQI TEALVECGPT
ERDLYLYYFL LLYPGSTLVF ANSIDSVKRL APFLNNLKVP TFSIHSSMIQ KQRLRTLERF
KEASSKNSTA VLIASDVAAR GLDIPNIDHV AHYHLPRSAD VYIHRSGRTG RAGKEGVSIM
FCSPQESSGP LRKLRKLVAN NTKKRTRLNV HNDVKLLPLE MDLVSQIKPR VTLASKLADA
ERSSSSTRKE DNWVHEAAEE LGIDNLSDID NFEDDFIKRQ RKRKENKALT KDEARSLRLE
LNDLLSKQIR KNSRRSYLTS GLQNLAHQMV TGNTHKDVLG HASVNALDDL RTKKAIKKKQ
IKTKKVKDKK
