MAK5_CANGA
ID MAK5_CANGA Reviewed; 733 AA.
AC Q6FY67;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; OrderedLocusNames=CAGL0A03652g;
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 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; CR380947; CAG57819.1; -; Genomic_DNA.
DR RefSeq; XP_444926.1; XM_444926.1.
DR AlphaFoldDB; Q6FY67; -.
DR SMR; Q6FY67; -.
DR STRING; 5478.XP_444926.1; -.
DR EnsemblFungi; CAG57819; CAG57819; CAGL0A03652g.
DR GeneID; 2886320; -.
DR KEGG; cgr:CAGL0A03652g; -.
DR CGD; CAL0126771; CAGL0A03652g.
DR VEuPathDB; FungiDB:CAGL0A03652g; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; Q6FY67; -.
DR OMA; HYHVPRT; -.
DR Proteomes; UP000002428; Chromosome A.
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 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..733
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000232232"
FT DOMAIN 186..376
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 428..594
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 53..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..183
FT /note="Q motif"
FT MOTIF 315..318
FT /note="DEAD box"
FT COMPBIAS 59..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 733 AA; 82851 MW; 04C0036883A76C02 CRC64;
MGKRVVATDK ELKWKKVDIP DTLDDFGGFY GLEEIDGVDV KVVNGQVQFI ASEAQVKEEE
ESSESDFPDF DAMEQEDDGD VEEAEEEEEE EEDVAEADEP EVKQKQEQAR VEQIDKGVDS
EKHEDEKETP EDDLATNVFD IDVDLSDVGS GELPGWTDTV DLSMTTINGL SNLGFTEMTP
IQKLSIPAAL EGKDIMGKAS TGSGKTLAYG IPIIEKMIKS KDNLRTNGII FTPTRELAQQ
VTKHLQNVCS MLLKKNPYMI LSLTGGLSIQ KQERLLKYDG SARIVVATPG RFLELIEKNE
ELMKRFAKID VLVLDEADRL LQDGHFDEFE KILKHLGRIR KSLKNMEYWQ TLIYSATFST
DLFDKLANSS WKKKNNSKDE SEMESVLKHL MTKINFKSKP MMIDANPEDK ISAQIKESLI
ECAPLERDLY CYYFVTLYPG TTLIFCNSIE SVKKLNAYLI NLGINSFQIH SSMTQKNRLK
NLEKFEAMAS KNNHLGKPTV LIASDVAARG LDIKGIKHVV HYHLPHSADT YIHRSGRTAR
GDNEGVAVMI CSPQEAMGPL RKLRRLLASK EQISKSTKNK KWQQTVPLLP IEIDILQQLR
ERSSLANDIA EHELASRSLR KDSNWLKQAA DELGIDMDSD EEDKDIILAK NKNKKMNKTL
DKNELKSMKA ELTHLLKIPI RKDMRRSYLT GGLVNLADSL VKKRGHHNII GHEKTDALNV
LKKGKSNKKQ KTK
