MAK5_CANAL
ID MAK5_CANAL Reviewed; 782 AA.
AC Q59ZH9; A0A1D8PHB5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
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=CAALFM_C205090WA;
GN ORFNames=CaO19.11024, CaO19.3540;
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 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; CP017624; AOW27527.1; -; Genomic_DNA.
DR RefSeq; XP_714899.2; XM_709806.2.
DR AlphaFoldDB; Q59ZH9; -.
DR SMR; Q59ZH9; -.
DR STRING; 237561.Q59ZH9; -.
DR PRIDE; Q59ZH9; -.
DR GeneID; 3643454; -.
DR KEGG; cal:CAALFM_C205090WA; -.
DR CGD; CAL0000200900; MAK5.
DR VEuPathDB; FungiDB:C2_05090W_A; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; Q59ZH9; -.
DR OrthoDB; 973872at2759; -.
DR PRO; PR:Q59ZH9; -.
DR Proteomes; UP000000559; Chromosome 2.
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: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; 2.
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..782
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000232231"
FT DOMAIN 228..426
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 478..635
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 197..225
FT /note="Q motif"
FT MOTIF 364..367
FT /note="DEAD box"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 782 AA; 88059 MW; 33E3DEB22FE54F45 CRC64;
MAKQGKNKVS KPRKPPTLKQ KLKKESKVVK AKDLQWKLVD IPDNLGDYEG FYGLEEIDGV
DVQIVNGKAE FIVRDNGKVE NKSKKEETNE NGENNMDVED NETPEVEDEK PTEQEEEEEE
EEEEEEEEEE EEEEEEFAGF EDDENNQEDA NTSERVSNND KDDKLAESND ELNAVSFANL
DLPLPDDNEI NLPNWQEGDL GSSISAYTLY GLSQLDFKKP TPIQKETIPI ALSGKDVIGK
ATTGSGKTLA YGIPILEKYI QSLNLIKQNN KDKKINHPTG IIFAPTRELA HQVVDHLNKL
AKYSPLSTRG IVSITGGLSI QKQQRLLRHG PGIIVATPGR MLELVQGDSE LAKRLASIDI
IVLDEADRLL QDGHFDEFEK ILELFGKNRP KSKSIEWKWQ TLVFSATFSR DLFRKLDRHQ
KGKSSSLMGN DEIVQLLNEK LKFKDKKPTL VDANPKEIVS GQITEALVEC GPTERDLYLY
YFLLMYKGST LVFANSIDSV KRLVPLLNNL NIPAFSIHSS MIQKQRLRAL EKFKEASQKN
EVAVLVASDV AARGLDIPNI DHVVHYHLPR SADVYIHRSG RTARAGKEGV SVMFCSPQEA
SGPLRKLRRL VAGNSNKESR LNMHNDVKLL PIEMDLVSQI KPRVEISSKL ADASISSTAT
RKEDSWVKQA AEDLGLDDLS GLEDFEDDII KKQRKRKEGK MLSKDETKAL KYELKTLLAN
PIKKNTRKSY ITSGLQNLAH QMVTGAHHDD VLGHEKVNAL SDLKGSKNKN KKIEKKRISK
KK
