MAK5_LODEL
ID MAK5_LODEL Reviewed; 855 AA.
AC A5DUB2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; ORFNames=LELG_00948;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981524; EDK42770.1; -; Genomic_DNA.
DR RefSeq; XP_001528428.1; XM_001528378.1.
DR AlphaFoldDB; A5DUB2; -.
DR SMR; A5DUB2; -.
DR STRING; 379508.A5DUB2; -.
DR PRIDE; A5DUB2; -.
DR EnsemblFungi; EDK42770; EDK42770; LELG_00948.
DR GeneID; 5234662; -.
DR KEGG; lel:LELG_00948; -.
DR VEuPathDB; FungiDB:LELG_00948; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; A5DUB2; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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..855
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000294637"
FT DOMAIN 250..449
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 515..668
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..247
FT /note="Q motif"
FT MOTIF 386..389
FT /note="DEAD box"
FT COMPBIAS 10..31
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..149
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 855 AA; 96698 MW; E2107FA467C56247 CRC64;
MVKTVANGKK KPQKVVKKQQ KTQKKHNQQK LQKRNTPTLK QKLKKESKIV KINELAWKPV
EIPDNFGDFG GFYGLEEIDG VDVEMVDGKP QFVVKGEEGE KSVSNENTTT NELEDGDDIE
VDEGEEIAQQ EQENSDNDEL IEEDAEEVEE QQQHGEKELE EEEFTGFGDD IAKEEKDSDG
AKKKLNSSED IDELKYNAFA NLDLPLPNDD EIDLPEWGED KIETCLSPYI LNGLSNMKFT
TPTPIQKRTI PLALEGKDVI GKATTGSGKT LAYGIPILEK YIQSLDTVKR KVREKVVNHP
TGIIFAPTRE LAHQVVDHLN KIAQYSPLST KGIVSVTGGL SIQKQERLLS FGPGIIVATP
GRMLELCQND QELVKRLSMT DIIVLDEADR LLQDGHFEEF EKILELFNKN RPKNDKSIEW
KWQTLVFSAT FSRDLFGKLD KQQKQKSVKG NGKALNKADS GNSLVQNDEI IELLREKLRF
KDKAPSLVDA NPKEIVSGQI TEALVECGPL ERDLYLYYFL LMYKGSTLVF ANSIDSVKRL
VPLLNNLNIP AFAIHSSMIQ KQRLRSLERF KDASEKNQTA VLVASDVAAR GLDIPNIDHV
AHYHLPRSAD VYIHRSGRTA RAGKEGVSVM FCSPQEASGP LRKLRKLVAS NAANNKNQKI
NVHSDVKLLP VEMDLVSQLR PRVELAGRLA DSNISSTATR KENSWVKQAA EELGVEDLHD
LDEFEDDIIK KQRKRQESKR LDKNEQKRLR FELRELLANP IRKNNRRSYL TSGLQNLAHL
MVQGTHHEDV LGHEKVKALK DLQKNGSKIK PVKGDDKMKR IAKVNQRKQA KKDAKKDAKQ
KRQELRHGHS NKSEE
