MAK5_ASHGO
ID MAK5_ASHGO Reviewed; 752 AA.
AC Q757I6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; OrderedLocusNames=AER027W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016818; AAS52711.1; -; Genomic_DNA.
DR RefSeq; NP_984887.1; NM_210241.1.
DR AlphaFoldDB; Q757I6; -.
DR SMR; Q757I6; -.
DR STRING; 33169.AAS52711; -.
DR EnsemblFungi; AAS52711; AAS52711; AGOS_AER027W.
DR GeneID; 4621089; -.
DR KEGG; ago:AGOS_AER027W; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; Q757I6; -.
DR OMA; HYHVPRT; -.
DR Proteomes; UP000000591; Chromosome V.
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 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..752
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000227957"
FT DOMAIN 211..402
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 454..609
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 180..208
FT /note="Q motif"
FT MOTIF 340..343
FT /note="DEAD box"
FT COMPBIAS 10..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..157
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 752 AA; 83477 MW; BC49F94DC506BCB3 CRC64;
MSPTNNGRNK KLGPRRKVPG RVSKSKSRAK VQAGDAKRVL DANALKWEKV DVPDTLGDFG
GFYGLEEIDG VDVEVVDGKV QFVARDESRL KSPADAVDGT DMVEVDEDAG MEDVTEFRNL
DDVAEGELSA LSDEGSASED DGSDSSGSSD MDEDDDQELQ SEIFNKDIGL DEAEAPELPS
WTNTMKLSAT VLQGLSRLGF SNPTEIQLQS IPKALDGHDI MGKASTGSGK TLAYGIPILE
GIIRDDTDSR PIGLIFTPTR ELAHQVTDHL REVGALLVKR NPYSIMCLTG GLSIQKQERL
LKYKGSARVV VATPGRFLEL LEKDQTLIDR FAKVDTLVLD EADRLLQDGH FEEFERILKH
LSRARKFTNG KKHGWKTMIY SATFSLDYFN KLSNTSWKKM KKAPSENEME EVLKHLMTKI
PFRGKPLIID TNPEQKVASQ IKESLIECLP TERDLYVYYF VTLYPGTTLV FCNAIDSVKK
LNAYLHNLKI SAFQIHSSML QKNRLKSLEK FQEQAKKNQA LNKPTVLIAS DVAARGLDIP
GIQHVIHYHL PRSADVYIHR SGRTARAENE GVAVTICSPQ EAMGPLRKLR RVLAGKAGSK
GKRWQNEIAL LPVEPDIVSQ LRERSRLASA LADSEIATSS LSKDDNWLKK AADDLGIDVD
SDDETKDTFL AKNKTKKLNK QLDKSTSKSY KMELNALLNT PIRKDARKSY LTGGLSNLAD
DLTKKKGHSS IIGHDKVDAL TLLKSKSKRA KR
