(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 101.
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}.
DR   EMBL; AE016818; AAS52711.1; -; Genomic_DNA.
DR   RefSeq; NP_984887.1; NM_210241.1.
DR   SMR; Q757I6; -.
DR   STRING; 33169.AAS52711; -.
DR   PRIDE; Q757I6; -.
DR   EnsemblFungi; AAS52711; AAS52711; AGOS_AER027W.
DR   GeneID; 4621089; -.
DR   KEGG; ago:AGOS_AER027W; -.
DR   HOGENOM; HOG000290702; -.
DR   InParanoid; Q757I6; -.
DR   KO; K14805; -.
DR   OMA; TMILASE; -.
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:0003723; F:RNA binding; IBA:GO_Central.
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   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;
DR   PRODOM; Q757I6.
DR   SWISS-2DPAGE; Q757I6.
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   NP_BIND         224..231
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           180..208
FT                   /note="Q motif"
FT   MOTIF           340..343
FT                   /note="DEAD box"
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
//

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