MAK5_ASPTN
ID MAK5_ASPTN Reviewed; 774 AA.
AC Q0CI35;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=ATP-dependent RNA helicase mak5;
DE EC=3.6.4.13;
GN Name=mak5; ORFNames=ATEG_06649;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU33193.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476602; EAU33193.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215827.1; XM_001215827.1.
DR AlphaFoldDB; Q0CI35; -.
DR SMR; Q0CI35; -.
DR STRING; 341663.Q0CI35; -.
DR GeneID; 4322181; -.
DR eggNOG; KOG0347; Eukaryota.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000007963; 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..774
FT /note="ATP-dependent RNA helicase mak5"
FT /id="PRO_0000282486"
FT DOMAIN 233..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 493..643
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..230
FT /note="Q motif"
FT MOTIF 368..371
FT /note="DEAD box"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 774 AA; 85744 MW; 443838E3FDD8BC19 CRC64;
MGQKRQRDQK GSGFQSKKRK RGANSSNADD KDDGWDGIVG VEDLNWKEVA LPDRLDDAEG
FFGLEEIEGV DIVRPEGSGE IRFKAKAGKP KKSILKNKTI PQEDKTFDDE WEGFSDGEAA
QETTTTEPTE EPVQTTNEET EVKEKKEPKK KEAKKEVKKD AKNAKKEPKK KDLPSQKDKD
IKPGLSFAAL QDAEEDDGVD ISAWESLGLS PEILNSLSKL KFSSPTAVQK SCIPPILDGH
DVVGKASTGS GKTLAFGIPI LEYYLEKKRR ETKNKDDKKE TSPIALILSP TRELAHQLVK
HIGEVITHAP GVNARIALLT GGLSVQKQQR LLNGADIVIG TPGRVWEVLS GGQGLISKMK
EIKYLVVDEA DRLLSEGHFK EAHEILAALD REEINDFPGA EEDESDDEDS KTQRQTLVFS
ATFHRDLQQK LAGKGKWTGS DLMNKQESME YLLKKLNFRE EKPKFIDVNP VSQMAEGLKE
GIVECAAMEK DLYLYTLLLY HPKHRTLVFT NSISAVRRLT QFLQALQLPA LALHSSMAQK
ARLRSVERFS SPTADPSTIL VATDVAARGL DIKGIDFVIH YHAPRTADTY VHRSGRTARA
GASGKSVIIC APEEMVGVVR LAAKVHANMA NGKRLPLESL ELDRRIVSRV KQRVTLAARI
CDANIAKEKV SAEDNWLKNA AEELGVDYDS EEFDERQGRG RGRGRGRQQR ERQASSISKA
ELAGMRAELK QLLSQRVNVG VSERYLTSGR VDIEALLRGE GNASFLGQVD PLGF
