ID   MAK5_NEUCR              Reviewed;         805 AA.
AC   Q7RZH4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=ATP-dependent RNA helicase mak-5;
DE            EC=3.6.4.13;
GN   Name=mak-5; ORFNames=B10H18.180, NCU04041;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; BX897678; CAE85602.1; -; Genomic_DNA.
DR   EMBL; CM002241; EAA28420.1; -; Genomic_DNA.
DR   RefSeq; XP_957656.1; XM_952563.2.
DR   AlphaFoldDB; Q7RZH4; -.
DR   SMR; Q7RZH4; -.
DR   STRING; 5141.EFNCRP00000003590; -.
DR   PRIDE; Q7RZH4; -.
DR   EnsemblFungi; EAA28420; EAA28420; NCU04041.
DR   GeneID; 3873827; -.
DR   KEGG; ncr:NCU04041; -.
DR   VEuPathDB; FungiDB:NCU04041; -.
DR   HOGENOM; CLU_003041_13_0_1; -.
DR   InParanoid; Q7RZH4; -.
DR   OMA; HYHVPRT; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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: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..805
FT                   /note="ATP-dependent RNA helicase mak-5"
FT                   /id="PRO_0000232238"
FT   DOMAIN          240..463
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          510..666
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          79..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           209..237
FT                   /note="Q motif"
FT   MOTIF           372..375
FT                   /note="DEAD box"
FT   COMPBIAS        122..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..430
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   805 AA;  89254 MW;  4036B27AB744D369 CRC64;
     MAVDKKRKNT KAPASGPKRR KTQPSSKQIK RPVSVDALAW KTVDIPEMFD DAEGFFGLEE
     ITGVDIVKDG DVVKFMAAVP KSEAEVEDDG EEFGGFDDEE TPKPAGNADQ EVKTSETKAE
     AASTPAKEKK ASKDQRKPKE QQKQQKQQKQ QPKKEQPNKA ANKKNAEDKK KARKNEKTTV
     EPKDPELETD LFTKLEELPE PEEEEIDMSE WVPLDLSPRM ISSIAKLRFS KPTVIQSKAI
     PEIMAGHDVI GKASTGSGKT LAFGIPVIES WLSAAETRKQ NKEERKGATA LILSPTRELA
     QQIRDHLQAL CKGLPTAPYI CSVLGGMAVQ KQKRQLQVAD IVIATPGRMW EVMSSDNSVL
     ASLRNISFLV LDEADRLLKD GHFKEAEEIF KALDRPPVEE NNEDQKMGGT DEEGQEEEEE
     DSEEEEEEEE EHVNKRQTLI FSATFNKNLQ QKLAGKSKFK ATSTQDMEYL LQKLNFRETP
     KFVDANPVHQ MAENLKEGLI MCGDMEKDLY LYATLMLQPT RRALVFTNSV NSVRRLTPLL
     ENLNLPAFPL HSGMIQQARL RSIDRFKANE GAKKKNGSAA ILVATDVAAR GLDIPDVDLV
     IHYHVPRAAE DYVHRSGRTA RASNSGTSIL LCGPKEAVPT QRLVAKVHAQ AEVKAGNSGN
     NTKKLVSSGL RTIDIDRRIV AKLRERVDLA KKIADAVQAK TMGGKEDDWM KKAAEDLGVD
     YDSEELEKAG KWGGKGSSKK QKQKEAQQMS KGELASLRAA LRDLLSKRIN TGVSERYLTG
     LDVSELLKGE QGLFLGQVDG LGLDD