MAK5_NEOFI
ID MAK5_NEOFI Reviewed; 777 AA.
AC A1DMT9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent RNA helicase mak5;
DE EC=3.6.4.13;
GN Name=mak5; ORFNames=NFIA_054560;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16110.1; -; Genomic_DNA.
DR RefSeq; XP_001258007.1; XM_001258006.1.
DR AlphaFoldDB; A1DMT9; -.
DR SMR; A1DMT9; -.
DR STRING; 36630.CADNFIAP00004212; -.
DR EnsemblFungi; EAW16110; EAW16110; NFIA_054560.
DR GeneID; 4584522; -.
DR KEGG; nfi:NFIA_054560; -.
DR VEuPathDB; FungiDB:NFIA_054560; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000006702; 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..777
FT /note="ATP-dependent RNA helicase mak5"
FT /id="PRO_0000282487"
FT DOMAIN 232..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 496..646
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 201..229
FT /note="Q motif"
FT MOTIF 370..373
FT /note="DEAD box"
FT COMPBIAS 116..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 777 AA; 84961 MW; 6918FB8D8CFA416C CRC64;
MGQKRQRDSK SSTFHAKKRK KAENATAPDS DDGWDGIVGA DELNWKEVAL PDHLEDAGGF
FGLEEIEGVD IVRGSGNGEV KFKAVAGKPK KSILKKKAPE DENSEYDEEW SGFSDDDADR
PENASSPAVE KPEKSDTKAD KKSEKNADKK EAKDAKKKEA KAAKKEQKEK GSAIQHDTSI
NAGLSFAALQ DTEEDDGADV SAWDSLGLSP EILTGLSKMK FASPTSVQEA CIPQILEGHD
VIGKASTGSG KTLAFGIPIL EHYLEKKRDD ISAEKEKKSE KDSTPIALIL SPTRELAHQL
SKHIGELIAQ APGVNARIAL LTGGLSVQKQ QRLLSGADIV IGTPGRVWEI LSTGQGLIRK
MQQIKFLVVD EADRLLSEGH FKEVEEILNA LDRVEDGEVP GGENQASEEE SDPSSERQTL
VFSATFHRDL QQKLAGKGKW TGGDVMDKKE SMDYLLQKLN FREEKPKFID MNPISQMADN
LKEGIVECGA MEKDLFLYTL LLYHPKHRTL VFTNSISAVR RLTKLLQTLQ LPALALHSSM
AQKARLRSVE RFSSPSSDPS TILVATDVAA RGLDIKGINL VIHYHAPRTA DTYVHRSGRT
ARAGASGKSV IICGPDEMVG VVRLAAKVHA NMANGKKLPL ESLELDRRVV SRVKPRVSLA
SRITDANIAK EKISAEDNWL RNAAEDLGVE YDSEEFDESN GKGRGRGRGR HQKQKEVGSV
SKAELAGLRA ELKQLLSQRV NVGVSERYLT AGRVDIDALL RGEGNASFLG PVDPLHF
