MAK5_PHANO
ID MAK5_PHANO Reviewed; 817 AA.
AC Q0U6X2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; ORFNames=SNOG_12492;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445346; EAT80305.1; -; Genomic_DNA.
DR RefSeq; XP_001802714.1; XM_001802662.1.
DR AlphaFoldDB; Q0U6X2; -.
DR SMR; Q0U6X2; -.
DR STRING; 13684.SNOT_12492; -.
DR PRIDE; Q0U6X2; -.
DR EnsemblFungi; SNOT_12492; SNOT_12492; SNOG_12492.
DR GeneID; 5979623; -.
DR KEGG; pno:SNOG_12492; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; Q0U6X2; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..817
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000256021"
FT DOMAIN 280..479
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 531..675
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 249..277
FT /note="Q motif"
FT MOTIF 411..414
FT /note="DEAD box"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 817 AA; 90193 MW; DA0E89D4593B3569 CRC64;
MKRAHKAPKA SHKAHKRQKV EKKPRPEINV PKRKIRLDDL GWNQVSMPDR LEDFEGFYGL
EEIEDVHVVK DAVTGNLSFE TTKTDEQIEQ DIEKAWQREE EEAKFLEKIT FGGEPKNGED
VVEEETAPVE DTVEATQDED AASWGGFSDD DVAQNGDEQS EDVQMVEEDA PPTPNVVLST
TKADGDGEAE PKKMNKRERA AEKKRIAALA KKTKKPDDDE ASEGKTFGPG AFDILANRAD
DEDDEVDVSA WEELELSTKI LESLAKLKFS KPTTIQASTI PEIMAGRDVI GKASTGSGKT
LAFGIPIIES YLASKSKSKD VKDKTPLALI IAPTRELAHQ ITAHLTALCA KGAFEAPLIA
SVTGGLAVQK QRRQLEKADI IVGTPGRLWE VISTGHGLLE KVKQIRFLVV DEADRLLSQG
NYKELGEILK ILEKDAPAEG EAEAEETTEV ERQTLVFSAT FQKGLQQKLA GKAKGGSDNL
MSKQQSMEYL LKKINFREEK PKFIDANPSS QMASKLKEGL IECAGTEKDL YLYSLLMFYP
KKRALIFTNS ISAVRRLTPF LQNLALPALP LHSSMAQKAR LRSIERFKER PGSILVATDV
AARGLDIPKV ELVIHYHLPR AADTYVHRSG RTARAEASGS SILICAPEEV GGVRRLIAKV
HARADEAPKS KKTAYFIRTL DIDRRIVARL KPRASISKKL ADTVIAKEKK HSEDDTLRQA
AEDLGVDYDS EEFEKEAKGK KGRGTGRKKK EKEASEMTKG EQQALRAELR GLLSQRINTG
VSARYLTSGG IDVDALMAGE GNMEFLGNVD GLGFDEE
