MAK5_SCLS1
ID MAK5_SCLS1 Reviewed; 780 AA.
AC A7EAY2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=ATP-dependent RNA helicase mak5;
DE EC=3.6.4.13;
GN Name=mak5; ORFNames=SS1G_02468;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476623; EDN99610.1; -; Genomic_DNA.
DR RefSeq; XP_001596248.1; XM_001596198.1.
DR AlphaFoldDB; A7EAY2; -.
DR SMR; A7EAY2; -.
DR STRING; 665079.A7EAY2; -.
DR EnsemblFungi; EDN99610; EDN99610; SS1G_02468.
DR GeneID; 5492605; -.
DR KEGG; ssl:SS1G_02468; -.
DR VEuPathDB; FungiDB:sscle_04g034850; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; A7EAY2; -.
DR OMA; HYHVPRT; -.
DR Proteomes; UP000001312; 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..780
FT /note="ATP-dependent RNA helicase mak5"
FT /id="PRO_0000310210"
FT DOMAIN 244..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 477..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 213..241
FT /note="Q motif"
FT MOTIF 378..381
FT /note="DEAD box"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 780 AA; 86191 MW; 2F7B58DBB92290B1 CRC64;
MDTKQKKRSH SETNGSQKAP KRQKIQKTSK KQKKAAPKKP VAVDSLPWNE VTMPDMFEDA
EGFYGLEEVD DVEVVRDGDV VTFVSSKIQT KNNEDEEFEG FGDEVEDGGN AATDNTGEVK
PILKPTEEST KNDVPQGNKQ KIEKKAKPEK KDKKEGSNTE EGEEKVPSKK EKKQKQEKPQ
KQPVDKDATL KQDPLKNVFE ALDEDAAGEV EVSGWVELDL SSNTLMALSK MGFSKPTPIQ
SEAIPEVLAG HDVVGKASTG SGKTLAFGIP IVEKWLEVYG ELDEDELKKS TRPPTALILS
PTRELAHQLT EHITTLCKGM PTSPYVAAVT GGLSVQKQQR QLSKADIIIG TPGRLWEVIS
SSNELSAGLK QVRFLVIDEA DRLLTDGHFK EAEEILNALD RTHGNEDDDE EDTLPPRQTL
VFSATFHKGL QQKLAGKGKQ SFKDDSQSME YLLKKLNFRE EKPKFVDVNP ISQMAANLKE
GMVECGGEEK DLYLYSLLLH HPNQRTLIFT NSIHSVRRLT PMLQTLNIPA HSLHSQMIQK
ARMRSIEKFS RTNNTGSVLV ATDVAARGLD IGGVQLVIHY HLPRTADMYV HRSGRTARAA
ASGSSILLCG PEEVVGTRRL VAKVHAQNAL HGEGKKSKFY IRSLDIDRRV VSRLKPRVTL
AKKIADSALA KEKKGHDDDW VKNAAEELGV EYDSEEFEAL GGGRKGRGTG RRMKEKEARG
MSKGEVGALR AELRALLAQR VNVGVSERYL TSGTVNVNDL LKGAKGEWLG EVEGIGMEDD
