MAK5_CRYNJ
ID MAK5_CRYNJ Reviewed; 772 AA.
AC P0CQ90; Q55JG1; Q5KC99;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; OrderedLocusNames=CNH00280;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017348; AAW44914.1; -; Genomic_DNA.
DR RefSeq; XP_572221.1; XM_572221.1.
DR AlphaFoldDB; P0CQ90; -.
DR SMR; P0CQ90; -.
DR STRING; 5207.AAW44914; -.
DR PaxDb; P0CQ90; -.
DR EnsemblFungi; AAW44914; AAW44914; CNH00280.
DR GeneID; 3259037; -.
DR KEGG; cne:CNH00280; -.
DR VEuPathDB; FungiDB:CNH00280; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; P0CQ90; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002149; Chromosome 8.
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 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..772
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000232233"
FT DOMAIN 203..424
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 473..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..200
FT /note="Q motif"
FT MOTIF 344..347
FT /note="DEAD box"
FT COMPBIAS 84..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 772 AA; 85544 MW; 3D65397C0A897D06 CRC64;
MAKIDKKTKL KLNKKSVRAP SKPTTEKKPK KYVTADTLTW KPVKTSSFSG IDGGGGMMML
EELEDVGIEW EETDGGRKIA KFVEVESKTS KGKKNAAQEE PNQEGRGDDE KASSASETEE
GKKADDKEAV EEDDEEEFPD FAGFAEEDLN AADEEEHPNL DDEPAFNDDL LPEWSSISLH
PSLKRSFLAS SFTAPTAIQS RAIPAGITGR DVVGVAETGS GKTLAYSLPI LHYLLGQRKS
KAGIKRPLSA LVLCPTRELA LQVMDHLNAL LKHALATPDG EKPQGPPRVS VGSVVGGLSA
QKQKRILERG CDVIVATPGR LWDLIKADDE LATSVRTLRF LVIDEADRMI ENGHFAELES
IVKLTQRSTA QQGPDDDDPV FQAMATLFEE STAREDMQTF VFSATLSKDL QKNLKRRSRS
WKGKGKRSST LEDLVEKLDF RDENPEVIDL SPEGGVVSSL RESMIESTKD DKDLYLYYFL
LRYPGRSIVF VNSIDSIRRL LPLFTLLQLP VFPLHSHLQQ KQRLKNLDRF KSNPKGILIA
TDVAARGLDI PQVDHVVHFN LPRTADAYIH RSGRTARAQN EGFALQLVSP DEKSVQRALM
KSLERTHELP DLPIEAGFLP SLRERLRVAT EIEKAQHRAT KATHDKNWLL EAAEAMDIDI
DPSMLDGEDD DPDAPYYKPK KQDRGKGKAS VENLKMELKA LLQEKLVARG VSIRYPTSGS
KVIVDDLIKS TGHGMLLGAS TSKAYDQVEK TGKRKLGSGR PGAVKKKKVE GR
