DBP9_CRYNJ
ID DBP9_CRYNJ Reviewed; 627 AA.
AC P0CR10; Q55I26; Q5K7L2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=ATP-dependent RNA helicase DBP9;
DE EC=3.6.4.13;
GN Name=DBP9; OrderedLocusNames=CNM02050;
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. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; AE017353; AAW46985.1; -; Genomic_DNA.
DR RefSeq; XP_568502.1; XM_568502.1.
DR AlphaFoldDB; P0CR10; -.
DR SMR; P0CR10; -.
DR STRING; 5207.AAW46985; -.
DR PaxDb; P0CR10; -.
DR EnsemblFungi; AAW46985; AAW46985; CNM02050.
DR GeneID; 3255082; -.
DR KEGG; cne:CNM02050; -.
DR VEuPathDB; FungiDB:CNM02050; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; P0CR10; -.
DR OMA; GYEKDFK; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002149; Chromosome 13.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 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..627
FT /note="ATP-dependent RNA helicase DBP9"
FT /id="PRO_0000232339"
FT DOMAIN 52..238
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 249..487
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 337..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Q motif"
FT MOTIF 181..184
FT /note="DEAD box"
FT COMPBIAS 337..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 627 AA; 68915 MW; 576E9E4ADA4BB300 CRC64;
MLSKSNQPSD ALLDADFSFS QPPFSTLIDS RVLVALADQK FAHPTLVQAK AIPLLLEGKD
VLARARTGSG KTAAYIVPAV QKILEAKADL SPASAEYQAT RAIILVPTKE LALQVSSFTK
NVTKYCDGLV QCVDVAAGGA SIQRVLLNDK PDIVISTPTK LLSLLQSKSL SLSQLSFLAI
DEADLLLSYG FKDDLTRIMD PTSGWIPKLG VQGCLMSATL SDDVEGIKGL VLRNPAILTL
SEPASASSLL SQHYTHTSER DKFLLIYVLL KLKLIRGKSI IFVNDVERGY RVKLFLEQFG
VKCCVVNSEL PLASRYHVVE EFNRGVYDVV VATDEGAGAD AEEEEDVKQE ESESEGEEDE
DDDKEAEDKE KEAKEEAKPA PGPSKRRATS PPSKPNKRAR RADPTSSLAR GIDFTSASSV
INFDLPLTST SYMHRVGRTA RAGQSGLALS FVVPRENWGK DKAVSIKSAE KDEKVFERIK
ERVKKESDSE IKEWDWKGRK GEIEGFRYRM EDALKAVTGK RVAEARREEV RRELLNSEKL
KSHFAANPLD LSYLRHDAPL HPARQQTHLK HVPNYLMPKI AALPTGGDVT DHAGVGFSRR
GRGGHRGRGG RGSKSGRGKK VDPLKFK
