DBP7_CRYNJ
ID DBP7_CRYNJ Reviewed; 948 AA.
AC P0CQ94; Q55KZ7; Q5KAI2;
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 DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; OrderedLocusNames=CNJ01590;
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. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; AE017350; AAW45820.1; -; Genomic_DNA.
DR RefSeq; XP_567337.1; XM_567337.1.
DR AlphaFoldDB; P0CQ94; -.
DR SMR; P0CQ94; -.
DR STRING; 5207.AAW45820; -.
DR PaxDb; P0CQ94; -.
DR PRIDE; P0CQ94; -.
DR EnsemblFungi; AAW45820; AAW45820; CNJ01590.
DR GeneID; 3254316; -.
DR KEGG; cne:CNJ01590; -.
DR VEuPathDB; FungiDB:CNJ01590; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; P0CQ94; -.
DR OMA; QMGFERW; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002149; Chromosome 10.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0042254; P:ribosome biogenesis; IBA:GO_Central.
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; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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..948
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000256026"
FT DOMAIN 250..476
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 597..757
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 43..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..229
FT /note="Q motif"
FT MOTIF 397..400
FT /note="DEAD box"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..607
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 948 AA; 102839 MW; A293CD6322EC7B6A CRC64;
MADDIELNFA VPASGLVRQV APKKGGRWTD RVRAKREARD AFKSMKANHL TVQNPSMPTV
SASELVPKPA VIKPAPTSAS VSRHPQPKSQ VVAPPRFTNA TAGPSRPAPS PQAASSNVPK
SASIPAPATI KHRTSLPTNA FERPPLPPQA GPSRPHPAEK LKTPQFISSL FTSAPLPGVK
SSVAPEISTG APSNAPVDTT TFQGLGLNKL LINHLKGKMG VEKPTGIQRN CLPYMLSSPL
NPDKKAGDEG PKEEPLRDVL IQAQTGSGKT LSYLLPIVQT LLPLSRLSYI DRSIGTLAII
LAPTRELAQQ ISKVLEQLLH MSFAASKEGS DDEDEDDRPF TRWLVSGLLT GGSTRTHEKA
KLRKGVPILV STPGRLLDHL QNTMSFQCAK TMFLVLDEAD RLMDLGFEET IQGIIKALEG
RRRNEINIEK EMDKEGGGTM RWPFWDRGRL NVLCSATVDA KVERLAGAAL RDPVLFRSEK
DEAEAKKKAE GKDDAVIKAL NEAQAIVIPQ ESEEKFTPPS QLSQKYVVLP TKLRLVALVA
LLRSLISSVA KGISVSNGTK VIVFLSSTDA VDFHWKLLGG VQMGQQGQQA DGEKEEDEEE
EGESVEERES DGESKAKKSK RKAKSKSTDD IVSLASPLFP NTTLHRLHGS LPLRTRLASL
KAFATSSSQP SVLFATSVAS RGLDLPLVRA VVQYDLPTEG GANEYVHRVG RTARAGKGGE
AWAFVSPSEE GWVKWIEGKM GAAEGKSGVN LGQVGVEDVL RKGFGGKSYE YEARATDVQL
SFENWVLASE QNAALARKAF ASFVRAYSTH PLEEKQFFHT KLLHLGHLAK SFALREAPAQ
LASALSAGKS KRPKSKAASS ATHPGKRKRD EDEDEMEERG GKELTARNET ERRMYEAVRK
QGRTIKSGGK LGEFSGKGQN KGQKAAATGG EFHIVNTGEL ERLVARRK
