DBP2_CRYNB
ID DBP2_CRYNB Reviewed; 540 AA.
AC P0CQ77; Q55QJ0; Q55QJ1; Q5KFM5; Q5KFM6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=ATP-dependent RNA helicase DBP2-A;
DE EC=3.6.4.13;
GN Name=DBP2; OrderedLocusNames=CNBF3470;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {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 -!- SUBUNIT: Associates with polysomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL20020.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAL20021.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAEY01000032; EAL20020.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAEY01000032; EAL20021.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_774667.1; XM_769574.1.
DR RefSeq; XP_774668.1; XM_769575.1.
DR AlphaFoldDB; P0CQ77; -.
DR SMR; P0CQ77; -.
DR EnsemblFungi; AAW43961; AAW43961; CNF01240.
DR EnsemblFungi; EAL20020; EAL20020; CNBF3470.
DR EnsemblFungi; EAL20021; EAL20021; CNBF3470.
DR GeneID; 4936899; -.
DR KEGG; cnb:CNBF3470; -.
DR HOGENOM; CLU_003041_16_9_1; -.
DR Proteomes; UP000001435; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
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; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..540
FT /note="ATP-dependent RNA helicase DBP2-A"
FT /id="PRO_0000410249"
FT DOMAIN 141..316
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 344..490
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 492..519
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT REGION 494..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..138
FT /note="Q motif"
FT MOTIF 264..267
FT /note="DEAD box"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 540 AA; 57952 MW; 5157056F758E2A9F CRC64;
MSYGGGYGGG GYGGGYGGGG GGGGYGGGGG GYGGGYGGGG YGGGFGGDRM GNLGQGLHNI
DWQNQSLAKF EKNFYVQDPR VTARSDAEVE AFRAEKEMKI QGKNVPRPIT TFEEAGFPDY
IMSEIRRMGF TAPSSIQCQA WPMALSGRDL VAIAETGSGK TISFCLPAMV HINAQPLLAP
GDGPIVLILA PTRELAVQIQ TEATKFGQSS RIRNTAIYGG APKGPQIRDL QRGVEICVAT
PGRLIDMLET GKTNLKRVTY LVMDEADRML DMGFEPQIRK IVSQIRPDRQ TLLFSATWPK
EVQRLAMDFL HDFIQVNIGS LDLTANHNVA QHVEVCTDFD KRSKLLSHLE KISQENGKVL
IFVATKRVAD DLTKFLRMDG WPALAIHGDK QQAERDWVLA EFKSGRSPIM LATDVASRGL
DVRDIGYVIN YDFPNNCEDY IHRIGRTGRA GRKGTSYTYF TMDNSKAARE LVQILRESKA
DIPPELEEMA MYGGRGGGGG RGRGGRGGGR GGYGGGGGRG GYSSGANSYG GGGGGYSSRW
