ID   DBP5_CRYNJ              Reviewed;         546 AA.
AC   P0CQ86; Q55NB1; Q5KBP4; Q5KBP5;
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 DBP5;
DE            EC=3.6.4.13;
GN   Name=DBP5; OrderedLocusNames=CNI01880;
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-dependent RNA helicase associated with the nuclear pore
CC       complex and essential for mRNA export from the nucleus. May participate
CC       in a terminal step of mRNA export through the removal of proteins that
CC       accompany mRNA through the nucleopore complex. May also be involved in
CC       early transcription (By similarity). {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 the nuclear pore complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore
CC       complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore
CC       complex cytoplasmic fibrils. {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. DDX19/DBP5
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW45355.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AE017349; AAW45356.1; -; Genomic_DNA.
DR   EMBL; AE017349; AAW45355.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_572662.1; XM_572662.1.
DR   RefSeq; XP_572663.1; XM_572663.1.
DR   AlphaFoldDB; P0CQ86; -.
DR   SMR; P0CQ86; -.
DR   STRING; 5207.AAW45355; -.
DR   PaxDb; P0CQ86; -.
DR   GeneID; 3259615; -.
DR   KEGG; cne:CNI01880; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; P0CQ86; -.
DR   OrthoDB; 608788at2759; -.
DR   Proteomes; UP000002149; Chromosome 9.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; 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; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; 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; Membrane; mRNA transport;
KW   Nuclear pore complex; Nucleotide-binding; Nucleus; Protein transport;
KW   Reference proteome; RNA-binding; Translocation; Transport.
FT   CHAIN           1..546
FT                   /note="ATP-dependent RNA helicase DBP5"
FT                   /id="PRO_0000232221"
FT   DOMAIN          181..350
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          361..531
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           148..176
FT                   /note="Q motif"
FT   MOTIF           297..300
FT                   /note="DEAD box"
FT   BINDING         194..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   546 AA;  59443 MW;  A1339D5ECBFD5FB1 CRC64;
     MSDAQAPPAS TSWADMVDED EKQKQEQNMS NQNDGWGETA TETSAPAPPP ASAPVSSSNN
     DGWGEPAPSA PADNGWADAG ASNGGSGANN NDGWFDAPVP PSSQPPKKEA SDIQLQDDTE
     GLITNTFQVE VKLADLQGDP NSPLYSVQSF KELNLHEDLM KGIIAAGFQK PSKIQEKALP
     LLLSNPPRNL IGQSQSGTGK TAAFTLNMLS RVDPTIPTPQ AICIAPSREL ARQIQEVIDQ
     IGQFTQVGTF LAIPGSWSRN SRIDKQILIG TPGTLVDMLM RGSRILDPRM IRVLVLDEAD
     ELIAQQGLGE QTFRIKQLLP PNVQNVLFSA TFNDDVQEFA DRFAPEANKI FLRKEDITVD
     AIRQLYLECD SEDQKYEALS ALYDCLVIGQ SIVFCKRKVT ADHIAERLIS EGHAVASLHG
     DKLSQERDAI LDGFRNGETK VLITTNVIAR GIDIPAVNMV VNYDVPDLGP GGNGPDIETY
     IHRIGRTGRF GRKGCSVIFT HDYRSKSDVE RIMNTLGKPM KKIDARSTTD IEQLEKALKL
     AMKGPA