DBP5_CANAL
ID DBP5_CANAL Reviewed; 540 AA.
AC Q5AJD0; A0A1D8PJB3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP-dependent RNA helicase DBP5;
DE EC=3.6.4.13;
GN Name=DBP5; OrderedLocusNames=CAALFM_C301860CA;
GN ORFNames=CaO19.1661, CaO19.9230;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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DR EMBL; CP017625; AOW28226.1; -; Genomic_DNA.
DR RefSeq; XP_721738.2; XM_716645.2.
DR AlphaFoldDB; Q5AJD0; -.
DR SMR; Q5AJD0; -.
DR BioGRID; 1219658; 4.
DR STRING; 237561.Q5AJD0; -.
DR PRIDE; Q5AJD0; -.
DR GeneID; 3636564; -.
DR KEGG; cal:CAALFM_C301860CA; -.
DR CGD; CAL0000188126; DBP5.
DR VEuPathDB; FungiDB:C3_01860C_A; -.
DR eggNOG; KOG0332; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q5AJD0; -.
DR OrthoDB; 608788at2759; -.
DR PRO; PR:Q5AJD0; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IEA:EnsemblFungi.
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 GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR GO; GO:0006409; P:tRNA export from nucleus; IEA:EnsemblFungi.
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..540
FT /note="ATP-dependent RNA helicase DBP5"
FT /id="PRO_0000232219"
FT DOMAIN 183..350
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 361..538
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 24..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 150..178
FT /note="Q motif"
FT MOTIF 297..300
FT /note="DEAD box"
FT COMPBIAS 49..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 540 AA; 60206 MW; 1CB36CE3394A520E CRC64;
MSSEKVKRVE ADATDLLASL SIDKSGEKLE EIKKGSTPDP SDLLGGLSLK EGDSKKPEEK
KEVVEEPENK EINDDKKDED KKDESKDEVK DGDGAKEETK EEVKEESKEE PKEPKEPKEP
ATNLIKSSYE VKVKLADIQA DPNSPLYSVK SFEELGLSPE LLKGLYAMKF NKPSKIQEKA
LPLLLSNPPR NMIGQSQSGT GKTAAFSLTM LSRVDPTIKM PQCLCLSPTR ELARQTLEVI
TTMGKFTNIT TQLVVPNAIP RGSSVNAQVL VGTPGIAIDL IRRRQLNLSK MKVFVLDEAD
NMLEAQGLGD QAIRVKKALP RGVQLVLFSA TFPTEVREYA ERLVPDANSL ELKQEELNVD
GIKQLYMDCR SEQHKFEVLC ELYGLLTIGS SIIFVEKKET ADVLYGKMKK EGHTVSVLHG
GLDNTDRDRL IDDFREGRSK VLITTNVLAR GIDIASVSMV VNYDMPTDKY GKPDPSTYLH
RIGRTGRFGR VGVSISFIHD RRSYDILMAI KAYFGNVEMT RVPTDDWDEV EKIVKKVIKS
