DBP2_PICGU
ID DBP2_PICGU Reviewed; 554 AA.
AC A5DL80;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=ATP-dependent RNA helicase DBP2;
DE EC=3.6.4.13;
GN Name=DBP2; ORFNames=PGUG_04031;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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=EDK39933.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH408159; EDK39933.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001483302.1; XM_001483252.1.
DR AlphaFoldDB; A5DL80; -.
DR SMR; A5DL80; -.
DR STRING; 4929.XP_001483302.1; -.
DR EnsemblFungi; EDK39933; EDK39933; PGUG_04031.
DR GeneID; 5125550; -.
DR KEGG; pgu:PGUG_04031; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_16_9_1; -.
DR InParanoid; A5DL80; -.
DR OrthoDB; 638613at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..554
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000294616"
FT DOMAIN 156..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 346..506
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 521..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 125..153
FT /note="Q motif"
FT MOTIF 279..282
FT /note="DEAD box"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 554 AA; 60956 MW; 95178905F6F350E7 CRC64;
MSYNQNYNQD FNNNSYGSYG NSYNNNSYGQ NNYGGSYGGN SYGGGRGGSR GGFRGGRGGG
FGGRRVDERV ELTTPEWDLD SLPKFEKNFY SEHPDVSARS ESEVQSFRKE HDMKCVGTDI
PKPITSFDEA GFPDYVLNEV KQQGFPKPTA IQCQGWPMAL SGRDMIGIAA TGSGKTLSYC
LPSIVHINAQ PLLGPGDGPI VLVLAPTREL AVQIQQECSK FGASSRIRNT CIYGGAPKGQ
QIRDLARGVE ICIATPGRLI DMLETGKTNL RRVTYLVLDE ADRMLDMGFE PQIRKIVDQI
RPDRQTLMWS ATWPKEVQTL TRDYLNDPIQ VTIGSLELAA SHTITQIVEV LSEFEKRDRL
VKHLETATAD KEAKVLIFSS TKRACDEITS YLRADGWPAL AIHGDKQQNE RDWVLREFKT
GKSPIMVATD VAARGIDVKG ISYVINYDMP GNIEDYVHRI GRTGRAGTTG TAVSLFTEAN
SKLGGDLCKI MREANQTVPP ELLRYDRRSF GSHIRYGRGG GRGGWGGRGR GGRGRGRGGF
QSGSNGAPMG NRRF
