DBP4_PICGU
ID DBP4_PICGU Reviewed; 754 AA.
AC A5DLF4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase DBP4;
DE EC=3.6.4.13;
GN Name=DBP4; ORFNames=PGUG_04105;
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 required for ribosome biogenesis.
CC Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC Required for pre-rRNA cleavage at site A2 (By similarity).
CC {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: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC ribosomal complexes (By similarity). {ECO:0000250}.
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. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408159; EDK40007.2; -; Genomic_DNA.
DR RefSeq; XP_001483376.1; XM_001483326.1.
DR AlphaFoldDB; A5DLF4; -.
DR SMR; A5DLF4; -.
DR STRING; 4929.XP_001483376.1; -.
DR PRIDE; A5DLF4; -.
DR EnsemblFungi; EDK40007; EDK40007; PGUG_04105.
DR GeneID; 5125326; -.
DR KEGG; pgu:PGUG_04105; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; A5DLF4; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; 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: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 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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..754
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000294624"
FT DOMAIN 77..251
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 265..429
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..74
FT /note="Q motif"
FT MOTIF 199..202
FT /note="DEAD box"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 754 AA; 85220 MW; 262E1918140B025F CRC64;
MAKPKKGAKV NNPNRKSRNQ KVLQTIADLQ KRIDEYDPAT DEQSISQFKH LPISEGTYKG
LLENNFVSLT DIQKKAIPVA LKSEDVMGTA RTGSGKTLAF LVPVIEKLIR ENITEYDGLA
ALIVSPTREL AVQTFEVLTK IGKYNSFSAG LVTGGKDVKY EKERISRMNI LIGTPGRISQ
HLNEAVGMET SNLQVLVLDE ADRCLDMGFR KQIDNILGHL PVTRQTLLFS ATQSDNVKDL
ARLSLVNPKR VGVSSDQEVS SIPESLEQYY IKISLASKMD VLWSFLKSHL KSKILVFFSS
SKQVQFAYEA FRRLQPGISL LKLYGRHKQT SRLETTMKFS RAQHACLFAT DIVARGLDFP
AIDWVVQVDC PEDAATYVHR VGRAARFGRQ GKSLLMLAPS EEEGMVKRLE AHKISLKMMN
IKQKNKKVIS PQLQSLCFQD PELKNLGQRA FISYMKSVHI QKDKDIFKVE ELPAAEYAKA
LGLPGTPNIN IKNGAGNKDK KNMSRELLAL QKPEKQKSDS EKVRTKYDRM FERQNQTVLS
KNYLNMAAGD DSGSEDDFMS VKRKDHIIKD EELPDLSVPV SKRQSKKALS KKASLKSKGN
PTKLIFDDEG VTHHLYEFED EEDFKSRGDA KLQKAEFVSK ENEAMSKADV DDKATAREKR
QEKKRRWKEQ ERLAREQDEF SGSEDEAHTV TLAGADIDRD MDYGRSSEDE QPPSKKPKWF
EQEKPKKKKV DIVEVEEPET LEDLEALTAK LIGS
