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DBP7_CANAL
ID   DBP7_CANAL              Reviewed;         727 AA.
AC   Q59S50; A0A1D8PQS9; Q3MPL8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP-dependent RNA helicase DBP7;
DE            EC=3.6.4.13;
GN   Name=DBP7; OrderedLocusNames=CAALFM_C701200CA;
GN   ORFNames=CaJ7.0136, CaO19.6902;
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=15937140; DOI=10.1534/genetics.104.034652;
RA   Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA   Mikami Y.;
RT   "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT   syntenic analysis against the Saccharomyces cerevisiae genome.";
RL   Genetics 170:1525-1537(2005).
RN   [2]
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   [3]
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   [4]
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-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits and is required for the normal formation of 25S and
CC       5.8S rRNAs. {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   -!- 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   -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP006852; BAE44642.1; -; Genomic_DNA.
DR   EMBL; CP017629; AOW30490.1; -; Genomic_DNA.
DR   RefSeq; XP_712474.1; XM_707381.1.
DR   AlphaFoldDB; Q59S50; -.
DR   SMR; Q59S50; -.
DR   BioGRID; 1228996; 1.
DR   STRING; 237561.Q59S50; -.
DR   PRIDE; Q59S50; -.
DR   GeneID; 3645903; -.
DR   KEGG; cal:CAALFM_C701200CA; -.
DR   CGD; CAL0000199731; DBP7.
DR   VEuPathDB; FungiDB:C7_01200C_A; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   InParanoid; Q59S50; -.
DR   OMA; AVHIKAD; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000559; Chromosome 7.
DR   GO; GO:0005730; C:nucleolus; 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; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
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; 2.
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..727
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000232252"
FT   DOMAIN          168..363
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          406..613
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          14..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           135..164
FT                   /note="Q motif"
FT   MOTIF           295..298
FT                   /note="DEAD box"
FT   COMPBIAS        15..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   727 AA;  81139 MW;  67A8502B9159C495 CRC64;
     MDDDDELLLN FAAPDTSSVA ASKNQNVKVS GGRWKDRRKL QLALQGRTKK RQPETGVNLI
     PVDESKRKRD SEDKVQLDSN KRSKFTESKG ENGGKGDSYV SSLFTNNQPT SHLAPTSTTK
     ELTYLPSNAP MKDATNFSGL GLNEKLSIHL TDHLRFMHPT KIQQLVIPSL ISTENDLFVK
     AQTGSGKTLA FVLPIFHKLM RENKFKINRE SGLFAIILTP TRELATQIYG VLETLTRCHH
     WIVPGIVIGG EKKKSEKARL RKGCNILVAT PGRLADHLEN TKTLDISQLR WLVLDEGDKL
     MELGFEDTIA QITAKIDSNS KIADTAEKWQ GLPSRRINML CSATLHSNVK KLGSIVLKDP
     EMISVETASV AGTVSFDETI ATTTSTAPDQ LIQNVVVVPP KLRLVTLDAL LLKISKHSAE
     RTIVFFSCSD SVDFHFDVFT RDGKKFKKVT DEETGEVKTV LVSPEDDEND GLLTAPQLSD
     NTIIYKLHGS LSQQTRASTL QSFVKDNNSY NKILFCTDVA SRGLDLPNVA NVIEYDPPFT
     IDDHLHRIGR SARLGNEGNA TLFLLPGIEE GYVDGKLRVA HPREGNLRVK NYEKILQEGF
     AQGNIKSKDN KLGKWDIHAT TWHLDVERWL LEDQASHDEA VRAFTSHIRA YATHLSSERE
     FFNVKLLHLG HLAKSFGLRE TPKKLGKSVG NNSNYSESKK GKKEDPRKKM LRMAKMAVKS
     ASSEFNY
 
 
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