DBP6_KLULA
ID DBP6_KLULA Reviewed; 630 AA.
AC Q6CKZ4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ATP-dependent RNA helicase DBP6;
DE EC=3.6.4.13;
GN Name=DBP6; OrderedLocusNames=KLLA0F06941g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- SUBUNIT: Associated with pre-ribosomal particles. {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. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382126; CAG98103.1; -; Genomic_DNA.
DR RefSeq; XP_455395.1; XM_455395.1.
DR AlphaFoldDB; Q6CKZ4; -.
DR SMR; Q6CKZ4; -.
DR STRING; 28985.XP_455395.1; -.
DR EnsemblFungi; CAG98103; CAG98103; KLLA0_F06941g.
DR GeneID; 2895685; -.
DR KEGG; kla:KLLA0_F06941g; -.
DR eggNOG; KOG0350; Eukaryota.
DR HOGENOM; CLU_003041_15_2_1; -.
DR InParanoid; Q6CKZ4; -.
DR OMA; HLEWLVI; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); 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 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.
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..630
FT /note="ATP-dependent RNA helicase DBP6"
FT /id="PRO_0000232295"
FT DOMAIN 222..402
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 434..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..206
FT /note="Q motif"
FT MOTIF 342..345
FT /note="DEAD box"
FT COMPBIAS 40..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 630 AA; 70582 MW; 10F676D0AB7AE09C CRC64;
MFAARFDPTK VTENVLTAEV TQIKEPTVPQ KRKRDAETDD EGSGEDDASS SEDDASSSED
DSDTISEQDE NKVASVAPTE TSQQSVDAKH SSVLNRFQQT LSLQGALSAS DKVSSDNDVH
DEDVSMKDVH SLTPIPQPAK VTNEALKLLD PSTYKSTAWD AATKIHYDSK MVKQFDSYEG
ELDARLLKNI TSNFSSETFP IQTILFDKVL PLLNSSFKAN RKLFTRRVGD ILVNASTGSG
KTLAYSVPLV QILRSRTVNK VRAIILVPTK ILIHQVYDCL SKLSQGTSLN VSMSKLENSL
KEEHNKFLYN SPDILIITPG RLVDHLQMES FDLKTLKFLV LDEADRLLNQ SFQNWNQVLF
HHLTNDKQDK RPGNVIKMVF SATLTTNAEK LYNLYLHNPK IFLTDSVKLY SIPKKLQELN
VNIPTAKSLF KPLLLLRIIH DIKSSASRNA KILVFVKSNE ASIRLESLLH AMLGSGIIED
EYNMFLSSIH SNISKGSSRK LIQEFASSEQ KKSVLISTDI MARGIDINEI THVINYDLPI
SSQQYVHRCG RTARANTEGI AINLLVGKGE QKFWSQHIDT DLSRDIDGYQ PSAYLDEEKL
SELFSIEDTL KDTYKGCIKQ LQTSKEADSK
