DBP10_CHAGB
ID DBP10_CHAGB Reviewed; 762 AA.
AC Q2H0R2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ATP-dependent RNA helicase DBP10;
DE EC=3.6.4.13;
GN Name=DBP10; ORFNames=CHGG_04634;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408032; EAQ88015.1; -; Genomic_DNA.
DR RefSeq; XP_001223848.1; XM_001223847.1.
DR AlphaFoldDB; Q2H0R2; -.
DR SMR; Q2H0R2; -.
DR STRING; 38033.XP_001223848.1; -.
DR EnsemblFungi; EAQ88015; EAQ88015; CHGG_04634.
DR GeneID; 4392546; -.
DR eggNOG; KOG0337; Eukaryota.
DR HOGENOM; CLU_003041_5_0_1; -.
DR InParanoid; Q2H0R2; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000001056; 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; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10.
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 PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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..762
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000256044"
FT DOMAIN 117..289
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 334..511
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..114
FT /note="Q motif"
FT MOTIF 237..240
FT /note="DEAD box"
FT COMPBIAS 338..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 762 AA; 84422 MW; 0928C8A2D6341258 CRC64;
MKRRAASPAM SENEVDIAGS LFANHADSDD EVQVHKQQPA DLDFGDLLDN GDGSDDGGDA
AFIAKQQRSS NRKTGSLQSK SAKKSGGFQA MGLNSNLLRA ISRKGFSVPT PIQRKTIPLV
LERRDVVGMA RTGSGKTAAF VIPMIERLKA HSARVGARAI IMSPSRELAL QTLKVVKELG
KGTDLKTVLL VGGDSLEEQF GLMAANPDII IATPGRFLHL KVEMSLNLSS VRYVVFDEAD
RLFEMGFAAQ LTEILHALPP SRQTLLFSAT LPSSLVEFAR AGLQEPSLIR LDAETKVSPD
LESAFFSVKG GEKEGALLHI LHDVIKMPLG VPEGIEEETD EQQARKRKRD SERRNRKEKP
TEHSTIIFTA TKHHVEYIAH LLRHAGFSVS YIYGSLDQTA RKIQVDNFRR GRTNILVVTD
VAARGIDIPV LANVINYDFP PQPKIFVHRV GRTARAGQRG WAYALLQGTS RPCGGRVRRM
RTQRWRMQTR MNQPLRKTKW TSSPEKTNPP GDDEEAWEDE ESESELEVTV TSSGKSYQGA
NILPRPRNLH VLHTIAPPAP AEERGVRAFN SGGTTQFVEA ARDAAMDLAN DDGAKAFGLP
TRSKLRWDKR HSKYVARAND DDGSRGAKMI RGESGVKIAA SFQSGRFDKW RRANRLGRLP
GVGEAEKANL VRNFSGGGPG GAGAGHYKHR QEKAPKDADK FRDDYHVRKK RVAEAREKRI
GKYKDGEGSR RELKSATDIR KARQVQEQKR EKNARPAKRA KR
