DBP7_CHAGB
ID DBP7_CHAGB Reviewed; 806 AA.
AC Q2GZU7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; ORFNames=CHGG_04949;
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. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408032; EAQ88330.1; -; Genomic_DNA.
DR RefSeq; XP_001224163.1; XM_001224162.1.
DR AlphaFoldDB; Q2GZU7; -.
DR SMR; Q2GZU7; -.
DR STRING; 38033.XP_001224163.1; -.
DR EnsemblFungi; EAQ88330; EAQ88330; CHGG_04949.
DR GeneID; 4392137; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q2GZU7; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
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; 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 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..806
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000256024"
FT DOMAIN 174..380
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 413..611
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 24..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 141..170
FT /note="Q motif"
FT MOTIF 309..312
FT /note="DEAD box"
FT COMPBIAS 24..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 806 AA; 87023 MW; BE971C4BC071D7C0 CRC64;
MADDGMLLNF EIGDAPLKSQ VKFKGGRWRD RLKAQRSAKQ SHEDGPSSTP PRNRTTVGGY
DAGRLGKRPR TEDGESHRYA KVPRTSDAAP KAPSHAMKTG QISSSLFTSN PSAVTDFDQP
PAEEEAEPAK ASNAPLSEEA ENFHSLGVSR RVAQHLATKL EMKAPTAIQK NTVPQLINGD
SDAFLQAETG SGKTLAYLLP IVHRIMSLSL NEDGTPKDTK VHRNSGLFAI IMAPTRELCK
QISVVLEKVL RCAPWLVCTT VIGGESKKSE KARIRKGVNI LIATPGRLAD HLDNTKVLNV
GTVRWLVLDE GDRMMEMGFE DDIKTIVGKI RADKLEKVNA EGVVLDGVLP SRRVTVLCSA
TMKMNVQKLG EISLEDAIHI MAAKSESDGD ADAVFAAPSQ LKQSCIVTPA KLRLVTLIAL
LKSTFARRGS VMKAIIFISC ADSVDFHYQL LKDTKAVEPP TPDSSSTKDR NPHTDTTVAR
AAYITSPANP KVMLHKLHGS LAQPVRSATL NAFSACKDPA VLITTDISSR GLDVPAVDLV
IEYDPAFAVP DHVHRIGRTA RAGRAGKAVL FLLPGCEEGY TTILNSSTPI APQLYESILQ
KGLASVVNLP STHTTSETDK QTWSTRAEAL QLHLEQRLLA NPAGADDDAD DNPNPFRGNK
GNHNNNTKPK SKQYKPKIDN PLLDAARQAF RSHIRAYATH VREERVYFDI LQLHLGHLAK
AFALREPPGG IGGGVARRTH TAANKAAAER KSKVSGGGGG GGRVGFGRGA ADDDGDGVGA
VDEDAARRMR EKMRMVMNAS SEFNIG
