GenomeNet

Database: UniProt
Entry: Q2H2J1
LinkDB: Q2H2J1
Original site: Q2H2J1 
ID   DBP4_CHAGB              Reviewed;         825 AA.
AC   Q2H2J1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   18-SEP-2019, entry version 69.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; ORFNames=CHGG_04005;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC
OS   6347 / NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   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
RT   globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome
CC       biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal
CC       complexes. Required for pre-rRNA cleavage at site A2 (By
CC       similarity). {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
CC       pre-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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH408032; EAQ87386.1; -; Genomic_DNA.
DR   RefSeq; XP_001223219.1; XM_001223218.1.
DR   SMR; Q2H2J1; -.
DR   STRING; 38033.XP_001223219.1; -.
DR   EnsemblFungi; EAQ87386; EAQ87386; CHGG_04005.
DR   GeneID; 4391717; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; Q2H2J1; -.
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: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   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   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; 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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    825       ATP-dependent RNA helicase DBP4.
FT                                /FTId=PRO_0000256000.
FT   DOMAIN       84    258       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      284    439       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      97    104       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        53     81       Q motif.
FT   MOTIF       206    209       DEAD box.
FT   COMPBIAS    716    768       Gly-rich.
SQ   SEQUENCE   825 AA;  91324 MW;  52D67004262A40A3 CRC64;
     MAAGNAKGGF AHRNKSVPKK TDAKSLKRKR GQEDLGKLKA AIEELDPKSP AIKQFTDLPL
     CEATASGLRA SHFEVLTDVQ RAAIPLALKG RDILGAAKTG SGKTLAFLVP VLEKLYHAKW
     TEYDGLGALI ISPTRELAVQ IFEVLRKIGR NHFFSAGLVI GGKSLKEEAE RLGRMNILVC
     TPGRMLQHLD QTANFDVNNL QILVLDEADR IMDMGFQSAV DALVEHLPTT RQTLLFSATQ
     SKRVSDLARL SLKEPEYVSA HEAAVSATPT NLQQSYIVTP LAEKLDTLFG FLRTNLKSKI
     IVFFSSGKQV RFVFESFKRM QPGIPLLHLH GRQKQVARME ITSRFSSAKY GCLFATDVVA
     RGVDFPAVDW VVQADCPEDA DTYIHRVGRT ARYESKGRAV LFLEPSEEAG FLKRLEQKKV
     PLQKVNVREN KKKSIKNELQ SYNFQSPDLK YLGQKAFISY TRSIYLQKDK EVFNFNKLDL
     DGYAASLGLA GTPQIKYQKG DDIKRLKNAS RAAISSGSES DSDDEGKPKK DKKQVRTKYE
     KMAERQNQDI LSSHYRKLLG EDGDAAASDD DDDFLSVKRV LADDAQIDAA AGGDATNTTT
     TEPKVIKLGN SELIIDSNRR EKLLKSKKKL LKYMDKGTKL VFDDDGVARP VYELQDEDDF
     AQQGPAAALR QQFVAAESEK VKEADVDDKQ AAKMRRREKR ERQKARERGE ELERVGAGGG
     GGGVAMLDGG EGDEGDEDPL ALLRSLPIAG EESDGGRGGG GEDEGDDGEV EPPRKKARKW
     FQDDSDQEEE ERQKKKKGGK KVIEMAEEPE NLEDLEALAA GLLED
//
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