DBP7_PHANO
ID DBP7_PHANO Reviewed; 831 AA.
AC Q0UHM7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; ORFNames=SNOG_08737;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445337; EAT83905.1; -; Genomic_DNA.
DR RefSeq; XP_001799045.1; XM_001798993.1.
DR AlphaFoldDB; Q0UHM7; -.
DR SMR; Q0UHM7; -.
DR STRING; 13684.SNOT_08737; -.
DR EnsemblFungi; SNOT_08737; SNOT_08737; SNOG_08737.
DR GeneID; 5975944; -.
DR KEGG; pno:SNOG_08737; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q0UHM7; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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 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..831
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000256027"
FT DOMAIN 218..419
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 456..670
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 65..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 185..214
FT /note="Q motif"
FT MOTIF 353..356
FT /note="DEAD box"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 831 AA; 91247 MW; 86B525D071775E32 CRC64;
MADDGMLLNF SIPETGILSR PSLKGGNWRD RAAAKKAAQN WHTKASARLT GEKVDKVAKK
TVENATDVNR TQLGQRTRRA SKSPEVHEDI DRPAKRARVS GDFRPKSNEK SAAEAGDYRP
QINPGATQKP SERQSAPKGA KGGKQVISSL FTYNPTSTTK TQAPEKRHDE EPIEPSNAPL
SSELDTFTSL GISTTLAAHL LKKMDLKAPT AIQKAAITQL VKDDSDAFIQ AETGSGKTLA
YLLPIVQRLM ELSANMKKHK DDDAVQRNSG LFAIIMAPTR ELSKQIALVL EKLLGCAHWL
VATTVIGGEK KKSEKARLRK GINILVATPG RLADHLEHTE ALDVSNVRWL VLDEGDRLME
LGFEQEIQKI VGALNLRMRG NKTRIPGLPD KRTTVLCSAT MKMDVERLGQ ISLKDAVHLR
ADPTEREQEG DEPQDERSYA PAQLKQSYAV VAPKLRLVSL IAYLKRAFTR KGSVMKAIVF
VSCADSVDFH FDILTSNLEE KNEKAEGTKD DTEEKADDDE PKKSTKKPKA IPQADPTKLS
VTHAESPVLS PKSHAVTAYR LHGSLQQSLR TSTLAHFTKN NDAAVLIATD VASRGLDLPN
VDLVVEFDPA FAREDHLHRI GRTARAGRDG RACIFLMPGP EEGYVDILKT DRKDNEAGIT
ITRQDADDIL TRGLVTSGIA TKNAYMDIAQ DLQLNVERWA LASPARLESA RRAFQSHIRA
YATHVADERK YFDIKSLHLG HLAKAFALRE RPSGMKAPGL RTGAGRNDRT PAKIRGANAA
KIGSAPAAKK AVDLDIPDAK DTEEAAKMRK AVRAREKFMR HAGMADEFNL G
