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DBP2_GIBZE
ID   DBP2_GIBZE              Reviewed;         554 AA.
AC   Q4IF76; A0A0E0S6F9; I1S631;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=ATP-dependent RNA helicase DBP2;
DE            EC=3.6.4.13;
GN   Name=DBP2; ORFNames=FGRRES_16145, FGSG_12302;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA
CC       decay and ribosome biogenesis through rRNA processing. {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: Associates with polysomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ESU09004.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS231664; ESU09004.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; HG970333; CEF79084.1; -; Genomic_DNA.
DR   RefSeq; XP_011321503.1; XM_011323201.1.
DR   AlphaFoldDB; Q4IF76; -.
DR   SMR; Q4IF76; -.
DR   STRING; 5518.FGSG_12302P0; -.
DR   EnsemblFungi; ESU09004; ESU09004; FGSG_12302.
DR   GeneID; 23559117; -.
DR   KEGG; fgr:FGSG_12302; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G14563; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_16_9_1; -.
DR   InParanoid; Q4IF76; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
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; 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; 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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..554
FT                   /note="ATP-dependent RNA helicase DBP2"
FT                   /id="PRO_0000232169"
FT   DOMAIN          167..342
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          357..517
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..540
FT                   /note="RNA-binding RGG-box"
FT                   /evidence="ECO:0000250"
FT   MOTIF           136..164
FT                   /note="Q motif"
FT   MOTIF           290..293
FT                   /note="DEAD box"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   554 AA;  60129 MW;  F1E2C726C7E267AD CRC64;
     MSGYDGGYSG GGGRGGGGYG GGGYGRDRGG DRGGDRNGGG FGGRSNGNGY GGGGYGGGGG
     GYGGGGFGGG AGGDRMGALG SGLKNQEWDI NSLPKFEKSF YKEHPDVETR SDADVEAFRR
     KHQMTIAGSN VPKPVETFDE AGFPRYVMDE VKAQGFPAPT AIQSQGWPMA LSGRDVVGIA
     ETGSGKTLTY CLPSIVHINA QPLLAPGDGP IVLVLAPTRE LAVQIQEEMK KFGRSSRIRN
     TCVYGGVPKG PQIRDLSRGV EVCIATPGRL IDMLEAGKTN LRRVTYLVLD EADRMLDMGF
     EPQIRKIIGQ IRPDRQTLMW SATWPKEVRA LASDFLQDFI QVNIGSMELA ANHRITQIVE
     VVTEMEKRDR MIKHMEKVME NKENKILIFV GTKRVADEIT RFLRQDGWPA LSIHGDKQQN
     ERDWVLDQFK TGKSPIMVAT DVASRGIDVR NITHVLNYDY PNNSEDYIHR IGRTGRAGAM
     GTAITLFTTD NQKQARDLVN VLQEAKQQID PRLVEMTRYG GGGGRGYGGW GRGRGGGRAN
     AHNANNMPIG NRRW
 
 
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