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Database: UniProt
Entry: A2QIL2
LinkDB: A2QIL2
Original site: A2QIL2 
ID   PRP28_ASPNC             Reviewed;         810 AA.
AC   A2QIL2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   31-JUL-2019, entry version 73.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE            EC=3.6.4.13;
GN   Name=prp28; ORFNames=An04g03920;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing.
CC       May destabilize the U1/5'-splice site duplex to permit an
CC       effective competition for the 5'-splice site by the U6 snRNA,
CC       resulting in the switch between U1 and U6 at the 5'-splice site.
CC       May also act to unwind the U4/U6 base-pairing interaction in the
CC       U4/U6/U5 snRNP, facilitating the first covalent step of splicing
CC       (By 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: Component of the U5 snRNP complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {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. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
DR   EMBL; AM270075; CAK38656.1; -; Genomic_DNA.
DR   RefSeq; XP_001401758.1; XM_001401721.1.
DR   SMR; A2QIL2; -.
DR   PaxDb; A2QIL2; -.
DR   PRIDE; A2QIL2; -.
DR   EnsemblFungi; CAK38656; CAK38656; An04g03920.
DR   GeneID; 4990798; -.
DR   KEGG; ang:ANI_1_1790184; -.
DR   HOGENOM; HOG000268796; -.
DR   KO; K12858; -.
DR   Proteomes; UP000006706; Chromosome 6L.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN         1    810       Pre-mRNA-splicing ATP-dependent RNA
FT                                helicase prp28.
FT                                /FTId=PRO_0000282479.
FT   DOMAIN      403    609       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      620    783       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     416    423       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       372    400       Q motif.
FT   MOTIF       531    534       DEAD box.
FT   COMPBIAS     14     81       Pro-rich.
SQ   SEQUENCE   810 AA;  89810 MW;  7373DB3B22B0418D CRC64;
     MDGIMTNGSS EAHPPMPPPE PIERPPTPPP PPPEDSALPP PPPDTSAPPP PPEDLPPAPP
     PETEPKKKKV GWGTKRPAPT PLSVEELVRK KREADAAAAK PKFLSKKERE KLALEKRAQE
     VAATRRLKSE HASNGVDRSA THSPSVSSEG PNGDARSIPT GPRAMRNSDA APTAPAAMRH
     SQSHNKNYDL APPPPPKSMS FGLTSGKGDS RFVDEDEAAA QAALVKQRYM GADQTSNFSA
     KKKRKRTTDR KFNFEWNAEE DTSGDYNPLY QHRHETNFFG RGRLAGFGDD VAESVAHKYA
     RALEDRDREA GSIRAREILE MERRRREEST RNQLDKHWSE KKLEHMRERD WRIFKEDFNI
     STKGGSVPNP MRSWDESNLP KRLMELINRV GYKEPTPIQR AAIPIAMQNR DLIGVAVTGS
     GKTAAFLLPL LCYIAELPRI DEFEWRKADG PYAIVLAPTR ELAQQIEIEA KKFTGPLGFN
     VVSIVGGHSL EEQAYSLRDG AEIIIATPGR LVDCIERRIL VLSQCCYVIM DEADRMIDLG
     FEEPVNKILD ALPVSNEKPD SEDAENPLAM SRHINHDQHR YRQTMMYTAT MPTAVERIAR
     KYLRRPAIVT IGSAGEAVDT VEQRVEMIAG EDKRKKRLGD ILSSGEFRAP IIVFVNIKRN
     CDAIAREIKQ WGFSSVTLHG SKTQDQREAA LASVRNGTTD VLVATDLAGR GIDVPDVSLV
     VNFNMATSIE SYTHRIGRTG RAGKSGVAIT FLGNEDADVM YDLKQMLMKS PISRVPEELR
     KHEAAQSKPT RGFSSKKNNE EGGGGGKVGW
//
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