PRP28_ASPNC
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 03-AUG-2022, entry version 83.
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;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., 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., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May
CC destabilize the U1/5'-splice site duplex to permit an effective
CC competition for the 5'-splice site by the U6 snRNA, resulting in the
CC switch between U1 and U6 at the 5'-splice site. May also act to unwind
CC the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC the first covalent step of splicing (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 {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. DDX23/PRP28
CC subfamily. {ECO:0000305}.
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DR EMBL; AM270075; CAK38656.1; -; Genomic_DNA.
DR RefSeq; XP_001401758.1; XM_001401721.1.
DR AlphaFoldDB; A2QIL2; -.
DR SMR; A2QIL2; -.
DR PaxDb; A2QIL2; -.
DR EnsemblFungi; CAK38656; CAK38656; An04g03920.
DR GeneID; 4990798; -.
DR KEGG; ang:ANI_1_1790184; -.
DR VEuPathDB; FungiDB:An04g03920; -.
DR HOGENOM; CLU_003041_11_3_1; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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 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; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..810
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp28"
FT /id="PRO_0000282479"
FT DOMAIN 403..609
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 620..783
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..400
FT /note="Q motif"
FT MOTIF 531..534
FT /note="DEAD box"
FT COMPBIAS 12..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
