PRP5_ASPNC
ID PRP5_ASPNC Reviewed; 1180 AA.
AC A2QQA8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE EC=3.6.4.13;
GN Name=prp5; ORFNames=An08g01850;
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 spliceosome assembly and
CC in nuclear splicing. Catalyzes an ATP-dependent conformational change
CC of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP
CC association with intron RNA (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 -!- SUBCELLULAR LOCATION: 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. DDX46/PRP5
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK39865.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM270161; CAK39865.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001392304.2; XM_001392267.2.
DR AlphaFoldDB; A2QQA8; -.
DR SMR; A2QQA8; -.
DR PaxDb; A2QQA8; -.
DR PRIDE; A2QQA8; -.
DR EnsemblFungi; CAK39865; CAK39865; An08g01850.
DR GeneID; 4982500; -.
DR KEGG; ang:ANI_1_282074; -.
DR VEuPathDB; FungiDB:An08g01850; -.
DR Proteomes; UP000006706; Chromosome 8R.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:1990446; F:U1 snRNP binding; IEA:EnsemblFungi.
DR GO; GO:1990447; F:U2 snRNP binding; IEA:EnsemblFungi.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IEA:EnsemblFungi.
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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1180
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT /id="PRO_0000282691"
FT DOMAIN 578..756
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 783..933
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 547..575
FT /note="Q motif"
FT MOTIF 704..707
FT /note="DEAD box"
FT COMPBIAS 20..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 591..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1180 AA; 130133 MW; F500B4CDA5147C49 CRC64;
MARHGDTRSP SPVGSTYSSS RRNRRDDDRY ERSRRDDGRS YRRSRSPERR YRERERDRDR
DAFRRRDRSL DRRDEDSYRP GRRERSRDRR RSRERDDYRR RSRDRDYRSR REDSRDRARR
RTDDSADLKY KSRRDDSRDR AKDAPRSRET SKPSTPAATA APTEDEKRAE RLAKLEAWKQ
KQAAEKERKQ REAAAAGGAR SILEEIDRKS GLSPAVSSPQ SPATPGVDAT PGTYTGKFDP
KAIAKSASST PAPPAVLGND VAVPPSVKPV TTIPSQVKPK STTSASATLK AKGNVGGFGL
GTKQAADTEK STATKTLGFG EEESTRRKLE RLPTPPLEDA KDVNGTADGA ADEDEDDVDM
QDGGTEEEAA AAARAAAERR EERLQSEAIK AQSNGAESND TVMGDAPSQE AADNMEVDAQ
EEEEIDPLDA FMSELAESAP PKKKVGAKFS RTKEQQPEAL FGDEHDIDMT AVGDGDADDF
LAIANKAKKK KDIPAVDHKK VEYETFRKKF YTEPSDLAQM SDEEAASLRL ELDGIKVRGV
DVPKPVQKWS QCGLGVQTLD VIDKLGYEKT TSIQAQAIPA IMSGRDVIGV AKTGSGKTIA
FLIPMFRHIK DQRPLDNMEG PVGLIMTPTR ELATQIHKDC KPFLKALNLR AVCAYGGAPI
KDQIADLKRG AEIIVCTPGR MIDLLAANAG RVTNLRRVTY VVLDEADRMF DMGFEPQVMK
IMANIRPDRQ TVLFSATFPR NMEALARKTL TKPIEIVVGG KSVVAPEITQ IVEVRNDDQK
FVRLLELLGN LYSSDENEDA RALIFVDRQE AADALLRELM RKGYPCMSIH GGKDQIDRDS
TIEDFKAGIF PVLIATSVAA RGLDVKQLKL VVNYDAPNHL EDYVHRAGRT GRAGNTGTAV
TFLTEDQERY SVDIAKALKQ SGQKVPEPVQ KLVDAFLEKV KAGKEKASAS GFGGKGLERL
DQERDAARMR ERRTYKTGEE GEDEEEKEEK NEQAEERFNK AISSVQSTAA PSLPGVPKGI
DLDGKITVHK TEKDPNSTSK NPLDKVGSAV ADIHARLSRA GVMRSGVPID NRGPDAGAFH
ATLEINDFPQ KARWAVTNRT NVAKILEATG TSITTKGSFY PTGKVPGPGE NPKLYILVEG
ETELAVTNAM RELMRLLKEG TIAAADSDAR APVGGRYNVV
