ID   PRP5_ASPOR              Reviewed;        1186 AA.
AC   Q2U2J6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=AO090038000430;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
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DR   EMBL; AP007169; BAE64219.1; -; Genomic_DNA.
DR   RefSeq; XP_001825352.1; XM_001825300.2.
DR   AlphaFoldDB; Q2U2J6; -.
DR   SMR; Q2U2J6; -.
DR   STRING; 510516.Q2U2J6; -.
DR   PRIDE; Q2U2J6; -.
DR   EnsemblFungi; BAE64219; BAE64219; AO090038000430.
DR   GeneID; 5997447; -.
DR   KEGG; aor:AO090038000430; -.
DR   VEuPathDB; FungiDB:AO090038000430; -.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   OMA; CGLGVQT; -.
DR   Proteomes; UP000006564; Chromosome 6.
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..1186
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000232358"
FT   DOMAIN          585..763
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          794..940
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           554..582
FT                   /note="Q motif"
FT   MOTIF           711..714
FT                   /note="DEAD box"
FT   COMPBIAS        20..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..377
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..987
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         598..605
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1186 AA;  131044 MW;  03E9B4545414DEDC CRC64;
     MARHGDTRSP SPVGSTYSSS RRSRRDDDRY ERSRRDDGRS YRRSRSPEKR YRDRERDRDS
     YRRRDRSLDR RADYRDEDTY RPSRRDRSRD RRRSRDRDDD RDYRRRSRDR DFRSRRDDSR
     DRARRRTDDS ADLKHKSRRD DSRERARDSV PRSREASKPS TPAANTGPTD DEKRAERLAK
     LEAWKQKQAA EKERKQREAA AAGGTRSILD EIDRKSGLSP AVGSPQSSAT PIDAAPASYT
     GKFDPKAIAK NAAPAPAVKS VLGDDIAVPP SAKTSATFPS TKTEVQANKP SATSSKASSL
     KVKGNVGSFG LGTKQAADTE KASATKTLGF GEEESTRRKL ERLPTPPLDD AKDSNKEEDV
     TAEDEDDDVD MQDGDTEEEN AAAARAAAER REERLQNEAR DSQSNGDVQM SDASNQKAPD
     KMEVDAQEEE EVDPLDAFMS ELAESAPPKK TAGAKFAKAK PQQPEALFGD ENDMDMTAVG
     DGDADDFLAI ANKAKKKKDI PTVDHKKVEY EPFRKKFYTE PSDLAAMSEE EAASLRLELD
     GIKVRGVEVP RPVSKWSQCG LGVQTLDVID RLGYSAPTSI QAQAIPAIMS GRDVIGVAKT
     GSGKTIAFLI PMFRHIKDQR PLENMEGPVG LIMTPTRELA TQIHKDCKPF LKALNLRAVC
     AYGGAPIKDQ IADLKRGAEI IVCTPGRMID LLAANAGRVT NLRRVTYVVL DEADRMFDMG
     FEPQVMKILA NVRPDKQTVL FSATFPRNME ALARKTLNKP VEIVVGGRSV VAPEITQIVE
     VRSEDKKFIR LLELLGNLYS TDENEDARAL IFVERQEGAD TLLRELMRKG YPCMSIHGGK
     DQIDRDSTIE DFKAGIFPVL IATSVAARGL DVKQLKLVVN YDAPNHLEDY VHRAGRTGRA
     GNTGTAVTFL TEDQERYSVD IAKALKQSGQ SVPEPVQKMV DSFLEKVKAG KEKASASGFG
     GKGLERLDQE RDAARMRERK TYKTGDEGEE EEEKEEKNEK AEEQFNKVLS SVQSAAAPSL
     PGVPKGIDLD GKITVHKTEK DANGSKNPLD KVGSAVADIH ARLSRAGVMR SGVPIDNRGP
     DAGAFHATLE INDFPQKARW AVTNRTNVAK ILEATGTSIT TKGSFYATGK EPGPGENPKL
     YILVEGETEL SVTNAMRELM RLLKEGTIAA ADSDARAPVG GRYNVL