ID   PRP5_MAGO7              Reviewed;        1012 AA.
AC   A4RN46; G4MZC4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; ORFNames=MGG_11403;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(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; CM001232; EHA53679.1; -; Genomic_DNA.
DR   RefSeq; XP_003713486.1; XM_003713438.1.
DR   AlphaFoldDB; A4RN46; -.
DR   SMR; A4RN46; -.
DR   STRING; 318829.MGG_15532T0; -.
DR   EnsemblFungi; MGG_15532T0; MGG_15532T0; MGG_15532.
DR   GeneID; 12987087; -.
DR   KEGG; mgr:MGG_15532; -.
DR   VEuPathDB; FungiDB:MGG_15532; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   InParanoid; A4RN46; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000009058; Chromosome 2.
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..1012
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000294649"
FT   DOMAIN          409..587
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          614..762
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           378..406
FT                   /note="Q motif"
FT   MOTIF           535..538
FT                   /note="DEAD box"
FT   COMPBIAS        8..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..178
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         422..429
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1012 AA;  108571 MW;  AD254FA06546B31D CRC64;
     METEQQQRKD SVASAGSTRQ LLAQMDVKAT GSPSAMTSPG AASPATAQSA EDASPAVPYG
     GKFDPKAIAK KASARHQSPT VLGALQGRAA EKTAVSIAAP AKGSAASSLP QGKPISGFGF
     GKASNDDKVP TKRKLNLDDE EISKRKLAKL PDLSLETTDD APYVNQDDDE DSDGDNFAGT
     EEEAAAAARA AHERREERIL QQSMAMETDE ANPAAEGQVN GSEPAVSSAN APEEAQAKPQ
     TDSMDVDTKE DDDEVDPLDA FMADLTEPSF GPASKPVKTL SSAKVLPTPE AYFSDDDEFG
     ASTKEGVDAK AIMAMAAKRK KKEIPTIDYS KLDIVPVRKN FWVEPYELSE MTEAEVAELR
     LELDGIKVSG KDVPKPVQKW SLCGLTRPIL DVIAKLEYDK PTAIQMQALP VIMSGRDVVG
     VAKTGSGKTM AFLLPMFRHI KDQEPVKDNE GPIGLILTPT RELAVQIFRD CKPFLKTLGL
     RAVCAYGGPP IKDQIADLKR GAEIVVATTG RMIDLLAANQ GRVVSLRRTT YIVLDEADRM
     FDMGFEPQVM KIFANVRPDR QTVLFSATMP KIMDALVKKV LKNPVEIEVG GKSVVASEIT
     QIVEIRDEKS KFNRLLELLG ELYKDDDDVR SLIFVERQEK ADELLRELLR KGYGCMSLHG
     GKDQVDRDST ISDFKSGVCP VMIATSVAAR GLDVKQLKLV VNYDAPNHLE DYVHRAGRTG
     RAGNTGTAVT FVTEEQENCA IGIAKALEQS GQPVPEKLIE MRKAFREKVK AGKAKDQSGF
     GGKGLEKLDK EREAARNRER KTHKAEGEED DAEDDKKTTK NDEKTDKASS AILGAASAIV
     SRDAAKAEAE AKAAEGGSTP TAAATPAAGG KGGALDKAAS AINEINARLA RAGQLRPGQP
     IDNKGPDAGA FHATLEINDF PQKARWAVTN RTNVAKILEA TGTSITTKGN YYPPGKDPPA
     GADPKLYILI EGDTELVVGN ALSELTRLLK EGTMAAADAE SRAPASGRYT IT