ID   PRP5_BOTFB              Reviewed;        1151 AA.
AC   A6RW79;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=BC1G_04866;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476861; EDN23597.1; -; Genomic_DNA.
DR   RefSeq; XP_001556848.1; XM_001556798.1.
DR   AlphaFoldDB; A6RW79; -.
DR   SMR; A6RW79; -.
DR   PRIDE; A6RW79; -.
DR   OMA; CGLGVQT; -.
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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus.
FT   CHAIN           1..1151
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000310226"
FT   DOMAIN          585..763
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          774..938
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..427
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        18..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..379
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..404
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   1151 AA;  127330 MW;  EB7CBF3EC2E6F1FE CRC64;
     MARHRDSRSP SPTGSHHSSR RNRRDDNGRR DRDRRDDVRG QRRSRSPDRR ERDRDMNRRR
     DRSVGRLNDD YHRSGRRERS RDRRSYADRE RSPDRRRRRS RERDYRDRRD DSYDDRARRR
     REDSTDSWSR SRGDETRGQT PRSDAGAKVN DAPKVSTPAV QTEEQKKAER LAKLEAWKKK
     MAEDKERKEK ELAAGGTRKL LDAIDQKANG SPSLTSPNSP TTPATPATPG DLAPPTNYAG
     KFDPKAIAKK AVASSSSAHT LGKDLPLKEL SKASATLTST VKGLQADKKP TAFSSTSKVS
     ALPKTRGNLS VFGLGAKVTD NEKTSQKRAL DFDEDEGSRK KLEKLPSLPM ANTEEDDAAL
     ANGVEEQDDD DDADLEAAGT EEEAAAAARA AAEKREERLQ EAEAQPHTNG DVQMEDAPQP
     DSTAMDEDEE IDPLDAFMEE MGDPFSLPKN NATFIKDNIK SQPQEPEPLF GDDDVDLKAL
     DADPDEILAI ANKARKKKDI PTINYSALDL PPFRKNFYTE PTELAEMTEA EIADLRLELD
     GIKVAGKDVP KPVQKWSQCG LDVKSLDVIT KLGYERPTSI QMQAIPAIMS GRDVIGVAKT
     GSGKTIAFLL PMFRHIRDQR PLKGSDGPIG LIMTPTRELA TQIHKECKPF LKAMGLRAVC
     AYGGAIIKDQ IADLKRGAEI IVCTPGRMIE LLAANSGRVT NLQRVTYVVL DEADRMFDMG
     FEPQVMKVFN NIRPNRQTIL FSATMPRIMD ALAKKTLQSP VEIVVGGRSV VAPEITQIVE
     VREEKEKFHR LLELLGELYN TDEDARTLIF VDRQEKADDL LKDLMRKGYP CMSIHGGKDQ
     VDRDSTIDDF KAGVVPIMIA TSVAARGLDV KQLKLVVNFD APNHLEDYVH RAGRTGRAGN
     TGTAVTFITE EQEQYSVGIA KALEQSGQEV PDRLNEMRKS YKDKVKSGAK KESSGFRGKG
     LERFDAEREA TKARELVQPA ASTAPPKLLG VPKGIDLDGD IKVHRTEPAA TTGSKLDKVT
     SAIDAINARL NKTGQLRSGV PIDNKGPDAG AFHATLEIND FPQKARWAVT NRTNVAKILE
     ATGTSITTKG SFYPAGKEVQ ADPKLYILVE GDTEVVVTNA MRELMRLLKE GTMAAADAEG
     RAPVGGRYTV T