ID   PRP5_SCLS1              Reviewed;        1114 AA.
AC   A7ENE0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=SS1G_06839;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476628; EDO04356.1; -; Genomic_DNA.
DR   RefSeq; XP_001592598.1; XM_001592548.1.
DR   AlphaFoldDB; A7ENE0; -.
DR   SMR; A7ENE0; -.
DR   STRING; 665079.A7ENE0; -.
DR   PRIDE; A7ENE0; -.
DR   GeneID; 5488511; -.
DR   KEGG; ssl:SS1G_06839; -.
DR   InParanoid; A7ENE0; -.
DR   OMA; CGLGVQT; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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..1114
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000310227"
FT   DOMAIN          514..692
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          703..867
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          20..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..924
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           483..511
FT                   /note="Q motif"
FT   MOTIF           640..643
FT                   /note="DEAD box"
FT   COMPBIAS        20..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..308
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..915
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         527..534
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1114 AA;  122005 MW;  2F42FA989B359915 CRC64;
     MADAIEIEEM MLEDRDIAVV LEVPTRRRRS RERDYRDRRD DSYDDRARRR REDSTDSWSR
     SRGDENRGQT PRSDSGAKVH DAPKASAPAA QTEEQKKAER LAKLEAWKKK MAEDKERKEK
     ELAAGGTRKL LDDIDQKANG SSSQPSPNTP TTPSTSAISG DLAPTNYAGK FDPKAIAKKA
     VASSSSAHAL GRDLPLKELS KTSATLTSTV KGLQADKKPT AFNSTSKVSA LPKTRGNLSV
     FGLGAKVTDN EKTYQKRALD FDEDEGSRKK LEKLPTLPMA NSKEDDAALA NGIEGQDDDD
     DAELEAAGTE EEAAAAARAA AEKREERLQE AESQPHTNGD VHMEDAPQAD STAMDEDEEI
     DPLDAFMEEM GDPFSLPKSN TTFVKNNTKS QPQEPEALFG DDDVDLKALD ADPDEILAIA
     NKARKKKDIP TINYANLNLP PFRKNFYTEP AELVDMTEAE INDLRLELDG IKVAGKDVPK
     PVQKWSQCGL DVKSLDVIKK LGYDKPTSIQ MQAIPAIMSG RDVIGVAKTG SGKTIAFLLP
     MFRHIRDQRP LKNSDGPIGL IMTPTRELAT QIHKECKPFL KAMGLRAVCA YGGAIIKDQI
     ADLKRGAEII VCTPGRMIEL LAANSGRVTN LQRVTYVVLD EADRMFDMGF EPQVMKVFNN
     IRPNRQTILF SATMPRIMDA LAKKTLQSPV EIVVGGRSVV APEITQIVEV REEKEKFHRL
     LELLGELYNA DEDARTLIFV DRQEKADDLL KDLMRKGYPC MSIHGGKDQV DRDSTIDDFK
     AGVVPIMIAT SVAARGLDVK QLKLVVNFDA PNHLEDYVHR AGRTGRAGNT GTAVTFITEE
     QEQYSVGIAK ALEQSGQEVP ERLNEMRKSY KDKVKSGAKK ESSGFGGKGL ERFDAEREAT
     KARERKIHKL NGDDDEEEKE EKDDDVLLKA ASVVQPASAS TAPPKLLGVP KGIDLDGDIK
     VHRTETAASS SGSKNPLDKV TSAIDAINAR LNKTGQLRSG VPIDNKGPDA GAFHATLEIN
     DFPQKARWAV TNRTNVAKIL EATGTSITTK GSFYPAGKEV QAGGDPKLYI LVEGDTEVVV
     TNAMRELMRL LKEGTMAAAD AEGRAPASGR YTVT