ID   PRP28_SCLS1             Reviewed;         816 AA.
AC   A7EGG4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE            EC=3.6.4.13;
GN   Name=prp28; ORFNames=SS1G_04405;
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 in mRNA splicing. May
CC       destabilize the U1/5' splice site duplex to permit an effective
CC       competition for the 5' splice site by the U6 snRNA, resulting in the
CC       switch between U1 and U6 at the 5' splice site. May also act to unwind
CC       the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC       the first covalent step of splicing (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   -!- SUBUNIT: Component of the U5 snRNP complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476625; EDO01930.1; -; Genomic_DNA.
DR   RefSeq; XP_001594598.1; XM_001594548.1.
DR   AlphaFoldDB; A7EGG4; -.
DR   SMR; A7EGG4; -.
DR   STRING; 665079.A7EGG4; -.
DR   EnsemblFungi; EDO01930; EDO01930; SS1G_04405.
DR   GeneID; 5491199; -.
DR   KEGG; ssl:SS1G_04405; -.
DR   eggNOG; KOG0333; Eukaryota.
DR   HOGENOM; CLU_003041_11_3_1; -.
DR   InParanoid; A7EGG4; -.
DR   OMA; KKFNFEW; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; 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:0003723; F:RNA binding; IBA:GO_Central.
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; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..816
FT                   /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp28"
FT                   /id="PRO_0000310208"
FT   DOMAIN          410..613
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          624..787
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           379..407
FT                   /note="Q motif"
FT   MOTIF           536..539
FT                   /note="DEAD box"
FT   COMPBIAS        18..65
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         423..430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   816 AA;  89525 MW;  8507DCE267C58C15 CRC64;
     MASNGYLNSI DAVPPPLIDS DGRPPSPPPP PPDSFVPPPP PSSLAPPPPP SSDLPPPPPS
     ELQPPPPEPK KKKGWGAPKP GPLSIEDILK KKKEADEAAA KPKFLSKAAR EKLALEKRAK
     EVEEQRRKRE SEQDNRIPVG TVNGNGYGAA NGRDGYERSH QQDNARRDSS FVPTGPRAMR
     NGQQNRPSSD KPNDMEPPPK SAKPATTAAG SSKASVAGEK RPANAEDLQA ALIRTRYMGA
     ETNQSTFSAK KKRRRTTEKK FNFEWNAEED TSPDYNPIYQ NRAEAGLYGR GRLAGFAEDE
     AATLKYAKAL EERDIEAGSA RAREIVEMER RRKEDAGRNS LDKHWSEKKL EHMRERDWRI
     FKEDFNISTK GGAIPNPMRS WSESKLPKRL LDVINQVGYD EPSAVQRAAI PIALQARDLI
     GVAVTGSGKT AAFLLPLLVY ISELPPLNEF TKNDGPYAII LAPTRELAQQ IEVEAKKFAT
     PLGFTCVSIV GGHSLEEQSY NLRNGAEIII ATPGRLVDCI ERRVLVLGQC CYIIMDEADR
     MIDLGFEESV NKILDALPVS NEKPDTDDAE DAQAMSRHLG GKDRYRQTMM YTATMPPAVE
     KIAKKYLRRP AIVTIGNIGE AVETVEQRVE FVAGEDKRKK RLNEILASGE FQPPIIVFVN
     IKRNCDAVAR DIKHMGFTSV TLHGSKTQEQ REAALASVRS GATNVLVATD LAGRGIDVPD
     VSLVVNFNMA TNIESYTHRI GRTGRAGKSG VAITFLGNED ADTMYDLKQM LMKSSISRVP
     EELRKHEAAQ QKSQRGQGLK KIEEGGFGGK GGAGGC