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Database: UniProt
Entry: A6RJA2
LinkDB: A6RJA2
Original site: A6RJA2 
ID   PRP28_BOTFB             Reviewed;         783 AA.
AC   A6RJA2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   01-OCT-2014, entry version 43.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE            EC=3.6.4.13;
GN   Name=prp28; ORFNames=BC1G_00523;
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.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   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.
CC       May destabilize the U1/5' splice site duplex to permit an
CC       effective competition for the 5' splice site by the U6 snRNA,
CC       resulting in the switch between U1 and U6 at the 5' splice site.
CC       May also act to unwind the U4/U6 base-pairing interaction in the
CC       U4/U6/U5 snRNP, facilitating the first covalent step of splicing
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of the U5 snRNP complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00542}.
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DR   EMBL; CH476842; EDN17945.1; -; Genomic_DNA.
DR   RefSeq; XP_001561438.1; XM_001561388.1.
DR   ProteinModelPortal; A6RJA2; -.
DR   STRING; 332648.A6RJA2; -.
DR   GeneID; 5442086; -.
DR   KEGG; bfu:BC1G_00523; -.
DR   eggNOG; COG0513; -.
DR   KO; K12858; -.
DR   OMA; PIRNWKE; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; DNA/RNA_helicase_DEAD/DEAH_N.
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; 2.
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.
FT   CHAIN         1    783       Pre-mRNA-splicing ATP-dependent RNA
FT                                helicase prp28.
FT                                /FTId=PRO_0000310207.
FT   DOMAIN      411    614       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      625    783       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     424    431       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       380    408       Q motif.
FT   MOTIF       537    540       DEAD box.
FT   COMPBIAS     14     82       Pro-rich.
SQ   SEQUENCE   783 AA;  85754 MW;  13CEE0292155AFDF CRC64;
     MASNGYSNSA DAVPPPPSDN DGRPPSPPPP PPDSFVPPPP PSSLAPPPPP SSDLPPPPPS
     ELLPPPPEPK KKKGWGAPKP GPLSIEDILK KKKEADEAAA KAKFLSKAAR EKLALETRAK
     EVEEQKRKRE AEQDNRISIG SVNGNGNGYG SAANGPDGYE RSYQQENGRR ESSFVPTGPR
     AMRNSQQSRS SSDKPNDMEP PPKPAKSAAA GTGKASVAGE KRPANAEDLQ AALIKTRYMG
     AETNQSTFSA KKKRRRTTEK KFNFEWNAEE DTSPDYNPIY QNRAEAGLYG RGRLGGFAED
     EGATLKYAKA LEERDAEAGG ARAREIVEME RRRKEDAGRN SLDKHWSEKK LEHMRERDWR
     IFKEDFNIST KGGAIPNPMR NWSESKLPKR LLDVIHQVGY DEPSAVQRAA IPIALQARDL
     IGVAVTGSGK TAAFLLPLLV YISELPPLNE FTKNDGPYAI ILAPTRELAQ QIEVEAKKFA
     TPLGFTCVSI VGGHSLEEQS YNLRNGAEII IATPGRLVDC IERRVLVLGQ CCYIIMDEAD
     RMIDLGFEES VNKILDALPV SNEKPDTDDA EDAQAMSRHL GGKDRYRQTM MYTATMPPAV
     EKIAKKYLRR PAIVTIGNIG EAVETVEQRV EFVAGEDKRK KRLNEILASG EFAPPIIVFV
     NIKRNCDAVA RDIKHMGFTS VTLHGSKTQE QREAALASVR SGATNVLVAT DLAGRGIDVP
     DVSLVVNFNM ATNIESYTHR IGRTGRAGKS GVAITFLGNE DSDTMYDLKQ MLTKSSISRC
     RKS
//
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