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 28-NOV-2012, entry version 35.
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; Botryotinia.
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).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Component of the U5 snRNP complex (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
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.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR EMBL; CH476842; EDN17945.1; -; Genomic_DNA.
DR RefSeq; XP_001561438.1; XM_001561388.1.
DR ProteinModelPortal; A6RJA2; -.
DR GeneID; 5442086; -.
DR KEGG; bfu:BC1G_00523; -.
DR eggNOG; COG0513; -.
DR KO; K12858; -.
DR OMA; PIRNWKE; -.
DR OrthoDB; EOG4KPXK0; -.
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 InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 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 DOMAIN 625 783 Helicase C-terminal.
FT NP_BIND 424 431 ATP (By similarity).
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
//
