ID M7TXU1_BOTF1 Unreviewed; 817 AA.
AC M7TXU1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 {ECO:0000256|ARBA:ARBA00040398};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28 {ECO:0000256|ARBA:ARBA00039685};
GN ORFNames=BcDW1_5299 {ECO:0000313|EMBL:EMR86079.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR86079.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBUNIT: Component of the U5 snRNP complex.
CC {ECO:0000256|ARBA:ARBA00038719}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000256|ARBA:ARBA00037954}.
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DR EMBL; KB707874; EMR86079.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TXU1; -.
DR STRING; 1290391.M7TXU1; -.
DR HOGENOM; CLU_003041_11_3_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd17945; DEADc_DDX23; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF56; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EMR86079.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00023187};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 380..408
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 411..614
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 625..788
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 380..408
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 17..65
FT /note="Pro 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 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 89384 MW; DEAF6F724B87E440 CRC64;
MASNGYSNSA DAVPPPPSDN DGRPPSPPPP PPDSFVPPPP PSSLAPPPPP SSDLPPPPPS
ELLPPPPEPK KKKGWGAPKP GPLSIEDILK KKKEADEAAA KPKFLSKAAR EKLALEKRAK
EVEEQKRKRE AEQDNRISIG SVNGNGNGYG SAANGRDGYE 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 MLTKSSISRV
PEELRKHEAA QQKSQRGQGM KKIEEGGFGG KGGGGGW
//
