PRP28_PHANO
ID PRP28_PHANO Reviewed; 746 AA.
AC Q0UWC8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE EC=3.6.4.13;
GN Name=PRP28; ORFNames=SNOG_03936;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT89141.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH445329; EAT89141.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001794480.1; XM_001794428.1.
DR AlphaFoldDB; Q0UWC8; -.
DR SMR; Q0UWC8; -.
DR STRING; 13684.SNOT_03936; -.
DR PRIDE; Q0UWC8; -.
DR GeneID; 5971343; -.
DR KEGG; pno:SNOG_03936; -.
DR eggNOG; KOG0333; Eukaryota.
DR InParanoid; Q0UWC8; -.
DR OMA; KKFNFEW; -.
DR OrthoDB; 820037at2759; -.
DR Proteomes; UP000001055; 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..746
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT /id="PRO_0000256019"
FT DOMAIN 358..556
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 567..730
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 327..355
FT /note="Q motif"
FT MOTIF 484..487
FT /note="DEAD box"
FT COMPBIAS 1..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 371..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 746 AA; 83308 MW; 6EB901F718BCCE3F CRC64;
MTDTTLPPPP PPPPPPADKM PPPPPTDVPP PPPPQEEELG PVLVPSKKAK KGWASQRKQP
PSIDDILKAK REQEAAAAKP KFLSKAERER IALEKRRKEV EEAQRRREGS NSSTNGASHK
GHYDASSSIP TGPRAMRPEA PSGPPSRQQR SNGDMAPPPL PDKKTGKRPP PEDAEAAMIR
QRYMGAEQNQ STFSAKKKRK RTTEKKFNFE WNEEEDTSYD YNPIYQQKAE AGFFGRGRLG
GFTEDVTEQG TQKFIEAMIE RDPVSGRERA ERILDMERRR KEEGGRAQLD KHWSEKKLEH
MRERDWRIFK EDFNIATKGG AIPNPMRNWQ ESGLPDKVLR LVEHVGYAEP SAVQRAAIPI
ALQCRDLIGV AVTGSGKTAS FVLPLLVYIS QLPPLGPSNR ADGPYAIVLA PTRELAQQIE
VETRKFAAPL GFNTAVIVGG HSIEEQAFQM RDGAEIVIAT PGRLVDCIER RMLVLSQCTY
VIMDEADRMI DMGFEEPVNK ILDALPVTNE KPDSDAAEDP NAMKRGMYRQ TMMYTATMPT
AVERIARKYL RRPAIVTIGN VGEAVETVEQ RVEHIQGEEK RKKRLQEILN SGEFTPPIIV
FVNIKRNCDA IARDIKNMGF SSVTLHGSKT QEQREAALAQ LREHRVDVLV ATDLAGRGID
ITDVSLVVNF NMATSIESYT HRIGRTGRAG KSGVAITFWG NEDADVLYDL KQMLTKSQIS
KVPEDLRKHE AAQQKGGRNK EKKALT
