ID   PRP28_NEUCR             Reviewed;         728 AA.
AC   Q7SEL0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp-28;
DE            EC=3.6.4.13;
GN   Name=prp-28; ORFNames=NCU02803;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA35223.1; -; Genomic_DNA.
DR   RefSeq; XP_964459.1; XM_959366.2.
DR   AlphaFoldDB; Q7SEL0; -.
DR   SMR; Q7SEL0; -.
DR   STRING; 5141.EFNCRP00000002412; -.
DR   PRIDE; Q7SEL0; -.
DR   EnsemblFungi; EAA35223; EAA35223; NCU02803.
DR   GeneID; 3880623; -.
DR   KEGG; ncr:NCU02803; -.
DR   VEuPathDB; FungiDB:NCU02803; -.
DR   HOGENOM; CLU_003041_11_3_1; -.
DR   InParanoid; Q7SEL0; -.
DR   OMA; KKFNFEW; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..728
FT                   /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp-28"
FT                   /id="PRO_0000232376"
FT   DOMAIN          324..527
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          538..701
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          19..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           293..321
FT                   /note="Q motif"
FT   MOTIF           450..453
FT                   /note="DEAD box"
FT   COMPBIAS        19..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         337..344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   728 AA;  82612 MW;  60AFF9AAA19E8B27 CRC64;
     MSTTSRREPP DLAALLRKKK EEEAAAAKPR FIPKKERERL EAEKKAKEEE ERKRKEEAKP
     QPNGTNHNGN RMDGIQSHHN HNPQRNIPTG PKAMRYDDDR GPNGMSNGRD YRDNRDNRDN
     RDRNQRGAKR GAPNDDEEKR AKMERNDEAE LRARYMGPVV NQSTFSAKKK RRRTAANKFN
     FDWDADDDTS RPFDPIYAER QEPLVRLGGY EMTEEMVMRK AEAIRRGDPE TGEERARQYL
     EQHRRIKEME QRKNLGKHWS EKKLEDMKER DWRIFKENFG IATKGGAIPN PMRSWEESTL
     PRRLLDIVKN VGYDEPTPIQ RAAIPIALQA RDLIGVAVTG SGKTAAFLLP LLVYISELPP
     LTEYNKNDGP YALILAPTRE LVQQIESEAK KFATPLGFTV VSIVGGHSLE EQAFALRNGA
     EIIVATPGRL VDCLERRLLV FSQCCYTIMD EADRMIDQGF EEPLTKILDA MPVTNEKPDT
     DDAENPQLMS RYVDGKDRYR QTMMYTATMP PIVERIAKKY LRRPAIVTIG NAGEAVDTVE
     QRVEFVSGED KRKKRLQEIL NSGQFKPPII VFVNIKRNCD MVARDIKGMG YSAVTLHGSK
     TQEQREAALA SLRNGQTDIL VATDLAGRGI DVPDVSLVVN FNMATNIESY THRIGRTGRA
     GKSGVAITFL GPEDNDVLYD LRQIISKSSI SKVPDELRRH EAAQNKPQKG QKKLEESNGY
     SGKGGSWN