ID   PRP28_ASPTN             Reviewed;         783 AA.
AC   Q0CLX0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE            EC=3.6.4.13;
GN   Name=prp28; ORFNames=ATEG_05314;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34383.1; -; Genomic_DNA.
DR   RefSeq; XP_001214492.1; XM_001214492.1.
DR   AlphaFoldDB; Q0CLX0; -.
DR   SMR; Q0CLX0; -.
DR   STRING; 341663.Q0CLX0; -.
DR   EnsemblFungi; EAU34383; EAU34383; ATEG_05314.
DR   GeneID; 4321214; -.
DR   VEuPathDB; FungiDB:ATEG_05314; -.
DR   eggNOG; KOG0333; Eukaryota.
DR   HOGENOM; CLU_003041_11_3_1; -.
DR   OMA; KKFNFEW; -.
DR   OrthoDB; 75792at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; 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..783
FT                   /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp28"
FT                   /id="PRO_0000282480"
FT   DOMAIN          374..583
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          594..757
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           343..371
FT                   /note="Q motif"
FT   MOTIF           502..505
FT                   /note="DEAD box"
FT   COMPBIAS        1..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         387..394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   783 AA;  86214 MW;  05122AD413B4B786 CRC64;
     MPGPPATAPP PEPIERPPTP PPPPPEDSAA PPPPPDMSAP PPPPQDELPP APEPKKKKLG
     WGSKRPAAAP LSVEELVRKK READAAAAKP KFLSKKEREK IALEKRAKEV EQSRRKTSTN
     GASDTASVRS ESATPNGVDR TASIPTGPRA MRTSEAPPPP RPRHDSSSNG NGNSNSNSNS
     NGTVDEDEAA AQAALVKQRY MGAEMTSSFS AKKKRKRTTD RKFNFEWNAE EDTSRDYNPL
     YAQRHEANFF GRGRLAGFGD DVADGVARKY AAALEDRDRE AGSVRAREIL EMERRRREES
     TRNQLDKHWS EKKLEHMRER DWRIFKEDFN IATKGGSVPN PMRSWAESGL PSRLLDLVHR
     VGYKDPTPIQ RAAIPIAMQS RDLIGVAVTG SGKTAAFLLP LLVYIAELPR IDEFEWRKND
     GPYAIVLAPT RELAQQIEIE AKKFTIPLGF TVVSIVGGHS LEEQAYSLRN GAEIIIATPG
     RLVDCIERRL LVLSQCCYVI MDEADRMIDL GFEEPVNKIL DALPVSNEKP DSDAAENAAA
     MSQLHHAGGG RDTRYRQTMM YTATMPTAVE RIARKYLRRP AIVTIGSAGE AVDTVEQRVE
     LIAGEDKRKK RLGDILSSGE FRPPIIVFVN IKRNCDAIAR EIKQWGFSSV TLHGSKTQEQ
     REAALASVRN GSTDVLVATD LAGRGIDVPD VSLVVNFNMA TSIESYTHRI GRTGRAGKSG
     VAITFLGNED ADVMYDLKQM LIKSPISRVP DELRKHEAAQ QKPTRGFSKK NDESSAFGGK
     GGW