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 27-MAR-2024, entry version 82.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; ARDIKHM; -.
DR OrthoDB; 5487240at2759; -.
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 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; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 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; 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
//
