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Database: UniProt
Entry: Q2UH00
LinkDB: Q2UH00
Original site: Q2UH00 
ID   PRP28_ASPOR             Reviewed;         803 AA.
AC   Q2UH00;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   31-JUL-2019, entry version 81.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE            EC=3.6.4.13;
GN   Name=prp28; ORFNames=AO090023000644;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing.
CC       May destabilize the U1/5'-splice site duplex to permit an
CC       effective competition for the 5'-splice site by the U6 snRNA,
CC       resulting in the switch between U1 and U6 at the 5'-splice site.
CC       May also act to unwind the U4/U6 base-pairing interaction in the
CC       U4/U6/U5 snRNP, facilitating the first covalent step of splicing
CC       (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
CC       {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
DR   EMBL; AP007157; BAE59165.1; -; Genomic_DNA.
DR   RefSeq; XP_001821167.1; XM_001821115.2.
DR   SMR; Q2UH00; -.
DR   PRIDE; Q2UH00; -.
DR   EnsemblFungi; BAE59165; BAE59165; AO090023000644.
DR   GeneID; 5993169; -.
DR   KEGG; aor:AO090023000644; -.
DR   HOGENOM; HOG000268796; -.
DR   KO; K12858; -.
DR   OMA; TEKKFNF; -.
DR   Proteomes; UP000006564; Chromosome 3.
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: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   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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN         1    803       Pre-mRNA-splicing ATP-dependent RNA
FT                                helicase prp28.
FT                                /FTId=PRO_0000232370.
FT   DOMAIN      398    603       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      614    777       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     411    418       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       367    395       Q motif.
FT   MOTIF       526    529       DEAD box.
FT   COMPBIAS     10     64       Pro-rich.
SQ   SEQUENCE   803 AA;  89340 MW;  39025E249EC94AC7 CRC64;
     MDDIVMNGSP EVPPPQPPPE PVERPPTPPP PPPEESVAPP PPPEVVAPPP PPEDLPPAPP
     PPEPKKKKVG WGAKKPAATP LSVEELVRKK READAAAARP KFLSRAERER IALEKRAKEV
     EAERRLKASN GVDRSATQSP SVSSEVNHSD GRTIPTGPRA MRSSDTPTAP AAMRNSHSHN
     KNRDLSPPPP PKSMSFGLAS SKGDKRPVDD DEVAAQVALV KQRYMGADQT STFSAKKKRK
     RTTDRKFNFE WNAEEDTSGD YNPLYQHRHE ANFFGRGRLA GFGDDVADNV AKKYARALED
     RDHEAGGIRA REILEMERRR REESTRNQLD KHWSEKKLEH MRERDWRIFK EDFNISTKGG
     SVPNPMRSWD ESGLPKRLME LVNKVGYKEP TPIQRAAIPI AMQSRDLIGV AVTGSGKTAS
     FLLPLLVYIA ELPRIDEFEW RKNDGPYAIV LAPTRELAQQ IEIEAKKFTE PLGFNVVSIV
     GGHSFEEQAY SLRNGAEIII ATPGRLVDCI ERRMLVLSQC CYVIMDEADR MIDLGFEEPV
     NKILDALPVS NEKPDSEEAE NSMAMSQHIG TKDRYRQTMM YTATMPTAVE RIARKYLRRP
     AIVTIGSAGE AVDTVEQRVE FIAGEDKRKK RLGDILSSGE FRPPIIVFVN IKRNCDAIAR
     EIKQWGFSSV TLHGSKTQEQ REAALASVRN GQTDVLVATD LAGRGIDVPD VSLVINFNMA
     TTIESYTHRI GRTGRAGKSG VAITFLGNED TDVMYDLKQM IMKSSISRLP EELRKHEAAQ
     SKPTRGFAKK NDDNSAFGSK GGW
//
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