(data stored in ACNUC6288 zone)

SWISSPROT: PRP28_DEBHA

ID   PRP28_DEBHA             Reviewed;         580 AA.
AC   Q6BLU9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE            EC=3.6.4.13;
GN   Name=PRP28; OrderedLocusNames=DEHA2F10538g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382138; CAG89165.2; -; Genomic_DNA.
DR   RefSeq; XP_460822.2; XM_460822.1.
DR   SMR; Q6BLU9; -.
DR   STRING; 4959.XP_460822.2; -.
DR   PRIDE; Q6BLU9; -.
DR   EnsemblFungi; CAG89165; CAG89165; DEHA2F10538g.
DR   GeneID; 2904336; -.
DR   KEGG; dha:DEHA2F10538g; -.
DR   HOGENOM; HOG000268796; -.
DR   InParanoid; Q6BLU9; -.
DR   KO; K12858; -.
DR   OMA; RITLMFT; -.
DR   OrthoDB; 820037at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005682; C:U5 snRNP; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000384; F:first spliceosomal transesterification activity; IEA:EnsemblFungi.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; IEA:EnsemblFungi.
DR   CDD; cd00079; HELICc; 1.
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; 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; 2.
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;
DR   PRODOM; Q6BLU9.
DR   SWISS-2DPAGE; Q6BLU9.
KW   ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN         1    580       Pre-mRNA-splicing ATP-dependent RNA
FT                                helicase PRP28.
FT                                /FTId=PRO_0000232374.
FT   DOMAIN      186    386       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      422    571       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     199    206       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       154    183       Q motif.
FT   MOTIF       318    321       DEAD box.
SQ   SEQUENCE   580 AA;  66188 MW;  E6E81BAB0692AAD4 CRC64;
     MSKRPISVEE LIGKSQSAEV ISKPKFLSKS ERQKLSLQRN QEIQDKKRQQ STVNNGAKKR
     YNNSIEDNPE PKKINKKLKK GRNFNFDWDE EEDTSNNYQP LVRYDNRTNP PDLGLSDMHW
     SEKQIDDMTT RDWRIFKEDY NITSKGGDIE NPLRCWAESK LPAKLLNILI KNLGYDSPTP
     IQRASIPLAL NGRDIVGIAE TGSGKTLAFL LPLFSYILSV DSNYLLYEHQ QESNFNKPLG
     LILAPTRELA LQITKEAKLF GDKLNLNVVT IIGGHQYEET VHSVRNGVHI VVATPGRLID
     SLERGIINLS NCYFFTMDEA DKMIDMGFEK SLQSILNYLP ASEKLETTID GKIFNIKKRI
     TLMFTATISP PIEKITKNYL MKPGYLFIGN VGEAVDNINQ QFEYFGARQS SDEILDPKKL
     DKLFSILRFH KDENRNYSII IFANFKKACE ELAYELSRKG FSDNTVIHGS KSQEARERAI
     DSFREGKDKI LIATDVAARG IDIPNVSLVV NYQMTKKFDE YIHRIGRTGR AGNKGTSCTF
     IDDGDSEVFL DLKKFLNKGK KKCPEWLLKH SSTQSQILRD
//

If you have problems or comments...

PBIL Back to PBIL home page