PRP28_KLULA
ID PRP28_KLULA Reviewed; 539 AA.
AC Q6CT49;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE EC=3.6.4.13;
GN Name=PRP28; OrderedLocusNames=KLLA0C15433g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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. 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; CR382123; CAH01741.1; -; Genomic_DNA.
DR RefSeq; XP_452890.1; XM_452890.1.
DR AlphaFoldDB; Q6CT49; -.
DR SMR; Q6CT49; -.
DR STRING; 28985.XP_452890.1; -.
DR PRIDE; Q6CT49; -.
DR EnsemblFungi; CAH01741; CAH01741; KLLA0_C15433g.
DR GeneID; 2892649; -.
DR KEGG; kla:KLLA0_C15433g; -.
DR eggNOG; KOG0333; Eukaryota.
DR HOGENOM; CLU_003041_1_5_1; -.
DR InParanoid; Q6CT49; -.
DR OMA; IDCLENH; -.
DR Proteomes; UP000000598; Chromosome C.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000384; F:first spliceosomal transesterification activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IEA:EnsemblFungi.
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 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..539
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT /id="PRO_0000227964"
FT DOMAIN 169..351
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 361..525
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 136..166
FT /note="Q motif"
FT MOTIF 297..300
FT /note="DEAD box"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 539 AA; 61249 MW; 7F97DA797310BD0E CRC64;
MLRPVSIDDL ISDTVPAKKP RFLIKKRTFP QPEEEEASKA LSHTVIKRKD NYRNLDEDEL
YEEQVSNEPD DLLFLARKSA DLLKKRQNED ESIVDNYLGK HWSEKKYEEM STRDWRILSE
DFNISSKGGT VEKPLRNWHE LKLIPEDLLN IITNDLHYNE PTSIQRSTIP NVINNRDFIG
VASTGSGKTL AFLLPILIKL HGIPPLNSIT KHDGPLALVL APTRELAQQI QHEGQSITKL
WKRPCNIVSI VGGHSLEEIS ANLRDGCDIL VATPGRLLDC LDSHLLFLKQ VNTLVLDEAD
KMIDFGFEDQ LTTILAKTET ISNRQTMMFT ATFSPTIEKV ANGYLKKPSY VTVGGEESKP
KIKQIVRYVP DEEEKLKILV KDFLPNYKAP IIIFINYKRT ADWLFDKLRE ARFRATTLHG
SKSQEQREHS LSLLRNGKVD ILIATDVAGR GIDIPNVSLV VNLQFPKSFD SFVHRVGRTG
RAGKTGTALT FLTEEEDHSA MAKLFDYVKK NDFTGENYIS KEAMSKYNVD KSSYKPIII
