PRP28_CANGA
ID PRP28_CANGA Reviewed; 582 AA.
AC Q6FM43;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE EC=3.6.4.13;
GN Name=PRP28; OrderedLocusNames=CAGL0K11198g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61664.1; -; Genomic_DNA.
DR RefSeq; XP_448701.1; XM_448701.1.
DR AlphaFoldDB; Q6FM43; -.
DR SMR; Q6FM43; -.
DR STRING; 5478.XP_448701.1; -.
DR EnsemblFungi; CAG61664; CAG61664; CAGL0K11198g.
DR GeneID; 2890090; -.
DR KEGG; cgr:CAGL0K11198g; -.
DR CGD; CAL0134849; CAGL0K11198g.
DR VEuPathDB; FungiDB:CAGL0K11198g; -.
DR eggNOG; KOG0333; Eukaryota.
DR HOGENOM; CLU_003041_11_4_1; -.
DR InParanoid; Q6FM43; -.
DR OMA; IDCLENH; -.
DR Proteomes; UP000002428; Chromosome K.
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..582
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT /id="PRO_0000232372"
FT DOMAIN 207..394
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 416..570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 170..199
FT /note="Q motif"
FT MOTIF 338..341
FT /note="DEAD box"
FT BINDING 220..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 582 AA; 65530 MW; 884936A79CA302D3 CRC64;
MLVLRKFRWR KWTAETLEST KMTRPIDVHQ LLKSRSAGPK YMSVEERERV VIEHSNDEVD
LGVEYAKKRN VDEVAEDSAR ESKKKSKRLD FDWDPADNTL EGYQPIVNPV ILERIRQQED
QGDDLEAQYL GKSWREKLLV EMDERDWRIM REEFNITSKG KGAVKHPLRN WSETNVIPTD
LVRALTEGMG FDEPTAIQRI TIPNAISSNK SVPRDILGIA STGSGKTLAF SIPILARLDA
LPARPVNLKT LDGPLALVLV PTRELAQQIS QEINRLLSAW ENKKNLNAVS IVGGHSMSDI
SHTLRNGCDI LIATPGRLLD VLDNHLVVLN KIQSLVLDEA DRMIDLGFED QMKSILSHLM
ADELAARQTM LFTATLSSSV ESIAKGYLKN PLHVSVGSRW DSDKPLITQV VRHTGDDDKK
LSFLKDDLIK NGLPAIIFIN YKETADWLTL RLSDRFNIVT LHGSKSQSQR ESAIQKLKSG
TANVLIATNV AARGLDIPDV ALVVNFQMSK KFDDYIHRIG RTGRAGKTGI AVTYLTGEED
PQLIKQLAKY VKDVDPNKEN DFPEECAKHF GIVSETRNRI IY
