PRP28_MAGO7
ID PRP28_MAGO7 Reviewed; 674 AA.
AC A4RK80; G4MTW0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE EC=3.6.4.13;
GN Name=PRP28; ORFNames=MGG_01583;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001232; EHA54754.1; -; Genomic_DNA.
DR RefSeq; XP_003714561.1; XM_003714513.1.
DR AlphaFoldDB; A4RK80; -.
DR SMR; A4RK80; -.
DR STRING; 318829.MGG_01583T0; -.
DR PRIDE; A4RK80; -.
DR EnsemblFungi; MGG_01583T0; MGG_01583T0; MGG_01583.
DR GeneID; 2679297; -.
DR KEGG; mgr:MGG_01583; -.
DR VEuPathDB; FungiDB:MGG_01583; -.
DR eggNOG; KOG0333; Eukaryota.
DR HOGENOM; CLU_003041_11_3_1; -.
DR InParanoid; A4RK80; -.
DR OMA; KKFNFEW; -.
DR OrthoDB; 820037at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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 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 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; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..674
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT /id="PRO_0000294635"
FT DOMAIN 288..492
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 520..666
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 14..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 257..285
FT /note="Q motif"
FT MOTIF 415..418
FT /note="DEAD box"
FT COMPBIAS 14..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 674 AA; 76093 MW; 5C388AE24D0A98FB CRC64;
MAPLDLEEIL KKHKAAKAEA AKPRFIPRGQ RKKMEEEKKL KVEEEQKRQQ EELQKTRSEL
QKAREELAGL QRVRRQEQSR SRESDHSVPT GPRAMRSYDD DSFNGNGNGS NSNRNNNNNQ
RDRQDASTKT NGSRTAEEVQ EEKKYLERYT GPPAKVSTFS ANKKRRRTTD QKFNFDWDPK
DDTSQPWRYE ETGAHERSAN GATEQVRRKK ATRDYNDPRL VPWQDKELSQ MTTRDWRLFK
VNLEIVTKGN NIPNPMRFWE ESNLPHVLKD TIKQVGYTEP TPVQRAAIPI ALQCRDLIGI
SKTGSGKTAA FVLPMLSYIE PLPPLNEVTK TEGPYALILA PTRELATQIQ AEVIKFATRM
GFTVVCLIGN KRTIEEDAFA LRNGAEIIVA TPGRLVDCLE RHLLVLSQCS YVVLDEADRM
VDGGFEDSIH KILAALPPSN GKPDDRDAED PNIMSKFLTP NLRYRQTVMY SATMPPSVER
IAKNYLKHPA MVTIGTIGEA VDTVEQQAMW VVSEDERRNK LRAMLNTYGT GKLVIVFVNT
KSNCDAVAKD LKSSSFSAVT LHGNKTQDQR EAALQSFRDG RTNVLVATDV AARGLDIPDV
SLVINFNMAG TIEVYTHRIG RTGRAGKEGM AITFCGPEDH GVLYHLKQIM SKSQMSKVPP
WLKDHPEAQS KPTF
