CWC2_MAGO7
ID CWC2_MAGO7 Reviewed; 394 AA.
AC Q51TF7; A4QSC1; G4ML32;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Pre-mRNA-splicing factor CWC2;
GN Name=CWC2; ORFNames=MGG_08641;
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: Involved in the first step of pre-mRNA splicing. Required for
CC cell growth and cell cycle control. Plays a role in the levels of the
CC U1, U4, U5 and U6 snRNAs and the maintenance of the U4/U6 snRNA
CC complex. May provide the link between the 'nineteen complex' NTC
CC spliceosome protein complex and the spliceosome through the U6 snRNA.
CC Associates predominantly with U6 snRNAs in assembled active
CC spliceosomes. Binds directly to the internal stem-loop (ISL) domain of
CC the U6 snRNA and to the pre-mRNA intron near the 5' splice site during
CC the activation and catalytic phases of the spliceosome cycle (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The C-terminal RRM domain and the zinc finger motif are
CC necessary for RNA-binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM CWC2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001231; EHA58459.1; -; Genomic_DNA.
DR RefSeq; XP_003711071.1; XM_003711023.1.
DR AlphaFoldDB; Q51TF7; -.
DR SMR; Q51TF7; -.
DR STRING; 318829.MGG_08641T0; -.
DR EnsemblFungi; MGG_08641T0; MGG_08641T0; MGG_08641.
DR GeneID; 2678873; -.
DR KEGG; mgr:MGG_08641; -.
DR VEuPathDB; FungiDB:MGG_08641; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_043308_1_0_1; -.
DR InParanoid; Q51TF7; -.
DR OMA; ARHFQEW; -.
DR OrthoDB; 877856at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IEA:EnsemblFungi.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR CDD; cd12360; RRM_cwf2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039173; Cwc2.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034181; Cwc2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR032297; Torus.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR PANTHER; PTHR14089:SF2; PTHR14089:SF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16131; Torus; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Cell cycle; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..394
FT /note="Pre-mRNA-splicing factor CWC2"
FT /id="PRO_0000081548"
FT DOMAIN 167..241
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 104..131
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 43256 MW; DB6537C336686420 CRC64;
MSDTEQPQAA EGTELVPTSN GPVVPEGQKK VKKIIRVKKK RPARPQIDPA LVKSEPPPQT
GTTFNIWYNK WSGGDREDKY TSQTAAKGRC NVAKDSGYTK ADQTTGSYFC LFFARGVCPK
GQDCEYLHRL PTLHDLYSPN VDCFGRDRFS DYRDDMGGVG SFMRQNRTVY VGRIHVTDDI
EEVVARHFAE WGQVERIRVL NQRGVAFITY TNEANAQFAK EAMAHQSLDH NEILNVRWAT
ADPNPMAQAR EARRVEEQAA EAVRRALPAE FVAEIEGRDP EARKRRKMES SYGLDGYEAP
DEVHFARGAQ AVNPVGRRGF EDQLMLEGGG EEVSAREALF GAEGSGSGDG DAGGIFSSST
LAALNSAQVK VSAQPKQAAA TGPLVAYGSD SEDD