CWC2_DEBHA
ID CWC2_DEBHA Reviewed; 339 AA.
AC Q6BLU8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Pre-mRNA-splicing factor CWC2;
GN Name=CWC2; OrderedLocusNames=DEHA2F10560g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: 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}.
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DR EMBL; CR382138; CAG89166.2; -; Genomic_DNA.
DR RefSeq; XP_460823.2; XM_460823.1.
DR AlphaFoldDB; Q6BLU8; -.
DR SMR; Q6BLU8; -.
DR STRING; 4959.XP_460823.2; -.
DR EnsemblFungi; CAG89166; CAG89166; DEHA2F10560g.
DR GeneID; 2904337; -.
DR KEGG; dha:DEHA2F10560g; -.
DR VEuPathDB; FungiDB:DEHA2F10560g; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_043308_1_0_1; -.
DR InParanoid; Q6BLU8; -.
DR OMA; WYNKWSQ; -.
DR OrthoDB; 877856at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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..339
FT /note="Pre-mRNA-splicing factor CWC2"
FT /id="PRO_0000081544"
FT DOMAIN 157..231
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 94..121
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 17..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 38544 MW; 7758EFF122C85CE3 CRC64;
MSYREPLGEY DCHIDNTRNM PPDTTIVSKS KKGKPARLQV DPESIPDDDR PPQTGNVFNI
WFLKWSGGDS STKNYTKSKF RVNIKKDSGY TKAPSNAPLC LFFARGCCYL GKKCSYYHRL
PSDTDYFIPT QDCFGRDKTS DYKDDMNGVG SFSKSNRTLY IGGLHMDDKM ENTLTKHFQE
FGSIDKIRVL HSKACAFVTF RTENEAQFAK EAMQNQSLDG NEVLNIRWAN EDPNPEAQRQ
EKRRLEEVTV NTVKNLLDSV SQTERKTKKV TVEVPDEIEE TESSSEIKAL PSSETSSGLF
NNSSLNALKQ FQSKKRKIDK PQPKENLPTM LGYSSSDEE
