ID   CWC2_KLULA              Reviewed;         337 AA.
AC   Q6CT50;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Pre-mRNA-splicing factor CWC2;
GN   Name=CWC2; OrderedLocusNames=KLLA0C15411g;
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: 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; CR382123; CAH01740.1; -; Genomic_DNA.
DR   RefSeq; XP_452889.1; XM_452889.1.
DR   AlphaFoldDB; Q6CT50; -.
DR   SMR; Q6CT50; -.
DR   STRING; 28985.XP_452889.1; -.
DR   EnsemblFungi; CAH01740; CAH01740; KLLA0_C15411g.
DR   GeneID; 2892477; -.
DR   KEGG; kla:KLLA0_C15411g; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_043308_0_0_1; -.
DR   InParanoid; Q6CT50; -.
DR   OMA; WYNKWSQ; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IEA:EnsemblFungi.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IEA:EnsemblFungi.
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   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039173; Cwc2.
DR   InterPro; IPR039171; Cwc2/Slt11.
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; PF16131; Torus; 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..337
FT                   /note="Pre-mRNA-splicing factor CWC2"
FT                   /id="PRO_0000081546"
FT   DOMAIN          136..229
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         68..95
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  38130 MW;  7EA51409C28C83D9 CRC64;
     MTGDWKNRPA RVQLQESDLP SSVPPQTGLA FNVWYNKWSQ GQSGSTRFVT PYSLDPENDS
     GITKGDKEGR IHFCLYFAKG MCCLGKNCRY LHHIPEPDDF ARLALHSSAL DCFGREKFAD
     YRDDMGGVGS FKKPNRVLYV GGITGALNNK TLKPHQIENR VKYKFGKLGE LDSVRYVESK
     NCAFVKFKLQ CNSEFTKEAM GNQTLLIPTD KEWDLRKEGT GLLVKWANED PNPAVRKREL
     EEQTQETLKA IKQLVASTEG TVNQKRKVEE INEVRDSQAN SRERFSIREN AIIDKTILDK
     LKQRKVTITN TNVAANITVS KPSSVLPLVT QYSSDED