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CWC2_CANAL
ID   CWC2_CANAL              Reviewed;         363 AA.
AC   Q59W50; A0A1D8PF37;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Pre-mRNA-splicing factor CWC2;
GN   Name=CWC2; OrderedLocusNames=CAALFM_C111280WA;
GN   ORFNames=CaO19.674, CaO19.8291;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26753.1; -; Genomic_DNA.
DR   RefSeq; XP_713807.1; XM_708714.1.
DR   AlphaFoldDB; Q59W50; -.
DR   SMR; Q59W50; -.
DR   STRING; 237561.Q59W50; -.
DR   PRIDE; Q59W50; -.
DR   GeneID; 3644554; -.
DR   KEGG; cal:CAALFM_C111280WA; -.
DR   CGD; CAL0000184865; orf19.8291.
DR   VEuPathDB; FungiDB:C1_11280W_A; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_043308_0_1_1; -.
DR   InParanoid; Q59W50; -.
DR   OMA; WYNKWSQ; -.
DR   OrthoDB; 877856at2759; -.
DR   PRO; PR:Q59W50; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
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..363
FT                   /note="Pre-mRNA-splicing factor CWC2"
FT                   /id="PRO_0000081541"
FT   DOMAIN          141..217
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         78..105
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          246..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..286
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  41272 MW;  4AFFBB5543523293 CRC64;
     MSRKVSISSL TLSEPMTKPA RVQVNPEDID DLDKTQQVNN HQYNIWYSKS LSDANNKSTT
     KSKYRVRIST DQGFTKANKN THICLFFSRG CCYLGSKCQY FHRLPKESDN FKPTQDCFGR
     DKTANYRDDM DGVGSLNKVN CTLYVGGIHI KPNTEQLLVK NFQEFGTVEK VRVLQGKGCA
     FVTMKTENQA QFAKEAMQSQ SLVEGSNEVL YVRWANEDKN PAAQKQEKKR QQELAYDTVK
     QLLEQESNKK PRLENGAVNR IETINIDDES EDEGAVEDDE ADDDIEETRV NSLSAGVKKN
     VSTHQANGTP ESSSTSDEND HNTILRNSLL KDISRLKKKM VYKREEPYLT NLLVDYSSDE
     DDD
 
 
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