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