CWC2_CRYNJ
ID CWC2_CRYNJ Reviewed; 342 AA.
AC P0CR14; Q55N26; Q5KBF5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Pre-mRNA-splicing factor CWC2;
GN Name=CWC2; OrderedLocusNames=CNI02720;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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}.
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DR EMBL; AE017349; AAW45373.1; -; Genomic_DNA.
DR RefSeq; XP_572680.1; XM_572680.1.
DR AlphaFoldDB; P0CR14; -.
DR SMR; P0CR14; -.
DR STRING; 5207.AAW45373; -.
DR PaxDb; P0CR14; -.
DR EnsemblFungi; AAW45373; AAW45373; CNI02720.
DR VEuPathDB; FungiDB:CNI02720; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_043308_1_1_1; -.
DR InParanoid; P0CR14; -.
DR OMA; WYNKWSQ; -.
DR OrthoDB; 877856at2759; -.
DR Proteomes; UP000002149; Chromosome 9.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IEA:EnsemblFungi.
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 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 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..342
FT /note="Pre-mRNA-splicing factor CWC2"
FT /id="PRO_0000081543"
FT DOMAIN 141..218
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 77..104
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 38515 MW; 4AEA776D91D828B7 CRC64;
MSSDNTVAPK RKLKPARKQV ASDEVDKSQG YQAGREYNIW YNKWAGGDRE DALASKVHSQ
TRCIISRDAG YTRADATGNK YCCLFFARGC CPYGYECQYL HRLPLPSHQL PDNSRDCFGR
EKHADYRDDM GGVGSFNRQN RTLYIGKIQE SPDKKQMTET LLRHFGEWGK IVKYNILFGR
GVAFVTYETD HQASFAKEAM ANQSMDGDEI LNVRWATEDP NPGEKVAEEK RIEEIGQKAI
AGMLDENLVE ATQAVRALED GDVEDFYHIE TSKPEEEEEN RPAKKGKSEG GFFNADALDN
IKFYAELAKK QAEEEKEKAR KVPAKQVGMS LLGGYGSGDE SD
