ID   CWC2_EMENI              Reviewed;         417 AA.
AC   Q5BB35; C8VMT8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Pre-mRNA-splicing factor cwc2;
GN   Name=cwc2; ORFNames=AN2245;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000036; EAA63930.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF86452.1; -; Genomic_DNA.
DR   RefSeq; XP_659849.1; XM_654757.1.
DR   AlphaFoldDB; Q5BB35; -.
DR   SMR; Q5BB35; -.
DR   STRING; 162425.CADANIAP00008932; -.
DR   EnsemblFungi; CBF86452; CBF86452; ANIA_02245.
DR   EnsemblFungi; EAA63930; EAA63930; AN2245.2.
DR   GeneID; 2875329; -.
DR   KEGG; ani:AN2245.2; -.
DR   VEuPathDB; FungiDB:AN2245; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_043308_1_0_1; -.
DR   InParanoid; Q5BB35; -.
DR   OMA; ARHFQEW; -.
DR   OrthoDB; 877856at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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   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..417
FT                   /note="Pre-mRNA-splicing factor cwc2"
FT                   /id="PRO_0000081545"
FT   DOMAIN          197..271
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         134..161
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  46018 MW;  0904357C4CA27F7A CRC64;
     MADTAVIDTS PAAATAEPSV DTTPQDGERE EITPNGENAL VQQQSETAET GITDANSTQK
     KTKKIIRRKR RPARPQVDPA TLKSEPPPQT GTVFNIWYNK WSGGDREDKY LSKTAAPSRC
     NIARDSGYTR ADKVRGSYFC LFFARGICPK GHECEYLHRL PTLHDLFNPN VDCFGRDKHS
     DYRDDMGGVG SFMRQNRTLY VGRIHVTDDI EEVVARHFAE WGQIDRTRVL TSRGVAFVTY
     TNEANAQFAK EAMAHQSLDH NEILNVRWAT VDPNPLAQKR EARRLEEQAA EAVRRALPAE
     FVAELEGRDP EAKKRKRIEG SYGLQGYEPP DEVWFARAKE LEGTGNEHAK LEAPEQPLMI
     ESGSASAPQN QVESSGGIFS SSAVAALRGL NGGNVTTKPA PQASGPLVAY GSDDESD