ID   CWC2_LEPMC              Reviewed;         421 AA.
AC   Q6T412;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-SEP-2021, entry version 60.
DE   RecName: Full=Pre-mRNA-splicing factor CWC2;
GN   Name=CWC2;
OS   Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=5022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14749893; DOI=10.1007/s00294-004-0488-6;
RA   Gardiner D.M., Howlett B.J.;
RT   "Negative selection using thymidine kinase increases the efficiency of
RT   recovery of transformants with targeted genes in the filamentous fungus
RT   Leptosphaeria maculans.";
RL   Curr. Genet. 45:249-255(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; AY437641; AAR99468.1; -; Genomic_DNA.
DR   GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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   RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..421
FT                   /note="Pre-mRNA-splicing factor CWC2"
FT                   /id="PRO_0000081547"
FT   DOMAIN          189..263
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         126..153
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  46189 MW;  EE7D1FA88E010B94 CRC64;
     MTEVQPPPAQ STVATADTPS LAPDTTLETS TSTELAPITT EQTIITTNAE GKKVKKIIRR
     KRRPARPQVD PATFKTDTPA PTGTSFNIWY NKWSGGDRED KYLSQTAAQG RCNVARDSGY
     TKADKTPGSY FCLFFARGIC PKGVDCEYLH RLPTVTDIFP SNIDCFGRDK HSDYRDDMGG
     VGSFQRQNRT LYIGRIHVTD DIEEIVARHF QEWGQIERTR VLTARGVAFV TYMNEANSQF
     AKEAMAHQSL DHNEILNVRW ATVDPNPQAA KREAHRIEEQ AAEAIRKALP AAYVAELEGR
     DPEAKKRRKI EGSFGLQGYE APDDVWYAKE KAEWEAAKEI EAAGGAAXPR QMIESGEDAH
     AHEADCAAMQ VAPSGQHSQG NGIFSTSTLA ALRGYTAAPA KPKVAPVAGP LVGYGSDDDS
     D