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CWC2_ASPFU
ID   CWC2_ASPFU              Reviewed;         414 AA.
AC   Q4WU07;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Pre-mRNA-splicing factor cwc2;
GN   Name=cwc2; ORFNames=AFUA_5G06760;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000003; EAL91919.1; -; Genomic_DNA.
DR   RefSeq; XP_753957.1; XM_748864.1.
DR   AlphaFoldDB; Q4WU07; -.
DR   SMR; Q4WU07; -.
DR   STRING; 746128.CADAFUBP00005319; -.
DR   EnsemblFungi; EAL91919; EAL91919; AFUA_5G06760.
DR   GeneID; 3510730; -.
DR   KEGG; afm:AFUA_5G06760; -.
DR   VEuPathDB; FungiDB:Afu5g06760; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_043308_1_0_1; -.
DR   InParanoid; Q4WU07; -.
DR   OMA; ARHFQEW; -.
DR   OrthoDB; 877856at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
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..414
FT                   /note="Pre-mRNA-splicing factor cwc2"
FT                   /id="PRO_0000081540"
FT   DOMAIN          192..266
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         130..156
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45526 MW;  BDE86805B6D9A438 CRC64;
     MAETAVIDPP HATEPTSLPT ESADPSGPAP SDENALTQPS ESAVTATTDA DGTQKKTKKI
     IRRKRRPARP QVDPATLKSE PPPQTGTVFN IWYNKWSGGD REDKYLSKHA APSRCNIAKD
     SGYTRADKVP GSYFCLFFAR GVCPKGHECE YLHRLPTLHD LFNPNVDCFG RDKFSDYRDD
     MGGVGSFTRQ NRTLYVGRIH VTDDIEEVVS RHFAEWGQID RIRVLTSRGV AFVTYTNEAN
     AQFAKEAMAH QSLDHNEILN VRWATVDPNP LAQKREARRL EEQAAEAVRR ALPAEFVAEL
     EGRDPEARKK KKIEGSFGLE GYEAPDDVWY ARTKELEDAR KAGQLEAPEQ HLMIEPAPSS
     SSAALPSQSE DTGIFSNSTV AALRGLAGGN VTTQKAPVNS GGPLVAYGSD DDSD
 
 
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