ID   CWC2_SCHPO              Reviewed;         388 AA.
AC   P87126; Q9P8I7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Pre-mRNA-splicing factor cwf2;
DE   AltName: Full=Complexed with cdc5 protein 2;
DE   AltName: Full=Pre-mRNA-processing protein 3;
GN   Name=cwf2; Synonyms=prp3; ORFNames=SPAC3A12.11c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 356-369.
RX   PubMed=10409726; DOI=10.1128/mcb.19.8.5352;
RA   McDonald W.H., Ohi R., Smelkova N., Frendewey D., Gould K.L.;
RT   "Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing
RT   complex and is essential for pre-mRNA splicing.";
RL   Mol. Cell. Biol. 19:5352-5362(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=2721492; DOI=10.1002/j.1460-2075.1989.tb03409.x;
RA   Potashkin J., Li R., Frendewey D.;
RT   "Pre-mRNA splicing mutants of Schizosaccharomyces pombe.";
RL   EMBO J. 8:551-559(1989).
RN   [4]
RP   IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
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). Involved in pre-mRNA splicing. {ECO:0000250,
CC       ECO:0000269|PubMed:2721492}.
CC   -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC       spliceosome sub-complex reminiscent of a late-stage spliceosome
CC       composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC       cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC       cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC       cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC       cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC       prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC       smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC   -!- INTERACTION:
CC       P87126; P39964: cdc5; NbExp=6; IntAct=EBI-538799, EBI-538771;
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; CU329670; CAC41387.1; -; Genomic_DNA.
DR   EMBL; AF250026; AAF63625.1; -; Genomic_DNA.
DR   RefSeq; NP_593337.1; NM_001018769.2.
DR   PDB; 3JB9; EM; 3.60 A; Y=1-289.
DR   PDBsum; 3JB9; -.
DR   AlphaFoldDB; P87126; -.
DR   SMR; P87126; -.
DR   BioGRID; 278989; 102.
DR   DIP; DIP-34853N; -.
DR   IntAct; P87126; 35.
DR   STRING; 4896.SPAC3A12.11c.1; -.
DR   iPTMnet; P87126; -.
DR   MaxQB; P87126; -.
DR   PaxDb; P87126; -.
DR   PRIDE; P87126; -.
DR   EnsemblFungi; SPAC3A12.11c.1; SPAC3A12.11c.1:pep; SPAC3A12.11c.
DR   GeneID; 2542531; -.
DR   KEGG; spo:SPAC3A12.11c; -.
DR   PomBase; SPAC3A12.11c; cwf2.
DR   VEuPathDB; FungiDB:SPAC3A12.11c; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_043308_1_0_1; -.
DR   InParanoid; P87126; -.
DR   OMA; ARHFQEW; -.
DR   PhylomeDB; P87126; -.
DR   PRO; PR:P87126; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR   GO; GO:0000974; C:Prp19 complex; IDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
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; IMP:PomBase.
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   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Direct protein sequencing; Metal-binding;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW   Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..388
FT                   /note="Pre-mRNA-splicing factor cwf2"
FT                   /id="PRO_0000081549"
FT   DOMAIN          174..248
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         111..138
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          43..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  44281 MW;  5CD36A5C880077DE CRC64;
     MSENGLEQEV TVEEKNNDVT EKILVEGEKS KEYEETPRKV KIVKRKKQPA RKQIETRPEY
     EMEPEQPGQV YNLWYNKWSG GMRQDPLKSQ VKSETRCVIS RDSGYTKADK NPGSFFCLYF
     ARGMCSEGSK CEYLHRLPKD TDFFNANVDC FGREKHADYR DDMGGVGSFL RQNYTLYVGG
     ITPTDDIEEI VSRHFAEWGD IERIRVLNSR GIAFITYLNE ANAQFAKEAM AHQSLDHDEC
     LNVRWATTDP NPASQARNQR RLEERAANAV KKLLPKQFLL DLEETKNGKS GNRKRKLELE
     FGLKGYVPSD DLLYADGANS VHNQLAANEF PNKSQSEEGS NDDHKSVTTT ESQNKFVNSQ
     ILSDLQVAKQ AVHTNQSALV SYYDSDED