ID   SLT11_SCHPO             Reviewed;         354 AA.
AC   O59800; Q9USC0;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 163.
DE   RecName: Full=Pre-mRNA-splicing factor cwf5;
DE   AltName: Full=Complexed with cdc5 protein 5;
GN   Name=cwf5; Synonyms=ecm2; ORFNames=SPCC550.02c;
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 211-227 AND
RP   258-278.
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 212-328, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
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: Facilitates the cooperative formation of U2/U6 helix II in
CC       association with stem II in the spliceosome. Binds to RNA (By
CC       similarity). Involved in pre-mRNA splicing. {ECO:0000250}.
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       O59800; P39964: cdc5; NbExp=4; IntAct=EBI-538826, EBI-538771;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the RRM SLT11 family. {ECO:0000305}.
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DR   EMBL; AF254352; AAF67751.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA19106.1; -; Genomic_DNA.
DR   EMBL; AB027880; BAA87184.1; -; Genomic_DNA.
DR   PIR; T41377; T41377.
DR   RefSeq; NP_588094.1; NM_001023085.1.
DR   PDB; 3JB9; EM; 3.60 A; a=1-285.
DR   PDBsum; 3JB9; -.
DR   AlphaFoldDB; O59800; -.
DR   SMR; O59800; -.
DR   BioGRID; 275548; 34.
DR   IntAct; O59800; 6.
DR   STRING; 4896.SPCC550.02c.1; -.
DR   MaxQB; O59800; -.
DR   PaxDb; O59800; -.
DR   EnsemblFungi; SPCC550.02c.1; SPCC550.02c.1:pep; SPCC550.02c.
DR   GeneID; 2538974; -.
DR   KEGG; spo:SPCC550.02c; -.
DR   PomBase; SPCC550.02c; cwf5.
DR   VEuPathDB; FungiDB:SPCC550.02c; -.
DR   eggNOG; KOG0153; Eukaryota.
DR   HOGENOM; CLU_027112_0_0_1; -.
DR   InParanoid; O59800; -.
DR   OMA; PYFRKGR; -.
DR   PhylomeDB; O59800; -.
DR   PRO; PR:O59800; -.
DR   Proteomes; UP000002485; Chromosome III.
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:0036002; F:pre-mRNA binding; IBA:GO_Central.
DR   GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IC:PomBase.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039171; Cwc2/Slt11.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR14089; PTHR14089; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing;
KW   Nucleus; Reference proteome; RNA-binding; Spliceosome.
FT   CHAIN           1..354
FT                   /note="Pre-mRNA-splicing factor cwf5"
FT                   /id="PRO_0000081553"
FT   DOMAIN          212..286
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          308..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  39576 MW;  5283C11C4BD504AA CRC64;
     MSHGPKGDIN KQEWEDVEFP SICERCLGDN SYVRMTKEPL GQECKICSKP CTIFRWIKER
     GQKPGKTQIC VGCARYKNCC QSCMLDLQFG LPIALRDAAL KLVESGPTND INREFFAQNQ
     QRLLSNGETA YDSQEASAAA RNLVKKVEKR ELHSRPPKRK LDDVESKQIL KEARASDASL
     NAERPLFPVK KIINGNVSLS INMEPPKDKK IASLFLIGVE DELADYKIRK HFEQYGPLKS
     VVCSHRAKCA FVNFKTRSSA EIAAAASPDG NVVIEGFRLK VQWGKPRSLG GPEGEVRNAK
     LADLVMRGSS HGNKTSQKST IKNIENEDHE NTKSPAVAIP IDPNQPRYRS QIPR