ID   CEF1_SCHPO              Reviewed;         757 AA.
AC   P39964;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Pre-mRNA-splicing factor cdc5;
DE   AltName: Full=Cell division control protein 5;
GN   Name=cdc5; ORFNames=SPAC644.12;
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 [MRNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8313892; DOI=10.1002/j.1460-2075.1994.tb06282.x;
RA   Ohi R., McCollum D., Hirani B., den Haese G.J., Zhang X., Burke J.D.,
RA   Turner K., Gould K.L.;
RT   "The Schizosaccharomyces pombe cdc5+ gene encodes an essential protein with
RT   homology to c-Myb.";
RL   EMBO J. 13:471-483(1994).
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, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE 40S
RP   CDC5-ASSOCIATED COMPLEX.
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   [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 mRNA splicing and cell cycle control.
CC       {ECO:0000269|PubMed:10409726, ECO:0000269|PubMed:8313892}.
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:10409726,
CC       ECO:0000269|PubMed:11884590}.
CC   -!- INTERACTION:
CC       P39964; O94316: cwf10; NbExp=5; IntAct=EBI-538771, EBI-538866;
CC       P39964; O94508: cwf11; NbExp=3; IntAct=EBI-538771, EBI-539118;
CC       P39964; O74370: cwf12; NbExp=3; IntAct=EBI-538771, EBI-538882;
CC       P39964; O94620: cwf17; NbExp=3; IntAct=EBI-538771, EBI-539124;
CC       P39964; P87126: cwf2; NbExp=6; IntAct=EBI-538771, EBI-538799;
CC       P39964; Q9P7R9: cwf3; NbExp=7; IntAct=EBI-538771, EBI-538809;
CC       P39964; P87312: cwf4; NbExp=7; IntAct=EBI-538771, EBI-538818;
CC       P39964; O59800: cwf5; NbExp=4; IntAct=EBI-538771, EBI-538826;
CC       P39964; Q9USV3: cwf7; NbExp=4; IntAct=EBI-538771, EBI-538841;
CC       P39964; Q09882: prp45; NbExp=3; IntAct=EBI-538771, EBI-457758;
CC       P39964; O13615: prp5; NbExp=7; IntAct=EBI-538771, EBI-538787;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC       ECO:0000269|PubMed:10409726}.
CC   -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR   EMBL; L19525; AAA17515.1; -; mRNA.
DR   EMBL; CU329670; CAB90139.1; -; Genomic_DNA.
DR   PIR; S41712; S41712.
DR   RefSeq; NP_593880.1; NM_001019310.2.
DR   PDB; 3JB9; EM; 3.60 A; W=1-236, W=652-757.
DR   PDBsum; 3JB9; -.
DR   AlphaFoldDB; P39964; -.
DR   BMRB; P39964; -.
DR   SMR; P39964; -.
DR   BioGRID; 279998; 89.
DR   DIP; DIP-34817N; -.
DR   IntAct; P39964; 51.
DR   STRING; 4896.SPAC644.12.1; -.
DR   iPTMnet; P39964; -.
DR   MaxQB; P39964; -.
DR   PaxDb; P39964; -.
DR   PRIDE; P39964; -.
DR   EnsemblFungi; SPAC644.12.1; SPAC644.12.1:pep; SPAC644.12.
DR   GeneID; 2543583; -.
DR   KEGG; spo:SPAC644.12; -.
DR   PomBase; SPAC644.12; cdc5.
DR   VEuPathDB; FungiDB:SPAC644.12; -.
DR   eggNOG; KOG0050; Eukaryota.
DR   HOGENOM; CLU_009082_0_0_1; -.
DR   InParanoid; P39964; -.
DR   OMA; PFRTQRE; -.
DR   PhylomeDB; P39964; -.
DR   PRO; PR:P39964; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA: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:0003677; F:DNA binding; IDA:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR021786; Cdc5p/Cef1_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   Pfam; PF11831; Myb_Cef; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51294; HTH_MYB; 2.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Repeat; Spliceosome.
FT   CHAIN           1..757
FT                   /note="Pre-mRNA-splicing factor cdc5"
FT                   /id="PRO_0000197104"
FT   DOMAIN          1..56
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          57..106
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        29..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        80..102
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          271..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  86844 MW;  9FCA639A2F9A9E84 CRC64;
     MVVLKGGAWK NTEDEILKAA VSKYGKNQWA RISSLLVRKT PKQCKARWYE WIDPSIKKTE
     WSREEDEKLL HLAKLLPTQW RTIAPIVGRT ATQCLERYQK LLDDLEAKEN EQLGLISGEG
     AEAAAPVNDP NSRLRFGEAE PNLETLPALP DAIDMDEDEK EMLSEARARL ANTQGKKAKR
     KDREKQLELT RRLSHLQKRR ELKAAGINIK LFRRKKNEMD YNASIPFEKK PAIGFYDTSE
     EDRQNFREKR EADQKIIENG IRNNEMESEG RKFGHFEKPK PIDRVKKPNK DAQEEKMRRL
     AEAEQMSKRR KLNLPSPTVS QDELDKVVKL GFAGDRARAM TDTTPDANYS TNLLGKYTQI
     ERATPLRTPI SGELEGREDS VTIEVRNQLM RNREQSSLLG QESIPLQPGG TGYTGVTPSH
     AANGSALAAP QATPFRTPRD TFSINAAAER AGRLASEREN KIRLKALREL LAKLPKPKND
     YELMEPRFAD ETDVEATVGV LEEDATDRER RIQERIAEKE RLAKARRSQV IQRDLIRPSV
     TQPEKWKRSL ENEDPTANVL LKEMIALISS DAINYPFGNS KVKGTANKVP DLSNEEIERC
     RLLLKKEIGQ LESDDYIQFE KEFLETYSAL HNTSSLLPGL VIYEEDDEDV EAAEKFYTND
     IQRDLAKKAL ECNKLENRVY DLVRSSYEQR NFLIKKISHA WKALQTERKN LTCYEFLYNQ
     ERLALPNRLE AAEIELSKMQ QIEAYAQQDY ARVTGQN