ID   CWC24_SCHPO             Reviewed;         533 AA.
AC   Q9P6R8;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Pre-mRNA-splicing factor cwf24;
DE   AltName: Full=Complexed with cdc5 protein 24;
GN   Name=cwf24; ORFNames=SPBC13E7.02;
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 [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   [2]
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.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CWC24 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB89877.1; -; Genomic_DNA.
DR   RefSeq; NP_596257.1; NM_001022177.2.
DR   AlphaFoldDB; Q9P6R8; -.
DR   SMR; Q9P6R8; -.
DR   BioGRID; 276719; 18.
DR   IntAct; Q9P6R8; 1.
DR   STRING; 4896.SPBC13E7.02.1; -.
DR   iPTMnet; Q9P6R8; -.
DR   MaxQB; Q9P6R8; -.
DR   PaxDb; Q9P6R8; -.
DR   PRIDE; Q9P6R8; -.
DR   EnsemblFungi; SPBC13E7.02.1; SPBC13E7.02.1:pep; SPBC13E7.02.
DR   GeneID; 2540186; -.
DR   KEGG; spo:SPBC13E7.02; -.
DR   PomBase; SPBC13E7.02; cwf24.
DR   VEuPathDB; FungiDB:SPBC13E7.02; -.
DR   eggNOG; KOG1813; Eukaryota.
DR   eggNOG; KOG3138; Eukaryota.
DR   HOGENOM; CLU_572605_0_0_1; -.
DR   InParanoid; Q9P6R8; -.
DR   OMA; TCKFLHM; -.
DR   PRO; PR:Q9P6R8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; ISM:PomBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; TAS:PomBase.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0034247; P:snoRNA splicing; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR039971; CWC24-like.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12930; PTHR12930; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..533
FT                   /note="Pre-mRNA-splicing factor cwf24"
FT                   /id="PRO_0000055892"
FT   DOMAIN          379..524
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ZN_FING         184..212
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         254..292
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  60708 MW;  2ED7BD9ECE7BF103 CRC64;
     MEQKNLNINQ ASGSKINTEL AVPIFQSRRR HRPRQGLKRK KGFKRDDDSG GSSESSNEDM
     RDNIPIVSGR KKTVRLNRLQ RESEQFENSA LKDINVEYQS NLSATGESVN TTTVSAINED
     TREVILGRPS PKLANQSTLP TELFQSQNDY SRFLPKRKDF EKKSQVGPVL SSNASTVRMN
     TIIDYQPDVC KDYKLTGYCG YGDTCKFLHM REDYKAGWQL DREWDSVQEK YKKGAKLEEG
     MVKNEKKEDI PFVCLICKKD YRSPIATTCG HHFCEQCAIT RYRKTPTCIQ CGADTKGLFS
     VDKNFDRLLK NRKSKNDEAV KQKVGGFESN NSATTEVSER KDREASFQGF ADTLAKPNTS
     AQQKMPSLGD NSNTIISKYF IREITESNIV HFKRLVRVVL EASYSDKFYR LVLKNPDYAR
     IATFEDKFVG AISSLVAEDN SLYVTVLCVL APYRCLGIGS LLIDHVKKTA INNNIDRISL
     HVQTTNESVI KWYTAHGFKI VKQINDFYRR LENKSAFYMV CPLSAHNNII SNH