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SPF27_SCHPO
ID   SPF27_SCHPO             Reviewed;         187 AA.
AC   Q9USV3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Pre-mRNA-splicing factor cwf7;
DE   AltName: Full=Complexed with cdc5 protein 7;
DE   AltName: Full=Splicing factor 27;
GN   Name=cwf7; Synonyms=spf27; ORFNames=SPBC28F2.04c;
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   IDENTIFICATION IN THE 40S 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   [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   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:10409726,
CC       ECO:0000269|PubMed:11884590}.
CC   -!- INTERACTION:
CC       Q9USV3; P39964: cdc5; NbExp=4; IntAct=EBI-538841, EBI-538771;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SPF27 family. {ECO:0000305}.
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DR   EMBL; AF254798; AAF67744.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB57933.1; -; Genomic_DNA.
DR   PIR; T40047; T40047.
DR   RefSeq; NP_595665.1; NM_001021560.2.
DR   PDB; 3JB9; EM; 3.60 A; i=1-187.
DR   PDBsum; 3JB9; -.
DR   AlphaFoldDB; Q9USV3; -.
DR   SMR; Q9USV3; -.
DR   BioGRID; 277111; 29.
DR   IntAct; Q9USV3; 5.
DR   STRING; 4896.SPBC28F2.04c.1; -.
DR   MaxQB; Q9USV3; -.
DR   PaxDb; Q9USV3; -.
DR   EnsemblFungi; SPBC28F2.04c.1; SPBC28F2.04c.1:pep; SPBC28F2.04c.
DR   GeneID; 2540585; -.
DR   KEGG; spo:SPBC28F2.04c; -.
DR   PomBase; SPBC28F2.04c; cwf7.
DR   VEuPathDB; FungiDB:SPBC28F2.04c; -.
DR   eggNOG; KOG3096; Eukaryota.
DR   HOGENOM; CLU_1435198_0_0_1; -.
DR   InParanoid; Q9USV3; -.
DR   OMA; KHGESAW; -.
DR   PhylomeDB; Q9USV3; -.
DR   PRO; PR:Q9USV3; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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:0045292; P:mRNA cis splicing, via spliceosome; IC:PomBase.
DR   InterPro; IPR008409; SPF27.
DR   PANTHER; PTHR13296; PTHR13296; 1.
DR   Pfam; PF05700; BCAS2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Spliceosome.
FT   CHAIN           1..187
FT                   /note="Pre-mRNA-splicing factor cwf7"
FT                   /id="PRO_0000079616"
SQ   SEQUENCE   187 AA;  21317 MW;  C2CE833F1036FA33 CRC64;
     MSYNISLDSL PYFESTYNEE DRSAAAQIVE EELKRSGGLL IKQEEQKKKF QSHRLSDRLE
     NAIVAAGKGE KLAAIDVQRY IQLKPPGTRE SLLQSAVVWE YQKSRNDNLY LLEKHGEKAF
     DSSLEALEVQ LELLEKELVN TKKLSQGCNR KRKHYQMEVG ARLAEAEVKF GQLLQSSIQC
     RVATLLS
 
 
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