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 24-JAN-2024, entry version 169.
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; 284812.O59800; -.
DR iPTMnet; O59800; -.
DR MaxQB; O59800; -.
DR PaxDb; 4896-SPCC550-02c-1; -.
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; CPLRVQW; -.
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 CDD; cd12265; RRM_SLT11; 1.
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 InterPro; IPR034356; Slt11_RRM.
DR InterPro; IPR048995; STL11/RBM22-like_N.
DR PANTHER; PTHR14089; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR PANTHER; PTHR14089:SF6; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF21369; STL11_N; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 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
//
