YJU2_SCHPO
ID YJU2_SCHPO Reviewed; 270 AA.
AC Q9P7C5; Q9UT15;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Splicing factor YJU2 {ECO:0000255|HAMAP-Rule:MF_03226};
DE AltName: Full=Complexed with cdc5 protein 16;
DE AltName: Full=Pre-mRNA-splicing factor cwf16;
GN Name=cwf16; ORFNames=SPAC9.13c, SPAPJ735.01c;
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: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA. Plays a role in stabilizing the structure of the
CC spliceosome catalytic core and docking of the branch helix into the
CC active site, producing 5'-exon and lariat intron-3'-intermediates.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SUBUNIT: Component of the spliceosome (PubMed:11884590). Present in the
CC activated B complex, the catalytically activated B* complex which
CC catalyzes the branching, the catalytic step 1 C complex catalyzing the
CC exon ligation, and the postcatalytic P complex containing the ligated
CC exons (mRNA) and the excised lariat intron (By similarity). Belongs to
CC the 40S cdc5-associated complex (or cwf complex), a spliceosome sub-
CC complex reminiscent of a late-stage spliceosome composed of the U2, U5
CC and U6 snRNAs and at least brr2, cdc5, cwf2/prp3, cwf3/syf1, cwf4/syf3,
CC cwf5/ecm2, spp42/cwf6, cwf7/spf27, cwf8, cwf9, cwf10, cwf11, cwf12,
CC prp45/cwf13, cwf14, cwf15, cwf16, cwf17, cwf18, cwf19, cwf20, cwf21,
CC cwf22, cwf23, cwf24, cwf25, cwf26, cyp7/cwf27, cwf28, cwf29/ist3, lea1,
CC msl1, prp5/cwf1, prp10, prp12/sap130, prp17, prp22, sap61, sap62,
CC sap114, sap145, slu7, smb1, smd1, smd3, smf1, smg1 and syf2
CC (PubMed:11884590). {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
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DR EMBL; CU329670; CAB57431.1; -; Genomic_DNA.
DR PIR; T39198; T39198.
DR RefSeq; XP_001713052.1; XM_001713000.2.
DR AlphaFoldDB; Q9P7C5; -.
DR SMR; Q9P7C5; -.
DR BioGRID; 280619; 35.
DR IntAct; Q9P7C5; 3.
DR STRING; 4896.SPAC9.13c.1; -.
DR iPTMnet; Q9P7C5; -.
DR MaxQB; Q9P7C5; -.
DR PaxDb; Q9P7C5; -.
DR PRIDE; Q9P7C5; -.
DR EnsemblFungi; SPAC9.13c.1; SPAC9.13c.1:pep; SPAC9.13c.
DR PomBase; SPAC9.13c; cwf16.
DR VEuPathDB; FungiDB:SPAC9.13c; -.
DR eggNOG; KOG2989; Eukaryota.
DR HOGENOM; CLU_053603_1_1_1; -.
DR InParanoid; Q9P7C5; -.
DR OMA; LMTVRLM; -.
DR PhylomeDB; Q9P7C5; -.
DR PRO; PR:Q9P7C5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA: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:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IEA:UniProtKB-UniRule.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IC:PomBase.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR12111; PTHR12111; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome; Zinc.
FT CHAIN 1..270
FT /note="Splicing factor YJU2"
FT /id="PRO_0000079612"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
SQ SEQUENCE 270 AA; 31653 MW; 3A403699FCC655CE CRC64;
MSERKVLNKY IPPDYDPSIR PPKKKKKFQG PNGGKLTVRL MTPFSMRCHT CGEYIYKGKK
FNARKEKTGE KYFSIDILRF YIRCTRCAAE ITFITDPKHA DYAAESGASR NYEPWHEKRL
QEYEENELAE RNDIPEEDEM EKLEQKTLDT KRQMQISDAL DELREKSARR SRVNIDDAIA
LLKEDAYGSI EEEESKKRKF EEEEIDREAK SLFSSQDGEI IRRLNAETTV EKELPKPIDL
VSEKLATSNI PNFQPPKYAK RKMEKKKVLV
