ID SN114_SCHPO Reviewed; 984 AA. AC O94316; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=Pre-mRNA-splicing factor cwf10; DE AltName: Full=114 kDa U5 small nuclear ribonucleoprotein component homolog; DE AltName: Full=Complexed with cdc5 protein 10; GN Name=cwf10; Synonyms=snu114, spef2; ORFNames=SPBC215.12; 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 [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 REVISION OF GENE MODEL. RX PubMed=21511999; DOI=10.1126/science.1203357; RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H., RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.; RT "Comparative functional genomics of the fission yeasts."; RL Science 332:930-936(2011). RN [3] RP IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. 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). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the fission RT yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). CC -!- FUNCTION: Component of the U5 snRNP complex required for pre-mRNA CC splicing. Binds GTP. 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 O94316; P39964: cdc5; NbExp=5; IntAct=EBI-538866, EBI-538771; CC O94316; O42975: SPBC20F10.05; NbExp=3; IntAct=EBI-538866, EBI-9003631; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus CC {ECO:0000269|PubMed:16823372}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU329671; CAA22126.2; -; Genomic_DNA. DR PIR; T39902; T39902. DR RefSeq; NP_596689.2; NM_001022612.2. DR PDB; 3JB9; EM; 3.60 A; B=1-984. DR PDBsum; 3JB9; -. DR AlphaFoldDB; O94316; -. DR SMR; O94316; -. DR BioGRID; 277234; 94. DR IntAct; O94316; 11. DR STRING; 284812.O94316; -. DR iPTMnet; O94316; -. DR MaxQB; O94316; -. DR PaxDb; 4896-SPBC215-12-1; -. DR EnsemblFungi; SPBC215.12.1; SPBC215.12.1:pep; SPBC215.12. DR GeneID; 2540711; -. DR KEGG; spo:SPBC215.12; -. DR PomBase; SPBC215.12; cwf10. DR VEuPathDB; FungiDB:SPBC215.12; -. DR eggNOG; KOG0468; Eukaryota. DR HOGENOM; CLU_002794_11_2_1; -. DR InParanoid; O94316; -. DR OMA; YIFRPIR; -. DR PRO; PR:O94316; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0005829; C:cytosol; HDA:PomBase. 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:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central. DR GO; GO:0005682; C:U5 snRNP; IDA:PomBase. DR GO; GO:0005525; F:GTP binding; ISO:PomBase. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISO:PomBase. DR CDD; cd04098; eEF2_C_snRNP; 1. DR CDD; cd04090; EF2_II_snRNP; 1. DR CDD; cd01683; EF2_IV_snRNP; 1. DR CDD; cd16264; snRNP_III; 1. DR CDD; cd04167; Snu114p; 1. DR DisProt; DP02109; -. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031950; EFTUD2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR044121; Snu114_GTP-bd. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR InterPro; IPR035655; U5-116kDa_C. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR42908:SF6; 116 KDA U5 SMALL NUCLEAR RIBONUCLEOPROTEIN COMPONENT; 1. DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF16004; EFTUD2; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; GTP-binding; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..984 FT /note="Pre-mRNA-splicing factor cwf10" FT /id="PRO_0000363370" FT DOMAIN 139..402 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 148..155 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 190..194 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 216..219 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 270..273 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 371..373 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT BINDING 148..155 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 216..220 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 270..273 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" SQ SEQUENCE 984 AA; 111306 MW; B15A139BEC1EA53E CRC64; MMEEDLYDEF GNYIGPENEE DEEELFPQAP SPTIAQVPSF EEVIPDEELE DVERAEEMAL SHLEPQNAVV LHEDKQYYPS AEEVYGSNVD IMVQEQDTQP LSQPIIEPIR HKRIAIETTN VPDTVYKKEF LFGLLTGTDD VRSFIVAGHL HHGKSALLDL LVYYTHPDTK PPKRRSLRYT DTHYLERERV MSIKSTPLTL AVSDMKGKTF AFQCIDTPGH VDFVDEVAAP MAISDGVVLV VDVIEGVMIN TTRIIKHAIL HDMPIVLVLN KVDRLILELR LPPNDAYHKL RHVIDEVNDN ICQISKDLKY RVSPELGNVC FASCDLGYCF TLSSFAKLYI DRHGGIDVDL FSKRLWGDIY FDSKTRKFAK QSLDGSGVRS FVHFILEPLY KLHTLTISDE AEKLKKHLSS FQIYLKPKDY LLDPKPLLQL ICASFFGFPV GFVNAVTRHI PSPRENAARK ASQSYIGPIN SSIGKAILEM SREESAPLVM HVTKLYNTVD ANNFYAFARV YSGQVKKGQK VKVLGENYSL EDEEDMVVAH IAEICVPCAR YRLHVDGAVA GMLVLLGGVD NSISKTATIV SDNLKDDPYI FRPIAHMSES VFKVAVEPHN PSELPKLLDG LRKTNKSYPL SITKVEESGE HTIFGTGEMY MDCLLYDLRT LYSEIEIRVS DPVARFCETA VDTSSIKCFS DTPNKKNRIT MVVEPLEKGI SNDIENGKVN INWPQKRISE FFQKNYDWDL LASRSIWAFG PDDRGTNILR DDTLSTDVDK NVLNSVKEYI KQGFQWGTRE GPLCDETIRN VNFRLMDVVL APEQIYRGGG QIIPTARRVC YSSFLTASPR LMEPVYMVEV HAPADSLPII YDLLTRRRGH VLQDIPRPGS PLYLVRALIP VIDSCGFETD LRVHTQGQAM CQMVFDHWQV VPGDPLDKSI KPKPLEPARG SDLARDFLIK TRRRKGLVED VSTTRYFDQE MIDSLKEAGV VLSL //