SN114_SCHPO
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 03-AUG-2022, entry version 158.
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; 4896.SPBC215.12.1; -.
DR MaxQB; O94316; -.
DR PaxDb; O94316; -.
DR PRIDE; O94316; -.
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; GPDEMGP; -.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
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:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
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; ISO:PomBase.
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; ISO:PomBase.
DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1902802; P:regulation of siRNA-dependent facultative heterochromatin assembly; IGI:PomBase.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISO:PomBase.
DR CDD; cd04098; eEF2_C_snRNP; 1.
DR CDD; cd04167; Snu114p; 1.
DR DisProt; DP02109; -.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 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
