CWF11_SCHPO
ID CWF11_SCHPO Reviewed; 1284 AA.
AC O94508;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Pre-mRNA-splicing factor cwf11;
DE AltName: Full=Complexed with cdc5 protein 11;
GN Name=cwf11; ORFNames=SPBC646.02;
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: Involved in mRNA splicing where it associates with cdc5 and
CC the other cwf proteins as part of the spliceosome.
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 O94508; P39964: cdc5; NbExp=3; IntAct=EBI-539118, EBI-538771;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CWF11 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22806.1; -; Genomic_DNA.
DR PIR; T40578; T40578.
DR RefSeq; NP_595360.1; NM_001021268.2.
DR PDB; 3JB9; EM; 3.60 A; X=1-1284.
DR PDBsum; 3JB9; -.
DR AlphaFoldDB; O94508; -.
DR SMR; O94508; -.
DR BioGRID; 277639; 47.
DR IntAct; O94508; 7.
DR STRING; 4896.SPBC646.02.1; -.
DR MaxQB; O94508; -.
DR PaxDb; O94508; -.
DR PRIDE; O94508; -.
DR EnsemblFungi; SPBC646.02.1; SPBC646.02.1:pep; SPBC646.02.
DR GeneID; 2541124; -.
DR KEGG; spo:SPBC646.02; -.
DR PomBase; SPBC646.02; cwf11.
DR VEuPathDB; FungiDB:SPBC646.02; -.
DR eggNOG; KOG1806; Eukaryota.
DR HOGENOM; CLU_001195_0_0_1; -.
DR InParanoid; O94508; -.
DR OMA; YQFIDVP; -.
DR PhylomeDB; O94508; -.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:O94508; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IC:PomBase.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032174; Aquarius_N.
DR InterPro; IPR026300; CWF11_fam.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10887; PTHR10887; 2.
DR PANTHER; PTHR10887:SF5; PTHR10887:SF5; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF16399; Aquarius_N; 1.
DR PIRSF; PIRSF038901; AQR_cwf11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT CHAIN 1..1284
FT /note="Pre-mRNA-splicing factor cwf11"
FT /id="PRO_0000079611"
SQ SEQUENCE 1284 AA; 148372 MW; F751A9F4B36534D5 CRC64;
MVLYKNKKKQ IINYANSNWG QNEGVEFQET MLQCILEAVI VSKDAKQVLS LLHELKLFEN
FLWQRVNTEM SLNHINLTCM LLLYKSKYEY ITWDLIDENR FQLFFEKVIE VSLSLNLSEV
VYMIQFITLC FQFSNIEKLR KLVYQLTNIS ILNSLDNLDK VKYLLHDSSS LTKAFDSYKE
KRPSIVEKFP LHNLLSRWIH SLLIKSISYA QTEKQEAKVT PLLAIINMSL VLLSAFPTRR
FAHPVIEDSC FYTALRMSLY YDSNELFKKM TDDLNYVLKF PFDNTRGNEY EKEQKIRNDE
LVYYHLQLTL FSDFQKELGD LVFCTQTSLQ QRQKLEEITS FLSFNSLKSL CSKCYLRTSF
PEKYAIKVDF EFLKNVFINT YDRTRLVNDY DEIINFTLKD VLGERSVMDQ ENSLTNYFLL
QNTAIQYLSI SFFMRQQSKA YKKLLLRSLY AELLNFSEQY RRLSIKNATK NLTKDNFFSL
NNFKVTSVAP PQIGQVLPQF VKCQMGLSRP GPFHSALRDL KNSIKSPFLC LIYISKDMEY
KLLHGNALDP LEGVTDFTIA TICNDDVGMF QSDMQSDSDN KSINVYLSPF YYHSLAGLGE
YRPKQLKFNF ALVLSPEANK YWLDLNILVS LLNRAKEFPK WFEDLFLGFG TPDICAFPNA
GLNSIYARNL FNTVEQLQSV LPNCHVPSNL STESLLIKFY TNQNKISADV TASDRHFLLP
SNRLYTYNDK QLESILRGSQ PGLTMVNGPT RCGKHVLVCK LLEVLQDTSP NDRTVVLSDS
NFSMNTLFTL LEKARCFHQG HLLYLSDEGK DETLERYGTL SSWISKLPGL LREIGRLAAS
IQAPGSHDAS PDTALYFRDA YIKRLWEKYL NTVDDKDSVD AYNRFPFHSY FGDKSKRPIE
TYNKDNFFDY ATKLYGELEY MFQQLEEIRP FGLLRYYEDQ ELYALCQQSR IIGCTWTSLS
TRLGTLKEKG FCFNNLIVMN SQNISESSIT SILLSNCEPT GFDRLVLLGN QYLTSGNQDI
NNTSNGSLFK RLRYLKSRII DLNTQYNVRE SISSLCSSIY PLDIKTVDSS PNKRLDYGNS
GFAHEVQFIN VGAFKGSQET EPVSGYKQNL GEAEYAVALF QYMRMLGYPT NEIVICTLYE
SQVSLLNEII SVRCSHNSFF GQPAFVGTVE KLPSDKRVNF VIFTTVESKE ASDHWNPKTF
YKAFSACSYG LYVLCNRDLF RSTRGLEKLW NEIEKTPDKL LLTTGEIYPS SHKIGSSVET
FEIENLLHLS NYVVEMTKKR LNTN