ID   CEF1_CANGA              Reviewed;         541 AA.
AC   Q6FUG1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Pre-mRNA-splicing factor CEF1;
GN   Name=CEF1; OrderedLocusNames=CAGL0F03751g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in pre-mRNA splicing and cell cycle control.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR   EMBL; CR380952; CAG59057.1; -; Genomic_DNA.
DR   RefSeq; XP_446133.1; XM_446133.1.
DR   AlphaFoldDB; Q6FUG1; -.
DR   SMR; Q6FUG1; -.
DR   STRING; 5478.XP_446133.1; -.
DR   EnsemblFungi; CAG59057; CAG59057; CAGL0F03751g.
DR   GeneID; 2887738; -.
DR   KEGG; cgr:CAGL0F03751g; -.
DR   CGD; CAL0130986; CAGL0F03751g.
DR   VEuPathDB; FungiDB:CAGL0F03751g; -.
DR   eggNOG; KOG0050; Eukaryota.
DR   HOGENOM; CLU_009082_2_1_1; -.
DR   InParanoid; Q6FUG1; -.
DR   OMA; RLPNQWR; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000974; C:Prp19 complex; IEA:EnsemblFungi.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000386; F:second spliceosomal transesterification activity; IEA:EnsemblFungi.
DR   GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IEA:EnsemblFungi.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; DNA-binding; mRNA processing; mRNA splicing;
KW   Nucleus; Reference proteome; Repeat; Spliceosome.
FT   CHAIN           1..541
FT                   /note="Pre-mRNA-splicing factor CEF1"
FT                   /id="PRO_0000197097"
FT   DOMAIN          1..59
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          62..109
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        32..55
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        83..105
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          115..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..262
FT                   /evidence="ECO:0000255"
FT   COILED          462..494
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        115..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  63042 MW;  206F6600C420FC90 CRC64;
     MAPPIYVRGG LWTNIEDQIL KAAVQKYGVH QWSKIASLLQ KKNARQCEIR WNEYLNPTLN
     FEEFTKEEDK KLLELVRTLP NQWRTISELM GRPSQQCIER YNILLETELS KTDGEATTSA
     NSAISTSFGF KPNEIHPSAE TQKAKPDNDE LDEDEREMLS EARARLLNTQ GKKATRKVRE
     RMLEESKRIA QIQKRRELKQ AGINTSLKKS KKKYENEIDY NADVVYEIVP PAVLYDVTRE
     NERTQKALQD FERNIAKKGK RKFKDDGEKE SSPRKRSRDK RPNKEDNKET SMSITSNDSV
     LLNDMKKPVL NLSAPRADGE NLSVSSNNTN DAVLVKKYLT ECFSALPTPK NDFEILWEDS
     DDDDEQEIVS EEDDNSIKVQ ESEQLYELPM ETFDIVDSSM IPSIIADPKN EFEEEYNKLI
     KDARTRAKPT ISKEHLQIWD DLNEEIQKDI SGRTSLTNPE VQISTDTNLD ELRAQIQKYQ
     QRISNYDEQL HIIKPLVENN EQICNTIIRS LIPELKSKQL KYYTRYYMFM KEQKHIKKRT
     K