ID   CEF1_DEBHA              Reviewed;         668 AA.
AC   Q6BLT3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Pre-mRNA-splicing factor CEF1;
GN   Name=CEF1; OrderedLocusNames=DEHA2F10901g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CR382138; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR382138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q6BLT3; -.
DR   SMR; Q6BLT3; -.
DR   STRING; 284592.Q6BLT3; -.
DR   InParanoid; Q6BLT3; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR021786; Cdc5p/Cef1_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   Pfam; PF11831; Myb_Cef; 1.
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..668
FT                   /note="Pre-mRNA-splicing factor CEF1"
FT                   /id="PRO_0000197099"
FT   DOMAIN          1..58
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          60..108
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        31..54
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        82..104
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          111..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          158..202
FT                   /evidence="ECO:0000255"
FT   COILED          599..635
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        262..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  76301 MW;  CFF08FFA3C90E685 CRC64;
     MPPIYVKGGV WTNVEDEILK AAVSKYGLNQ WSRVASLLAK KSAKQAKARW NEWLNPNIDK
     SEWTREEDEK LLSLAKLLPN QWRSIAPIIG RTATHCVERY QKLLEDTNDV GIEGDENDLR
     LSGPGIESLP ATGTSHVGDL NINPESKPAK PDEEDMDDEE KEMLSEARAR LANTQGKKAK
     RKARERMLEE SKRISLLQKR RELKAAGMKV SLESKNKKRR QEFDYNADIP HEHEPQSGLY
     DVDEENEANR LERIKFERGV AKEGIPLQEV DEKHKKQKQE AKKSKDDGAK QTQMSLEAAA
     EVFHEREQEI LKRRKLDLPA PEISLDTQPP IGESGSINIS DITTKDSNQE GIDDRILKAT
     RELKRNQATK SSLLAEDTPE IKKETLSKEP TSSKLKSQWK KSVLNLLKSY FAKLPKPHND
     IGIILPSYDP NEEPITASNE MSTDSRVDQG ERLRNLEILR QVDEEKAKLR RSQAVQRELP
     IPKPSSLQQI DTSKCSKLDL LIFNEMRTLL NSDYAKYEDP TFKTNLIDDL DEESFGIVNN
     EISGELMKME SAKVSPKSSH LPKTYEMAEQ IISKLHELSS ESSSIENSIS ANINISAFNY
     RENNALQNID NLYNELNRAD IELKGYTKML QNEEISIESR SKYLHELVDD LVDNEHLLEE
     KVRMLRRT