CEF1_NEUCR
ID CEF1_NEUCR Reviewed; 779 AA.
AC Q7SAF6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Pre-mRNA-splicing factor cef-1;
GN Name=cef-1; ORFNames=NCU06994;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002239; EAA33398.1; -; Genomic_DNA.
DR RefSeq; XP_962634.1; XM_957541.2.
DR AlphaFoldDB; Q7SAF6; -.
DR SMR; Q7SAF6; -.
DR STRING; 5141.EFNCRP00000007041; -.
DR PRIDE; Q7SAF6; -.
DR EnsemblFungi; EAA33398; EAA33398; NCU06994.
DR GeneID; 3878772; -.
DR KEGG; ncr:NCU06994; -.
DR VEuPathDB; FungiDB:NCU06994; -.
DR HOGENOM; CLU_009082_0_0_1; -.
DR InParanoid; Q7SAF6; -.
DR OMA; PFRTQRE; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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..779
FT /note="Pre-mRNA-splicing factor cef-1"
FT /id="PRO_0000197103"
FT DOMAIN 1..56
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 57..106
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 29..52
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 80..102
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 113..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..204
FT /evidence="ECO:0000255"
FT COILED 653..772
FT /evidence="ECO:0000255"
FT COMPBIAS 125..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 87508 MW; 988149AAAB9B21B3 CRC64;
MPVVKGGVWT NIEDEILKAS VSKYGLNQWA RVSSLLARKT PKQCKARWNE WLDPSIKKIE
WSKEEDEKLL HLAKLMPTQW RTIAPIVGRT ANQCLERYQR LLDEAEQREA SALGLTGPDG
GEAHAPSADD VRKLRPGEVD PDPETKPARP DTIDLDEDEK EMLSEARARL ANTQGKKAKR
KARERQQEES RRLAALQKRR ELKTAGINIK VTTKKQGQMD YNADIPFEKK PVPGFYDTTE
EMSRNEYQRA HFDPKKQQVG NKRKGEEDER DGKRRKGDKD PSVQAALKAG QLQKMREAEQ
SSKRRALVLP APQVGEGELE EIVKMGMIGE RANMLARESD NDATRGLINN YSTLNTNAPI
RTPMAPAQED HIANEIRNIR ALTETQSSLL GGENTPLHQG VGSTGFESVA PRKQVMSTPN
PLATPLRAAG AGPGATPLRV GQTPLRTPRD TFALNDAGDE MSMVGGTPRD VKMREMSIRH
QLKQGLASLP KPKETEWELE LPDDQQEPKT AEQLEEDAAE RDRREREIRE ARELLERKRR
TQVMQRDLPR PVQVDYQSLL KEASQAEDPV KVLIAREAAL LVAHDATKYP LPGAQPTGRA
LEIQKIDDAA LQEAKLQVLM EIKDKPKPEE VQAVWEKSNS SSLLLGLGCY EDDEEEEQIS
TMQIALEEVI DQIVASAEKG NKLEKKLNLH LGGYKNRAEM LRKKISEAHE ALEKANNALG
AFKVLQSSEQ AAIRNRLAAL REEVGFVSTR EREAQELYRR TREELDALTL NGPKANGFR
