CDC5L_DICDI
ID CDC5L_DICDI Reviewed; 800 AA.
AC Q54WZ0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Cell division cycle 5-like protein;
DE AltName: Full=Cdc5-like protein;
GN Name=cdc5l; ORFNames=DDB_G0279311;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: DNA-binding protein involved in cell cycle control. May act
CC as a transcription activator. Plays role in pre-mRNA splicing as core
CC component of precatalytic, catalytic and postcatalytic spliceosomal
CC complexes. May also play a role in the response to DNA damage (DDR).
CC {ECO:0000250|UniProtKB:Q99459}.
CC -!- SUBUNIT: Component of the precatalytic, catalytic and postcatalytic
CC spliceosome complexes. {ECO:0000250|UniProtKB:Q99459}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q99459}. Note=May shuttle between
CC cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q99459}.
CC -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR EMBL; AAFI02000030; EAL67804.1; -; Genomic_DNA.
DR RefSeq; XP_641787.1; XM_636695.1.
DR AlphaFoldDB; Q54WZ0; -.
DR SMR; Q54WZ0; -.
DR STRING; 44689.DDB0220620; -.
DR PaxDb; Q54WZ0; -.
DR EnsemblProtists; EAL67804; EAL67804; DDB_G0279311.
DR GeneID; 8621984; -.
DR KEGG; ddi:DDB_G0279311; -.
DR dictyBase; DDB_G0279311; cdc5l.
DR eggNOG; KOG0050; Eukaryota.
DR HOGENOM; CLU_009082_0_0_1; -.
DR InParanoid; Q54WZ0; -.
DR OMA; PLEGEMN; -.
DR PhylomeDB; Q54WZ0; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q54WZ0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; 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; 2.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 3: Inferred from homology;
KW Cell cycle; Coiled coil; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Spliceosome.
FT CHAIN 1..800
FT /note="Cell division cycle 5-like protein"
FT /id="PRO_0000342369"
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 109..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 621..700
FT /evidence="ECO:0000255"
FT COILED 748..800
FT /evidence="ECO:0000255"
FT COMPBIAS 109..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 92121 MW; DAD25C9077845FC6 CRC64;
MRNVKGGVWK NTEDEILKVA IMKYGLNQWA RISSLLTRKS PAQCKARWHE WLDPSIKKTE
WSKEEEEKLL HLAKIFPSQW KTIAPLVGRT ASQCLERYNR LLDEVQRQQD NENGGGSGGG
GTTTTTTTTT GENDPRRLRM GDIDPTPETK PAKPDPIDMD EDEKETLSEA KARLSNTQGK
KEKRKFREKQ LEEARRLAFL QKKRELKAAG INYNPKKKGK EKSWDISKEI PFYLKPKAGF
YDVPDEELRD EPNKDASFIG KRVDQIENPN YLQRQEKLNK LEDIKKSKKE IFNLPQLISE
TSKSNDVEHS IKRTKLQLPE PQLTDDDIQE ISDYEKLNGS GSGGGSGGVG VGEFPLPAPR
TASISSTAAN NNTNNIRTPM KQDTIMSEAQ NLLALSNAQT PLKGGAGPNV SQTPLPKSVN
NSTPFRTPNP LANQTPTQHN KKQSLNDSNE FAIEDKFKRQ QGKNQLLSNL KNLPSPTIEY
KLELPSELPT IEDDTTLELD NSEIHIREQQ QLKHKEQFKL RNRSTVLKRN LPRSRNLFPI
NKNNNNNNNN NINQDELRIL KEINRIISHD NKTFPNDSIT PSSTFDDDDD DDNHHHHHDD
IDNNSINDND EKYENYDYFT NTELEFADKL IRDEIEQIKQ ELKQPLPSSN EILEEIDQIR
SQFIYLPKEN QFIEKSNANQ TQLIENLQFE YDKTLNKIKN SSMKSVNLEK KLNIYNGGYQ
NRSNTIIKNI DDMFDQLEQS EIEYQCFVAL KNNESIQMEK RLKSIENQVY DQCEIESRLQ
QKYAQLLNEK NLLKKKLSIF
