ID A4RS43_OSTLU Unreviewed; 338 AA.
AC A4RS43;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Cyclin N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=OSTLU_39570 {ECO:0000313|EMBL:ABO94307.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO94307.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABO94307.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO94307.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; CP000581; ABO94307.1; -; Genomic_DNA.
DR RefSeq; XP_001416015.1; XM_001415978.1.
DR AlphaFoldDB; A4RS43; -.
DR STRING; 436017.A4RS43; -.
DR EnsemblPlants; ABO94307; ABO94307; OSTLU_39570.
DR GeneID; 4999668; -.
DR Gramene; ABO94307; ABO94307; OSTLU_39570.
DR KEGG; olu:OSTLU_39570; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_2_5_1; -.
DR OMA; QPTKTNV; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000001568; Chromosome 1.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR CDD; cd20567; CYCLIN_AtCycB-like_rpt1; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF615; G2_MITOTIC-SPECIFIC CYCLIN-B; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000001568}.
FT DOMAIN 124..208
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 217..333
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 221..302
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 13..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 38457 MW; 7930625BB6E274F5 CRC64;
MLNAFGQKAQ QVATRWGRTA QRTSHGKPRD GNQTGGSMTT AGADVDMRES YSTYLERSAG
SGDVMTDALP DIDLYDHDNP LCATEYVNDI YQYWYKVEPE TQVSETYMLI QGDINSKMRA
ILIDWLVEVH LKFKLMPETL FLTTNLIDRF LELKTVTRKN LQLVGVTAML VASKYEEIWA
PEVRDFVYIS DRAYTRQQIL EMEKQMLNAL GFHLTVPTPY QFMNRFFKAA GGDRKFQLYA
SYAVECALPD YNMLQYPGST LAAAGVYIAM RGLRTGSWNH VMEAHTRLSE AEVYPCACDM
AELMRKAPTA SLTAVYKKYS SEKFMKIASL PVPHDLRL
//