ID C8ZDH4_YEAS8 Unreviewed; 460 AA.
AC C8ZDH4;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Clb4p {ECO:0000313|EMBL:CAY81440.1};
GN ORFNames=EC1118_1L7_0540g {ECO:0000313|EMBL:CAY81440.1};
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY81440.1, ECO:0000313|Proteomes:UP000000286};
RN [1] {ECO:0000313|EMBL:CAY81440.1, ECO:0000313|Proteomes:UP000000286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse
RC {ECO:0000313|Proteomes:UP000000286};
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; FN393080; CAY81440.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZDH4; -.
DR HOGENOM; CLU_020695_12_1_1; -.
DR Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L7.
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 GO; GO:0001932; P:regulation of protein phosphorylation; IEA:UniProt.
DR CDD; cd20568; CYCLIN_CLBs_yeast_rpt1; 1.
DR CDD; cd20512; CYCLIN_CLBs_yeast_rpt2; 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 InterPro; IPR048258; Cyclins_cyclin-box.
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.
DR PROSITE; PS00292; CYCLINS; 1.
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}.
FT DOMAIN 245..329
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 338..453
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 342..423
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 101..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 53858 MW; FE166BCEEF75409A CRC64;
MMLEGYTVQP PQSTLMGDIE IQDENANQEV KNVLYQGVQK GIKRLEKRQR RVALGDVTSQ
KANKIHNAIH NKFHQTKNNF EIENIRSSAL VKEQQRDVRD EDSDYFLIDS SEGSSTDDEQ
VNEDAIDDLL SRRVNDQQIQ ADEVYEDFDG EMHDVIEEDV DSQIEPLSPI NNDEIQTELD
RAFEKYFRSV PNPLDDDTHD VVMVVEYASD IFYYLRELEV KYRPNPYYMQ NQVELTWPFR
RTMIDWLVQL HFRFQLLPET LYLTINIVDR FLSKKTVTLN RFQLVGVSAL FIAAKFEEIN
CPTLDDLVYM LENTYTRDDI IRAEQYMIDT LEFEIGWPGP MPFLRRISKA DDYDFEPRTL
AKYLLETTIV EPKLVAAAPS WLAAGAYFLS RTILGSNDWS LKHVFYSGYT SSQIIPLASL
ILENCKNASR RHHSIWKKYF DQKHYRCSQI VEEWIVSTEA
//
