ID   CG21_CANAX              Reviewed;         492 AA.
AC   P47829;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=G2/mitotic-specific cyclin CYB1;
GN   Name=CYB1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8654974; DOI=10.1016/0378-1119(95)00893-4;
RA   Damagnez V., Cottarel G.;
RT   "Candida albicans CDK1 and CYB1: cDNA homologues of the cdc2/CDC28 and
RT   cdc13/CLB1/CLB2 cell cycle control genes.";
RL   Gene 172:137-141(1996).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. Interacts with the CDC2 protein kinase to form
CC       MPF. G2/M cyclins accumulate steadily during G2 and are abruptly
CC       destroyed at mitosis (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U40430; AAC49451.1; -; mRNA.
DR   PIR; JC4828; JC4828.
DR   AlphaFoldDB; P47829; -.
DR   SMR; P47829; -.
DR   VEuPathDB; FungiDB:C2_01410C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03914; -.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:UniProt.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:UniProt.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 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; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Mitosis.
FT   CHAIN           1..492
FT                   /note="G2/mitotic-specific cyclin CYB1"
FT                   /id="PRO_0000080407"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  56777 MW;  B71353DBE74E26CF CRC64;
     MPQVTKTNNE NEFRLTRSKV QHQESISTIK NTTISNSQHK QQTQQQISSP PQVSVTSSEG
     VSHVNTRQYL GDVSNQYITN AKPTNKRKPL GGDNAPLQKQ QHRPSRPIPI ASDNNNNGST
     SSSSNSSNNN NNDANRLASL AVPSRLPQKR QATESSTNLV EKLRVPQPEV GERSQSYHKK
     SRLIDYEWQD LDEEDNDDQL MVSEYVNEIF SYYYELETRM LPDPQYLFKQ TLLKPRMRSI
     LVDWLVEMHL KFKLLPESLF LAVNVMDRFM SVEVVQIDKL QLLATAALFT AAKNEEVFSP
     SVKNYAYFTD GSYTPEEVVQ AEKYMLTILN FDLNYPNPMN FLRRISKADD YDVQSRTLGK
     YLLEITIVDY KFIGMRPSLC CASAMYLARL ILGKLPVWNG NLIHYSGGYR ISDMRECIEL
     MFQYLIAPIE HDEFFKKYAM RKFMRASTLC RNWAKKFQAS GRDLFDERLS THRLTLEDDD
     EEEEIVVAEA EE