CG11_CANAX
ID CG11_CANAX Reviewed; 698 AA.
AC P0CY18; P24866;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=G1/S-specific cyclin CLN1;
GN Name=CLN1; Synonyms=CCN1;
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 [GENOMIC DNA].
RC STRAIN=SGY126;
RX PubMed=7830719; DOI=10.1007/bf00297278;
RA Sherlock G., Bahman A.M., Mahal A., Shieh J.C., Ferreira M., Rosamond J.;
RT "Molecular cloning and analysis of CDC28 and cyclin homologues from the
RT human fungal pathogen Candida albicans.";
RL Mol. Gen. Genet. 245:716-723(1994).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC (start) transition. Interacts with the CDC2 protein kinase to form MPF.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; X80032; CAA56336.1; -; Genomic_DNA.
DR PIR; S49206; S49206.
DR AlphaFoldDB; P0CY18; -.
DR SMR; P0CY18; -.
DR VEuPathDB; FungiDB:C5_01680C_A; -.
DR VEuPathDB; FungiDB:CAWG_04553; -.
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:InterPro.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR028857; CCNF_metazoan.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR014399; Cyclin_CLN.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF252; PTHR10177:SF252; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001770; Cyclin_CLN; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cyclin.
FT CHAIN 1..698
FT /note="G1/S-specific cyclin CLN1"
FT /id="PRO_0000080414"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 79299 MW; 97F693A73BC77264 CRC64;
MTSLQQQQQQ QRVKYGPPHH IKRRPYHPIL ESLEFQTNQH LIQEYSLDIV NTLSQLESLT
LVNPAMIDLQ PEIQWFMRPF LLDFLIELHS SFKLQPTTLF LCLNIIDRYC AKRIVFKRHY
QLVGCTALWI ASKYEDKKSR VPTLKELTIM CRNAYDEEMF VQMEMHILST LDWSIGHPTL
EDCLQLAIDS NNLSNNTTND IENKSVRPNR KSSISSAVTA VARFLCELSL YDKYFLSVPP
SLIAITANLL SCSMLQIPHA SITLKNLIEQ EIINPQQKKQ KKAFSSNSSR TTTASYTHQN
QSDVRHSSFD EDIDLDSGDE GDDDEDYIDE FYETNNYDDT NATTFDESIN KSTTINDENQ
PPQIHTPFLS GLDEDSILSI KKICLMLIIQ LSKVTEVLSK KYENLGVIQV INNFHSNYKF
IIQSIYENQE LLLNTINDST NNNEIDYKLI QSSEILLQFP KFDEYLTEDE DENVSTDDEA
NSQPQGYDGS GSDGNNQLFT PKSPNAFSSN SSLTLNNHPQ SMVPVTPPSA TSQYSLFSNK
NNRTHESTSG LNSTCNTPTH ISISSFAPPQ PPPGSILKPK LTSINSTNSL KIKKLTSNSN
SSNINIHHGH HNTKQEKRYS HISIGSNSSS KYDGFSPIKS ISTNGSLITN NGSFTNIVNN
TNSSSPLMNQ QQQYYHQQQH QQQVTQSSLY QHHHQYHQ