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Database: UniProt
Entry: Q6FVY1_CANGA
LinkDB: Q6FVY1_CANGA
Original site: Q6FVY1_CANGA 
ID   Q6FVY1_CANGA            Unreviewed;       476 AA.
AC   Q6FVY1;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome D complete sequence {ECO:0000313|EMBL:CAG58524.1};
GN   OrderedLocusNames=CAGL0D04620g {ECO:0000313|CGD:CAL0128517,
GN   ECO:0000313|EMBL:CAG58524.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58524.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58524.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; CR380950; CAG58524.1; -; Genomic_DNA.
DR   RefSeq; XP_445613.1; XM_445613.1.
DR   AlphaFoldDB; Q6FVY1; -.
DR   STRING; 284593.Q6FVY1; -.
DR   EnsemblFungi; CAGL0D04620g-T; CAGL0D04620g-T-p1; CAGL0D04620g.
DR   GeneID; 2886985; -.
DR   KEGG; cgr:CAGL0D04620g; -.
DR   CGD; CAL0128517; CAGL0D04620g.
DR   VEuPathDB; FungiDB:CAGL0D04620g; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_020695_10_4_1; -.
DR   InParanoid; Q6FVY1; -.
DR   OMA; ANDPFMV; -.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0072687; C:meiotic spindle; IEA:EnsemblFungi.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR   GO; GO:0071958; C:new mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0140602; C:nucleolar peripheral inclusion body; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0071957; C:old mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:DNA damage response; IEA:EnsemblFungi.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0140013; P:meiotic nuclear division; IEA:EnsemblFungi.
DR   GO; GO:0075297; P:negative regulation of ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR   GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IEA:EnsemblFungi.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0032888; P:regulation of mitotic spindle elongation; IEA:EnsemblFungi.
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; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF520; G2_MITOTIC-SPECIFIC CYCLIN-1-RELATED; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN          251..335
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          344..459
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          348..430
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          82..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  54523 MW;  2D1D216C4857C2CD CRC64;
     MSLSGNNFEN PQNNGTSRLL KNVQRLALNN VTNTTAGPHV GFLGSQSQDN SALRSFKSSI
     ANLKGDSVPT YKVNPLSRPA LVNNERDLTK TKLGIQEEKE TRNYEENKEN HGPQKGHFTQ
     YDERVEDKNQ SESTVSSQTT TESTQITTSN GDDDQTEEEN SEDADSKKKR PISTIVEQDI
     PKKFKSCNRF GTEEYEWEDL DAEDANDPFM VSEDVNDIFE YLHQLEIVTL PRKEDLYKHR
     NICQNRDILV NWLVKIHNKF GLLPETLYLA VNLMDRFLCK ELVQLDKLQL VGTSCLFIAS
     KYEEVYSPSI KHFASETDGA CTEDEIKEGE KFILKTLEFN LNYPNPMNFL RRISKADDYD
     IQSRTLAKFL LEISLVDFRF IGVLPSLCAA AAMFLSRKML GKGQWDGNLI HYSGGYTKNQ
     LAPVCEMIMD YLVSPVVHDE FHRKYQSRRF MKASIISVQW ALKVRKNGYD IMSLHE
//
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