ID G0V8Y6_NAUCC Unreviewed; 312 AA.
AC G0V8Y6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN Name=NCAS0A13770 {ECO:0000313|EMBL:CCC67935.1};
GN OrderedLocusNames=NCAS_0A13770 {ECO:0000313|EMBL:CCC67935.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC67935.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC67935.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; HE576752; CCC67935.1; -; Genomic_DNA.
DR RefSeq; XP_003674315.1; XM_003674267.1.
DR AlphaFoldDB; G0V8Y6; -.
DR STRING; 1064592.G0V8Y6; -.
DR GeneID; 11529299; -.
DR KEGG; ncs:NCAS_0A13770; -.
DR eggNOG; KOG1674; Eukaryota.
DR HOGENOM; CLU_018149_0_0_1; -.
DR InParanoid; G0V8Y6; -.
DR OMA; DSSPMNK; -.
DR OrthoDB; 1467024at2759; -.
DR Proteomes; UP000001640; Chromosome 1.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:UniProt.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd20557; CYCLIN_ScPCL1-like; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR InterPro; IPR012104; PHO85_cyclin_1/2/9.
DR PANTHER; PTHR15615:SF10; PHO85 CYCLIN-2-RELATED; 1.
DR PANTHER; PTHR15615; UNCHARACTERIZED; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF016511; Cyclin_Pcl; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 1.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT DOMAIN 52..140
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 34959 MW; 2C230C5E1735FF5A CRC64;
MSDYEALLSF NKRAVSHEMI QFLASTTASI IQVKPHSEPK TNTAHIIPTL SNFIKALIKH
SNVQTPTLMA TTVYLSKLKS IIPCNVYGIE TTRHRIFLGC LILAAKTLND SSPMNKHWAQ
YTDGLLQIRE VNTIERELLE YFDWDVTIKT KDLIICLSPL LQPIIEQSLR KNQMDLLLFN
APTPGKVRNY IDSSSPNSHS RSSSNMSLPS LVSSATLSTV ESTRSRLSNL CGNTHINTIS
EQEEYSPVPR KTSAAYRGNP YNSPLSDTEN KAQVPTKLRK NSKGYPTILK SGLDKPINQS
DTKRSAWVSF FK
//
