ID H0GS70_SACCK Unreviewed; 309 AA.
AC H0GS70;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE SubName: Full=Pcl9p {ECO:0000313|EMBL:EHN03369.1};
GN ORFNames=VIN7_5983 {ECO:0000313|EMBL:EHN03369.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN03369.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN03369.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN03369.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN03369.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGVY01000153; EHN03369.1; -; Genomic_DNA.
DR HOGENOM; CLU_018149_0_0_1; -.
DR PhylomeDB; H0GS70; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
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}.
FT DOMAIN 50..138
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 242..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 35038 MW; F214194A1A9C77EF CRC64;
MFDYDALLQF NRKPVSQEMI QFLATSTASI IQIRQNSNQT HGCQLPELFT FIKKVVIQSN
VQTPTLMATT VYLNKLKNII PTNVYGIETT RHRIFLGCLI LAAKTLNDSS PWNKHWSTYT
EGLLKVREVN TIERELLEYF NWDVKITSSD LINALAHFLV PIKEQLSRQK RQEVLLFNAP
SPGRLKEYIN HRRPVSHSRS SSAMSVPSLT SMVTVSTTES XTSALAKLLP PVPLMVLDNF
NKENHAPSKN SGDTHHNFTT LSQKKVHSTD HIGASSSPSS LNLQTTLHKP TVHQRLNFTR
KGWSSFFKQ
//
