ID H0GQ34_SACCK Unreviewed; 491 AA.
AC H0GQ34;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Clb2p {ECO:0000313|EMBL:EHN04120.1};
GN ORFNames=VIN7_5128 {ECO:0000313|EMBL:EHN04120.1};
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:EHN04120.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN04120.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN04120.1,
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:EHN04120.1}.
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DR EMBL; AGVY01000050; EHN04120.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GQ34; -.
DR SMR; H0GQ34; -.
DR HOGENOM; CLU_020695_10_4_1; -.
DR PhylomeDB; H0GQ34; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:UniProt.
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; IPR046965; Cyclin_A/B-like.
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 PIRSF; PIRSF001771; Cyclin_A_B_D_E; 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}.
FT DOMAIN 266..350
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 359..474
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 363..445
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 59..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 56247 MW; B68FF888871022A0 CRC64;
MSNPIENTEN SQNTSSSRFL RNVQRLALNN VTNTTFQKSN ANNPALTNFK STLNSVKKEG
SRIPQFTRES VSRSTAAQEE KRTLKENGIQ LPKNNLLDDK ENQDPSSQQF GALTSIKEGR
AELPANISLQ ESSSAKEIIQ HDPLKGVGSS TEVVHNSVEN EKLHPARSQL QVRNTESETD
SGKKRPISTI VEQELPKKFK VCDENGKEEY EWEDLDAEDV NDPFMVSEYV NDIFEYLHQL
EVITLPKKED LYQHRNIHQN RDILVNWLVK IHNKFGLLPE TLYLAINIMD RFLGKELVQL
DKLQLVGTSC LFIASKYEEV YSPSIKHFAS ETDGACTEDE IKEGEKFILK TLKFNLNYPN
PMNFLRRISK ADDYDIQSRT LAKFLLEISL VDFRFIGILP SLCAAAAMFM SRKMLGKGKW
DGNLIHYSGG YTKEELAPVC HMIMDYLVSP IVHDEFHRKY QSRRFMKASI ISVQWALKVR
KNGYDIMTLH E
//
