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Database: UniProt
Entry: B3LH17_YEAS1
LinkDB: B3LH17_YEAS1
Original site: B3LH17_YEAS1 
ID   B3LH17_YEAS1            Unreviewed;       308 AA.
AC   B3LH17;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   08-NOV-2023, entry version 51.
DE   SubName: Full=G1 cyclin {ECO:0000313|EMBL:EDV08396.1};
GN   ORFNames=SCRG_00621 {ECO:0000313|EMBL:EDV08396.1};
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV08396.1, ECO:0000313|Proteomes:UP000008335};
RN   [1] {ECO:0000313|Proteomes:UP000008335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; CH408043; EDV08396.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LH17; -.
DR   HOGENOM; CLU_018149_0_0_1; -.
DR   Proteomes; UP000008335; 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          51..139
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          248..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  35222 MW;  926AE692B9285FBA CRC64;
     MSNYEALLKF NRKAVSKEMV QYLASTTASI IKIKKTNSMI DIALPAPPLT KFINRLIKHS
     NVQTPTLMAT SVYLAKLRSI IPSNVYGIET TRHRIFLGCL ILAAKTLNDS SPLNKHWAEY
     TDGLLILREV NTIERELLEY FDWDVTISTD DLITCLSPFL KPIKEEQLYK SQRDCRTLKK
     FSAQEKDIVN KTSISHSRSS SNMSIPSLAS TSTLSTLESR RSNLSNYSNR IRTLPELHES
     NNISDKFSPR TYNIDSKHDN KENRPIPTIK PFNFSKARPV ILKTGLNKQI IKEDTKVKKS
     NWSNYFKS
//
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