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Database: UniProt
Entry: B9S6T5_RICCO
LinkDB: B9S6T5_RICCO
Original site: B9S6T5_RICCO 
ID   B9S6T5_RICCO            Unreviewed;       432 AA.
AC   B9S6T5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN   ORFNames=RCOM_0873690 {ECO:0000313|EMBL:EEF40691.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- SUBUNIT: Interacts with the CDC2 protein kinase to form a
CC       serine/threonine kinase holoenzyme complex also known as maturation
CC       promoting factor (MPF). The cyclin subunit imparts substrate
CC       specificity to the complex. {ECO:0000256|ARBA:ARBA00011177}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006955}.
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DR   EMBL; EQ973882; EEF40691.1; -; Genomic_DNA.
DR   RefSeq; XP_002521704.1; XM_002521658.2.
DR   AlphaFoldDB; B9S6T5; -.
DR   SMR; B9S6T5; -.
DR   STRING; 3988.B9S6T5; -.
DR   GeneID; 8268759; -.
DR   KEGG; rcu:8268759; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   InParanoid; B9S6T5; -.
DR   OrthoDB; 5474295at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   CDD; cd20567; CYCLIN_AtCycB-like_rpt1; 1.
DR   CDD; cd20511; CYCLIN_AtCycB-like_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:SF203; CYCLIN-O; 1.
DR   PANTHER; PTHR10177; CYCLINS; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT   DOMAIN          214..298
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          307..424
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          311..393
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  49378 MW;  397EEB7BC8F7708D CRC64;
     MNVSDENNPN IAKPSSFQGG LEMGNRKFGQ EIRNNRRALN VLNQNFMGGQ GAYPCVVNKR
     GLSESDGVCE RNQLNPAHRP ITRKFAAQLS STHQNCPQET KKHKPSVSST NGFGDSIFID
     VEENKAAEDH PEPMFLEQTE ATLDEMEEVE MEDIIEEPIV DIDGCDAKNP LAVVDYVEDL
     YANYRKIENF TCVSQNYMAQ QFDINEKMRA ILIDWLIEVH DKFDLMKETL FLTVNLIDRF
     LSQQTVVRKK LQLVGLVAML LACKYEEVSV PVVGDLILIS DKAYNREEVL EMEKLMLNKL
     QFNMSFPTPY VFMQRFLKAA QSDKKIEMLS FFIIELSLVE YEMLKFPPSL LAAAAIYTAQ
     CTIYGFKQWN RTCEWHSNYS EDQLLECSRL MVGFHQKAGT GKLTGVHRKY NTSKFGHTSK
     CEPACFLLET QS
//
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