ID A0A0L9UI62_PHAAN Unreviewed; 323 AA.
AC A0A0L9UI62;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN ORFNames=LR48_Vigan04g244700 {ECO:0000313|EMBL:KOM42249.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM42249.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; CM003374; KOM42249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9UI62; -.
DR STRING; 3914.A0A0L9UI62; -.
DR EnsemblPlants; KOM42249; KOM42249; LR48_Vigan04g244700.
DR Gramene; KOM42249; KOM42249; LR48_Vigan04g244700.
DR Proteomes; UP000053144; Chromosome 4.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177:SF613; B-LIKE CYCLIN; 1.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 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:UP000053144}.
FT DOMAIN 118..202
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 211..318
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 218..303
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
SQ SEQUENCE 323 AA; 37391 MW; C5D24D1D4330B75E CRC64;
METLAGKRKS NSIASVVVQR QHPKKQRVGF TQPSNLPNFI LSKNESLQRE SAISWNNVNL
EKPNSINNFL LSSQIHELDV WDINEYLRVL ERKRRPVVNY IQKVQRTITS NNRAVLVDWL
VEVAEQYNLL SDTLLLCVSY IDRFLSVQPM IRSRLQLLGV SCMFIASKYE EINPPSLNEF
CNITDNTYDK TEIIKMEAEI LKALNFEMGN PTAITFLRFL SGAASDYQKT PNWKIEFLGW
YFAELSLLDD DCIRFLPSVV AASALFLARF FIDPKVHPWF KYVSNLPSPS YVPSNYFEDQ
LHMTDQQKLC TIDNLLDENF NLV
//
