ID A0A1S3U1A1_VIGRR Unreviewed; 348 AA.
AC A0A1S3U1A1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN Name=LOC106760859 {ECO:0000313|RefSeq:XP_014499779.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014499779.1};
RN [1] {ECO:0000313|RefSeq:XP_014499779.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014499779.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_014499779.1; XM_014644293.2.
DR AlphaFoldDB; A0A1S3U1A1; -.
DR STRING; 3916.A0A1S3U1A1; -.
DR GeneID; 106760859; -.
DR KEGG; vra:106760859; -.
DR OrthoDB; 994264at2759; -.
DR Proteomes; UP000087766; Chromosome 5.
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 CDD; cd20506; CYCLIN_AtCycA-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:SF613; B-LIKE CYCLIN; 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:UP000087766}.
FT DOMAIN 121..205
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 214..337
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 218..306
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
SQ SEQUENCE 348 AA; 39924 MW; F1CD442D8DD6ACE0 CRC64;
METRAAAKRK ATAAAAPMVV VQKQHPKRQR VVLGELSNFP NATQNKRKEK LQCRKNPNLK
KSSPTEFISS SSSPQFDQLY VSDIFEYLHV MEMQRKRRPM IDYIEKVQKE VTVIMRTILV
DWLVEVAEEY NLHSDTLHLS VSYIDRFLSV NPVSKSRLQL LGVSAMLIAA KYDEVDPPRV
DAFCNITDNT YQKAEVVKME ADILKSLKFE MGNPTVNTFL RRFVDVACDN KKASNLQFEF
LSCYLADLSL LDYDCLRILP SIVAASAVFL ARFIIAPEVH PWTSSLSECS GYKSVELKEC
VIILHDLYFS RKAASFKAVR EKYKQHKFKF VARLPSPPHI PSHYFETQ
//
