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Database: UniProt
Entry: A0A3Q0EZQ4_VIGRR
LinkDB: A0A3Q0EZQ4_VIGRR
Original site: A0A3Q0EZQ4_VIGRR 
ID   A0A3Q0EZQ4_VIGRR        Unreviewed;       298 AA.
AC   A0A3Q0EZQ4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN   Name=LOC106761430 {ECO:0000313|RefSeq:XP_022636671.1};
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_022636671.1};
RN   [1] {ECO:0000313|RefSeq:XP_022636671.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_022636671.1};
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.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   RefSeq; XP_022636671.1; XM_022780950.1.
DR   AlphaFoldDB; A0A3Q0EZQ4; -.
DR   Proteomes; UP000087766; Chromosome 5.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd20543; CYCLIN_AtCycD-like_rpt1; 1.
DR   CDD; cd20544; CYCLIN_AtCycD-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; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177:SF460; CYCLIN-D5-3; 1.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 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          76..162
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          248..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  34001 MW;  017D0B13D14AFB40 CRC64;
     MDDLSSSLLC QENDTCLEEG GDELEYQLVG SRHDCGVSED EYVGILVERE IVLGFRRDES
     LVFGDWMKRA RLEAINWILK TRATLGFRFE TAYLSVTYFD RFLSRRSIDS EKWWAIRLLS
     IACLSLAAKM EECNVPELTE FKLEDYSFEG KVIQKMELLV LSTLEWEMGI ITPFDFLSYF
     ITKFCKESPP SPTFSKAMQL IFTTMKEVNL MDQKPSVIAA AATLVAMDQK MTMEAVELKM
     SSIPQHRLLE PEEEETKRDT HTPIDVTDSS RVTSSAAMAK RRRLTFSDEG SSHGKGQG
//
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