ID A0A1S3UCY7_VIGRR Unreviewed; 478 AA.
AC A0A1S3UCY7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN Name=LOC106764116 {ECO:0000313|RefSeq:XP_014503829.1};
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_014503829.1};
RN [1] {ECO:0000313|RefSeq:XP_014503829.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014503829.1};
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_014503829.1; XM_014648343.2.
DR AlphaFoldDB; A0A1S3UCY7; -.
DR GeneID; 106764116; -.
DR OrthoDB; 994264at2759; -.
DR Proteomes; UP000087766; Chromosome 6.
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 CDD; cd20562; CYCLIN_AtCycA_like_rpt1; 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; CYCLINS; 1.
DR PANTHER; PTHR10177:SF583; G2_MITOTIC-SPECIFIC CYCLIN-A; 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 268..352
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 361..477
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 365..454
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 53660 MW; A3506FE96FEFD2A3 CRC64;
MKNRFSPNIC AHEMSTKNRR SSFSSSTASS LAKRHSSVVS SVKAAKRAPL ANITNERNAP
SSSSVSSSIK TAKTKKEDPA RRSSITRSTT CANKLRELKT INSGTTIIPK ANSLPQTKDA
VAAVARVSVS VQSSIDVSPS KSDARSVSMD ETLSSSYSMK SPDEVEYLDN RDVSAVGSIQ
RKTNNLSICD TTKPEGNIYS GEIVGNLKRE GKVVNIDNIC SDPQLCATYA CDIYKHLRES
EEKKRPSTDF MERIQNDINV SMRAILIDWL VEVAEEYRLV PDTLYLTVNY IDRYLSGNAM
NRKRLQLLGV SCMMIASKYE EICAPEVQDF CYITDNTYLK EELLRMESAV LNYLKFEMTA
PTVKCFLRRF VRAAAHDVQE LPSLQLECLT NFIAELSLLE YNMLRYPPSL IAASATFLGR
FILFPSKKPW NSILHHYTQY WPSDLCACVK DLHRLCCSSD TSNLPAIREK YSQHKAKF
//