ID   CCNB1_MEDSV             Reviewed;         428 AA.
AC   P46277;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=G2/mitotic-specific cyclin-1;
DE   AltName: Full=B-like cyclin;
DE   AltName: Full=CycMs1;
OS   Medicago sativa subsp. varia (Alfalfa) (Medicago varia).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=36902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. A2;
RX   PubMed=7647566; DOI=10.2307/3870177;
RA   Meskiene I., Boegre L., Dahl M., Pirck M., Ha D.T.C., Swoboda I.,
RA   Heberle-Bors E., Ammerer G., Hirt H.;
RT   "cycMs3, a novel B-type alfalfa cyclin gene, is induced in the G0-to-G1
RT   transition of the cell cycle.";
RL   Plant Cell 7:759-771(1995).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition.
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.
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC       destroyed at mitosis.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82039; CAA57559.1; -; mRNA.
DR   AlphaFoldDB; P46277; -.
DR   SMR; P46277; -.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 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; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Mitosis.
FT   CHAIN           1..428
FT                   /note="G2/mitotic-specific cyclin-1"
FT                   /id="PRO_0000080394"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  48754 MW;  D05A3296B85A0EA0 CRC64;
     MKFSEEKNVS NNPTNFEGGL DSRKVGQNRR ALGVINQNLV VEGRPYPCVV NKRALSERND
     VCEKKQADPV HRPITRRFAA KIASTKTSNA EGTTKRSNLA KSSSNGFGDF IFVDDEHKPV
     EDQPVPMALE QTEPMHSESD QMEEVEMEDI MEEPVMDIDT PDANDPLAVA EYIEDLYSYY
     RKVESTSCVS PNYMAQQFDI NERMRAILVD WLIEVHDKFD LMHETLFLTV NLIDRFLEKQ
     SVVRKKLQLV GLVAMLLACK YEEVSVPVVG DLILISDRAY TRKEVLEMEK VMVNALKFNI
     SVPTAYVFMR RFLKAAQADR KLELLAFFLI ELSLVEYAML KFSPSQLAAA AVYTAQCTMY
     GVKQWSKTCE WHTNYSEDQL LECSSLMVDF HKKAGTGKLT GAHRKYCTSK FSYTAKCEPA
     SFLLENEL