ID   CCNB2_MEDSV             Reviewed;         434 AA.
AC   P46278;
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-2;
DE   AltName: Full=B-like cyclin;
DE   AltName: Full=CycMs2;
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; X82040; CAA57560.1; -; mRNA.
DR   PIR; T09706; T09706.
DR   AlphaFoldDB; P46278; -.
DR   SMR; P46278; -.
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..434
FT                   /note="G2/mitotic-specific cyclin-2"
FT                   /id="PRO_0000080395"
SQ   SEQUENCE   434 AA;  49368 MW;  644EF0A2681A4C32 CRC64;
     MVNTSEENNS NAVMPRKFQG GMNQVGHGGG RIVGQNRRAL GGINQNFVHG RPYPCVVHKR
     VLSEKHEICE KKQADLGHRP ITRRFAAKIA GSQQSYAEKT KNSNPLNLNE FGNSIAIDDE
     LKSPEDQPEP MTLEHTEPMH SDPLEMEEVE MEDIEGEMIL DIDSCDANNS LAVVEYIEDL
     HAYYRKIEYL GCVSPTYMDE QLDLNERMRA ILVDWLIEVH DKFDLMQETL FLTVNLIDRF
     LAKQNVVRKK LQLVGLVAML LACKYEEVSV PVVSDLIHIA DRAYTRKDIL EMEKLMLNTL
     QYNMSLPTAY VFMRRFLKAA QADKKLELVA FFLVDLSLVE YEMLKFPPSL VAAAAVYTAQ
     CTVSGFKHWN KTCEWHTNYS EDQLLECSML MVGFHQKAGA GKLTGVHRKY GSAKFSFTAK
     CEPACFLLEN KNQP