ID   CCNB_ARBPU              Reviewed;         409 AA.
AC   P07818;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=G2/mitotic-specific cyclin-B;
OS   Arbacia punctulata (Punctuate sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Arbacioida; Arbaciidae; Arbacia.
OX   NCBI_TaxID=7641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2826125; DOI=10.1002/j.1460-2075.1987.tb02604.x;
RA   Pines J., Hunt T.;
RT   "Molecular cloning and characterization of the mRNA for cyclin from sea
RT   urchin eggs.";
RL   EMBO J. 6:2987-2995(1987).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition.
CC   -!- SUBUNIT: Interacts with the CDK1 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}.
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DR   EMBL; Y00608; CAA68650.1; -; mRNA.
DR   PIR; S00662; S00662.
DR   PDB; 6EF0; EM; 4.43 A; s=26-37.
DR   PDB; 6EF1; EM; 4.73 A; s=22-36.
DR   PDB; 6EF2; EM; 4.27 A; s=21-36.
DR   PDB; 6EF3; EM; 4.17 A; s=16-41.
DR   PDBsum; 6EF0; -.
DR   PDBsum; 6EF1; -.
DR   PDBsum; 6EF2; -.
DR   PDBsum; 6EF3; -.
DR   AlphaFoldDB; P07818; -.
DR   SMR; P07818; -.
DR   ELM; P07818; -.
DR   PRIDE; P07818; -.
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   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cyclin; Mitosis.
FT   CHAIN           1..409
FT                   /note="G2/mitotic-specific cyclin-B"
FT                   /id="PRO_0000080377"
SQ   SEQUENCE   409 AA;  46086 MW;  FAE254110567C618 CRC64;
     MALGTRNMNM NLHGESKHTF NNENVSARLG GKSIAVQKPA QRAALGNISN VVRTAQAGSK
     KVVKKDTRQK AMTKTKATSS LHAVVGLPVE DLPTEMRSTS PDVLDAMEVD QAIEAFSQQL
     IALQVEDIDK DDGDNPQLCS EYAKDIYLYL RRLEVEMMVP ANYLDRQETQ ITGRMRLILV
     DWLVQVHLRF HLLQETLFLT VQLIDRFLAE HSVSKGKLQL VGVTAMFIAS KYEEMYPPEI
     NDFVYITDNA YTKAQIRQME IAMLKGLKYK LGKPLCLHFL RRNSKAAGVD AQKHTLAKYL
     MEITLPEYSM VQYSPSEIAA AAIYLSMTLL DPETHSSWCP KMTHYSMYSE DHLRPIVQKI
     VQILLRDDSA SQKYSAVKTK YGSSKFMKIS GIAQLDSSLL KQIAQGSNE