ID   CCNB_PATPE              Reviewed;         394 AA.
AC   P18063;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   23-FEB-2022, entry version 99.
DE   RecName: Full=G2/mitotic-specific cyclin-B;
OS   Patiria pectinifera (Starfish) (Asterina pectinifera).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Valvatacea; Valvatida; Asterinidae; Patiria.
OX   NCBI_TaxID=7594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1695583; DOI=10.1016/0012-1606(90)90074-s;
RA   Tachibana K., Ishiura M., Uchida T., Kishimoto T.;
RT   "The starfish egg mRNA responsible for meiosis reinitiation encodes
RT   cyclin.";
RL   Dev. Biol. 140:241-252(1990).
RN   [2]
RP   CONCEPTUAL TRANSLATION.
RA   Gibson T.J.;
RL   Unpublished observations (AUG-1994).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA29994.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M33880; AAA29994.1; ALT_FRAME; mRNA.
DR   PIR; A37350; A37350.
DR   BindingDB; P18063; -.
DR   ChEMBL; CHEMBL2366468; -.
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   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..394
FT                   /note="G2/mitotic-specific cyclin-B"
FT                   /id="PRO_0000080378"
FT   REGION          360..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  45120 MW;  E1245635CF94F64E CRC64;
     MQTACSGNLC GYQLMFSLST VVTVCRSLRS RNRHWFLKLL GVRLTIAMRC ALENISNVAK
     NNVQAAAKKE IKQKRGMTKS KATSSLQSVI GLHVEPVEKV QSPEPMDMSE VSNALEAFSQ
     NILEMGVDDI DKDDHENPQL CSEYVNDIYL YMRHLEREFK VRTDYMAMQE ITERMRTILI
     DWLVQVHLRF HLLQETLFLT IQILDRYLEG ASVSKTKLQL VGVTSMLIAA YEEMYAEIGD
     FVYITDNAYS KAQIRAMECN ILRKLDFNLG KPLCIHFLRR CSKAGGVDGH KHTLSKYIME
     LTLXEYSFVK YDXEIAAAAL LSTRFWDEDM EWTKSLVHYS AYSEGHLGPI VQKMAVLSQQ
     SHPSPNSRLD QEEDMASSKF MSDQQATQEL KSIR