ID A0A2I4FKK2_JUGRE Unreviewed; 315 AA.
AC A0A2I4FKK2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN Name=LOC108999728 {ECO:0000313|RefSeq:XP_018832179.2};
GN ORFNames=F2P56_022443 {ECO:0000313|EMBL:KAF5458416.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018832179.2};
RN [1] {ECO:0000313|EMBL:KAF5458416.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5458416.1};
RA Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA Wegrzyn J.L., Langley C.H., Neale D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5458416.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5458416.1};
RA Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA Salzberg S.L., Neale D.B.;
RT "Walnut 2.0.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018832179.2}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018832179.2};
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.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; LIHL02000010; KAF5458416.1; -; Genomic_DNA.
DR RefSeq; XP_018832179.2; XM_018976634.2.
DR STRING; 51240.A0A2I4FKK2; -.
DR EnsemblPlants; Jr10_14790_p1; cds.Jr10_14790_p1; Jr10_14790.
DR Gramene; Jr10_14790_p1; cds.Jr10_14790_p1; Jr10_14790.
DR KEGG; jre:108999728; -.
DR OrthoDB; 3789612at2759; -.
DR Proteomes; UP000235220; Chromosome 10.
DR Proteomes; UP000619265; Unassembled WGS sequence.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR CDD; cd20544; CYCLIN_AtCycD-like_rpt2; 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; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177:SF188; CYCLIN-D6-1-RELATED; 1.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
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:UP000235220}.
FT DOMAIN 55..139
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 148..282
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
SQ SEQUENCE 315 AA; 36106 MW; 443EE323664C5859 CRC64;
MEFDLENPLT NLHETNSDTI ASLFLIECDH MPLENYFQSL QTNGFDISVR HEIISEISKF
CCRFDPLLSY LAVNYLDRFL SSQGMLQPKP WILSLLAISC ISLAAKMMKA EVSLVDFQGD
GGFIFDPQTI ERMEILILGA LKWRMRSITP FSFISYYISL FQLKDPPLWQ SLKARATEII
FKSQNDIKLL EMKPSIIAAS ALLYAAHELL PLQYPFFRKA VFCCSYVNKE NLLQCYYAMQ
DIVMDGYESV FDLASSSITP VSVLEQQFPS SEYGETNGTT PTTTIRSAEM RDIKRRKIIN
YCDNLTVQIS RIQQC
//
