ID A0A2P6PHQ1_ROSCH Unreviewed; 442 AA.
AC A0A2P6PHQ1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN ORFNames=RchiOBHm_Chr7g0239321 {ECO:0000313|EMBL:PRQ21446.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ21446.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ21446.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
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. Cyclin AB subfamily.
CC {ECO:0000256|ARBA:ARBA00006955}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRQ21446.1}.
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DR EMBL; PDCK01000045; PRQ21446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6PHQ1; -.
DR STRING; 74649.A0A2P6PHQ1; -.
DR EnsemblPlants; PRQ21446; PRQ21446; RchiOBHm_Chr7g0239321.
DR Gramene; PRQ21446; PRQ21446; RchiOBHm_Chr7g0239321.
DR OMA; CISDYAY; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000238479; Chromosome 7.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
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; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177:SF505; B-LIKE CYCLIN; 1.
DR PANTHER; PTHR10177; CYCLINS; 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; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
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:UP000238479}.
FT DOMAIN 227..311
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 320..439
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 324..408
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 49976 MW; 9EA770421CB80C2B CRC64;
MDTRGDGEVN GEVPRRNQRV ALQDRTNVEA AQLLANAQKN NVNPVLVPSL QDKVAVNRKC
APANKGTKKK PIDEDVVVIS SDEEEEKPVL LPCLQDKVAL NRKYAPEKKG TKKKPIDEDV
VGVSSDEEEE KPVSNRSKPS QGSRKEVKTL TSILTARSEA MAGGATNKPK EQVVDFDSAD
FNDELAVVEY VDDMYKFYKL EEDGNRVGDY LDSQPEVNSK MRSILIDWII EVHRKFELMP
ETFYLTVNII DRYLSVRIVP RRELQLLGIS SMVIASKYEE VWAPQVNDFV CISDDAYMED
EIRKMEKEIL GKLEWYLTVP TPYVFLARYI KASVSPDDEM KNMVFFLAEL GVMHYQTIIS
YSPSMIAAAA VYAARCTLNK TPFWTATLKH HTGYLEEQLR ECAKVLVGFH SNAAESNLKA
VYRKYSKPEF GAVAHLNPAK SF
//
