ID A0A445LV43_GLYSO Unreviewed; 416 AA.
AC A0A445LV43;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN ORFNames=D0Y65_005288 {ECO:0000313|EMBL:RZC27066.1};
OS Glycine soja (Wild soybean).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZC27066.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZC27066.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC27066.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RZC27066.1}.
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DR EMBL; QZWG01000002; RZC27066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445LV43; -.
DR Proteomes; UP000289340; Chromosome 2.
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 CDD; cd20567; CYCLIN_AtCycB-like_rpt1; 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; 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:SF253; CYCLIN-B1-4; 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:UP000289340}.
FT DOMAIN 196..280
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 289..408
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 293..377
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 46403 MW; A348F2C0F3A1062E CRC64;
MGGEGRNNRR VLQDIGNLVG KQGHGNGINL SKPVTRNFRA QLLANAQEKN KKSSTEANNG
AVVATDGDGV GNFVPARKVE AAKKTKEEPE VIVISSDDES EEKPAAKGKK EREKSARKNA
KAFSSVLSAR SKAACGLPRD LLVSIDATDM DNELAAAEYI DDIYKFYKET EEEGCVHDYM
GSQPDINAKM RSILVDWLIE VHRKFELMPE TLYLTLNIVD RFLSVKAVPR RELQLVGISS
MLIASKYEEI WAPEVNDFEC ISDNAYVSQQ VLMMEKTILR KLEWYLTVPT PYHFLVRYIK
ASTPSDKEME NMVFFLAELG LMHYPTAILY RPSLIAAAAV FAARCTLGRS PFWTSTLKHY
TGYSEEQLRD CAKIMVNLHA AAPGSKLRAV YKKFCNSDLS AVALLSPAKE NCLEQA
//
