ID A0A2P5BKK9_PARAD Unreviewed; 308 AA.
AC A0A2P5BKK9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN ORFNames=PanWU01x14_230970 {ECO:0000313|EMBL:PON49325.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON49325.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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.
CC {ECO:0000256|RuleBase:RU000383}.
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:PON49325.1}.
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DR EMBL; JXTB01000263; PON49325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5BKK9; -.
DR STRING; 3476.A0A2P5BKK9; -.
DR OrthoDB; 3789612at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:SF240; B-LIKE CYCLIN; 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:UP000237105}.
FT DOMAIN 55..141
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 150..284
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
SQ SEQUENCE 308 AA; 35082 MW; D33912B7FC6B8E30 CRC64;
MEFHLADPLT SFQEHHSDTI PDLFASEADH MPSRNFFSRL KTVDFYVPFR SEAISLILQA
QFSCNFDPFI SYLAVNYMDR FISKQEVPQE KSWFSRLLVI ACISLASKMK NSPFSLSDIQ
REESPVFDAQ TVHKMELLIL DALSWRMRSI TPFSFYSFFI SFFELNEPPS TQALKDRASE
IIFASQNDTK FLEYKPSIIA ASALLFACHE LFLLQFPCFK ASLSACQYVE SNNLSECFNM
MQEMVLMQGY GSNLDTLSSS ITPMSVLERK TTNSEGESSM SSTTLKTENK RRKLNGLCID
SSSSESGF
//
