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Database: UniProt
Entry: A0A2P5DLF9_PARAD
LinkDB: A0A2P5DLF9_PARAD
Original site: A0A2P5DLF9_PARAD 
ID   A0A2P5DLF9_PARAD        Unreviewed;       526 AA.
AC   A0A2P5DLF9;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN   ORFNames=PanWU01x14_053420 {ECO:0000313|EMBL:PON74132.1};
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:PON74132.1, 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. 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:PON74132.1}.
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DR   EMBL; JXTB01000030; PON74132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5DLF9; -.
DR   STRING; 3476.A0A2P5DLF9; -.
DR   OrthoDB; 5474295at2759; -.
DR   Proteomes; UP000237105; Unassembled WGS sequence.
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   CDD; cd20511; CYCLIN_AtCycB-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; 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; 3.
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:UP000237105}.
FT   DOMAIN          306..390
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          399..518
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          403..487
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  58591 MW;  E1542F2948134722 CRC64;
     MFGLPVQRPN DETSRSVTVS DLSRSPRKPV PLTAINPKRK SVSQNIAKGR IGGKKKKKKK
     TKGFDRTVVI VRSENPRTER VAIENAKGGG GGGGGSSRLQ VFLSSLFSSI GGVFSGVIVQ
     EQDSDMATRA HLVVPHQQLL KEGGRQKNVP AERRNRRVLK DIGNLVNGRV PEGKPHDQKP
     QVEKKNTEPT IEEHAATAKR DDQKKEDENS KPVSGRRLKE GLTRKNSRTF TSTLSARSKA
     ACGLINKPKE QIVNIDAKDA ENELAVVEYI DELYSFYKLS EDETKVNDYM GLQTDINAKM
     RSILVDWLVE VHHKFELMPE TLYLTINIVD RFLSMKVVPR RELQLVGISS MLLACKYEEI
     WAPEVNDFVC ISDNAYVKEQ ILIMEKAILG KLGWHLTVPT PYVFLVRYIK ASVPTDVELE
     NMVFFLAELG QMHYSAIISY SPSTIAASAV YAARCTLDRS PFWTETLEHH TGYSEVQLMD
     CAKLLASFHS GAAESKLKAV FKKYSGTKSG AVALHVPAKE LLPESP
//
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