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Database: UniProt
Entry: A0A2G5EJ88_AQUCA
LinkDB: A0A2G5EJ88_AQUCA
Original site: A0A2G5EJ88_AQUCA 
ID   A0A2G5EJ88_AQUCA        Unreviewed;       559 AA.
AC   A0A2G5EJ88;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN   ORFNames=AQUCO_00700222v1 {ECO:0000313|EMBL:PIA55751.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA55751.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA55751.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; KZ305024; PIA55751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5EJ88; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd20588; CYCLIN_AcCycT_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF51; CYCLIN-K; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF21797; CycT2-like_C; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT   DOMAIN          1..104
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          117..202
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          210..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  63207 MW;  31832729240747C3 CRC64;
     MCLKCNGWYF HYRPQVTIAT AIIFSHRFFL HQSHAKNDRR TIATVCMFLA GKVEETPRPL
     KDVILVSYEI IHKKDPAAVQ RIKQKEVYEQ QKELILLGER VVLTTLGFDF NIHHPYKPLV
     EAIKKLKVAQ NSLAQVAWNF VNDGLRTSLC LQFKPHHIAA GAIFLAAKFL KLKLPSEGEK
     VWWKEFDVTS RQLEEVSNQM LELYEQNRLP ASQGSDVGGS VGGRANHHTP AKPSTAHEKS
     AARHPQVEGM SSVKPGSSNP SSTKSASDQS HANHQGGSHR KSQSIDHAST ESKSLISEHR
     LDDEIKEPRH SEQRSVSCIR DSAGEASEAP RFGTEQRAKE VIKRENGRAI KLEEENDGTI
     SSKIDSKVLE NKDPVSISPE ACIKEKVKAA LEKRKKSRGD VARKKELMDD DDLIEQELED
     GVELAVEHEK VKRENMQDRL KSSNSPDPEN SSYETDHQNI GNGNYLETER HDVRELYTDS
     AEEGEVSLLH EDEQIRSPMP SSRKRKAESP DGHLDGKQHH DYIPGHRMNH HDNIGDRGRI
     GKLGYVERDQ KRHVQENPV
//
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