ID   A0A3Q3EM50_9LABR        Unreviewed;       559 AA.
AC   A0A3Q3EM50;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cyclin K {ECO:0000313|Ensembl:ENSLBEP00000008369.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000008369.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000008369.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Interacts with the CDK1 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:ARBA00025821}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   AlphaFoldDB; A0A3Q3EM50; -.
DR   STRING; 56723.ENSLBEP00000008369; -.
DR   Ensembl; ENSLBET00000008791.1; ENSLBEP00000008369.1; ENSLBEG00000006428.1.
DR   GeneTree; ENSGT00940000165223; -.
DR   InParanoid; A0A3Q3EM50; -.
DR   Proteomes; UP000261660; Unplaced.
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:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd20530; CYCLIN_CCNK_rpt1; 1.
DR   CDD; cd20531; CYCLIN_CCNK_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; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF51; CYCLIN-K; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00022618};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   DOMAIN          71..165
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          174..299
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          178..272
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..321
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..415
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..543
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  61953 MW;  1BA299F8C568A1C5 CRC64;
     MLKPSTAGPS SVASPQPMKD SKENYSMTNQ GMLDHIKPCW YWDKKDLAHT PSQSEGLDPG
     TEARYRREGA RFIFDVGTRL GLHYDTLATG IIYFHRFYMF HSFKQFPRYV TGACCLFLAG
     KVEETPKKCK DIIKTARSLL NDVQFAQFGD DPKEEVMVLE RILLQTIKFD LQVEHPYMFL
     LRYVKQLKGE KNKVCKVLQM AWTFVNDSLC TMLSLQWEPE IIAVAVMYLA GRLCKFDIQE
     WTAKQSSRRW WEQFVQDVPV ELLEDICHQI LDLYSQGNKP IPQQIQEKER ASVPPLPAPP
     VPLGQPPAAN PPPPPPKKTS PQGGSPARQL KRSHTSPKDE PKAPEQVGSK IPRLESPMPP
     LPTSQPPPDR KPAAPAPPTE AEPGSETAPL PPHAPPPHQP PPLPHRPPPP PPSNYIMSTT
     SSYMSGEGFQ SLQSMMKTEV PSYAPMPPNY APPIPPYHPH VYPPPAAPPP GPPPPPSSYP
     PPNLPPTYPP PGYNNYPPPP PRMPPGHVPP PGIGLPPTGY PPPPPGPPGQ SQVPLPPPPG
     MPLNRGGLDE MRMRQQSLN
//