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Database: UniProt
Entry: A0A3B4XBZ7_SERLL
LinkDB: A0A3B4XBZ7_SERLL
Original site: A0A3B4XBZ7_SERLL 
ID   A0A3B4XBZ7_SERLL        Unreviewed;       366 AA.
AC   A0A3B4XBZ7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Cyclin-K-like {ECO:0000313|Ensembl:ENSSLDP00000013601.1};
GN   Name=CCNK {ECO:0000313|Ensembl:ENSSLDP00000013601.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000013601.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000013601.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3B4XBZ7; -.
DR   Ensembl; ENSSLDT00000014103.1; ENSSLDP00000013601.1; ENSSLDG00000010751.1.
DR   GeneTree; ENSGT00940000156384; -.
DR   Proteomes; UP000261360; Unplaced.
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; 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:SF144; 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}.
FT   DOMAIN          56..150
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          159..291
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          163..257
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          342..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  41902 MW;  7947089C33563005 CRC64;
     LASNTEDSRP SEKDPAILDH IKPCWYWDKK DLAHTPSQSE GLDPATEARY RREGARFIFD
     VGTRLGLHYD TLATGIVYFH RFYMFHSFKQ FPRYVTGGCC LFLAGKVEET PKKCKDIIKT
     ARSLLNDTQF AQFGDDPKEE VMVLERILLQ TIKFDLQVEH PYQFLLRYAK QLKGDKNKVQ
     KLVQMAWTFV NDSLCTMVAL QWEPQIIAVA VMYLAGRLCK FDIQDWTSKQ SSRRWWEQFV
     YDVPVEVLED ICHQILDLYS QAKQQMPDGG MGTGDSLPPP SILSSSVLPP AKKASPQTSP
     RPPRPAQDWR TLHFKFIHPY TISFSLFFSV LYFCFPEIPN LEPPPPPPPP PPPPPVSINP
     GQCPLP
//
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