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Database: UniProt
Entry: A0A3P8S7N9_AMPPE
LinkDB: A0A3P8S7N9_AMPPE
Original site: A0A3P8S7N9_AMPPE 
ID   A0A3P8S7N9_AMPPE        Unreviewed;       365 AA.
AC   A0A3P8S7N9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cyclin J {ECO:0000313|Ensembl:ENSAPEP00000007654.1};
GN   Name=CCNJ {ECO:0000313|Ensembl:ENSAPEP00000007654.1};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000007654.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000007654.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000007654.1}
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; A0A3P8S7N9; -.
DR   STRING; 161767.ENSAPEP00000007654; -.
DR   Ensembl; ENSAPET00000007875.1; ENSAPEP00000007654.1; ENSAPEG00000005522.1.
DR   GeneTree; ENSGT00940000156981; -.
DR   OMA; GYAWENL; -.
DR   Proteomes; UP000265080; Chromosome 20.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd20528; CYCLIN_CCNJ-like_rpt1; 1.
DR   CDD; cd20529; CYCLIN_CCNJ-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:SF62; CYCLIN-J; 1.
DR   PANTHER; PTHR10177; CYCLINS; 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:UP000265080}.
FT   DOMAIN          45..136
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          145..287
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          153..247
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          296..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  41414 MW;  8C0CB5A162B6BD98 CRC64;
     MELEDQWWKG QLAADIYQAL RFKELKLPSY KGQSPQLNLR RYFADLIAII SNRFRLCPAA
     RHLAVYLLDL FMDRYDVTLQ QLHMVSLSCL LLASKFEERE DRVPKLETLN SLGCMSSMNL
     VLTKQGLLHM ELLLLETFQW NLYLPTAAHF IEYYLSIAVH EGDLHDGWPM TCLEKTKVYM
     AKYADYFLEV SLQDHVFLCF TPSLVAAACV ASSRLILHLS PTWPPRLQCL TGYTWENLVP
     CAEKLLVAHD SDVKEANKQK CQQPSQQQQQ GQTVFHSSGQ AATVAQYLHQ PSVQYPQQAP
     QSALAPNHRP ASYLNHSTTS LQAPNGSQLG STQTISASLD PKSNIPNRAY QVSMHYSCTA
     PCFDR
//
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