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Database: UniProt
Entry: A0A3Q0QXS8_AMPCI
LinkDB: A0A3Q0QXS8_AMPCI
Original site: A0A3Q0QXS8_AMPCI 
ID   A0A3Q0QXS8_AMPCI        Unreviewed;       359 AA.
AC   A0A3Q0QXS8;
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 J {ECO:0000313|Ensembl:ENSACIP00000002231.1};
GN   Name=CCNJ {ECO:0000313|Ensembl:ENSACIP00000002231.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000002231.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000002231.1}
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; A0A3Q0QXS8; -.
DR   STRING; 61819.ENSACIP00000002231; -.
DR   Ensembl; ENSACIT00000002312.1; ENSACIP00000002231.1; ENSACIG00000001773.1.
DR   GeneTree; ENSGT00940000156981; -.
DR   OMA; GYAWENL; -.
DR   Proteomes; UP000261340; Unplaced.
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}.
FT   DOMAIN          45..136
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          145..284
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          148..247
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          287..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  40841 MW;  253A4BCCE29D532C CRC64;
     MELEDQWWKG QLAADIYQAL RYKELKLPSF KGQSPQLNLR RYFADLIAIV SNRFRLCPAA
     RHLAVYLLDL FMDRYDVTVQ QLHMISLSCL LLASKFEERE DRVPKLETLN NLGCMSSMNL
     VLTKQGLLHM ELLLLETFQW NLYLPTAAHF IDYCLSIAVH EGDLHDGWPM TCLEKTKLYM
     AKYVDYFLEV SLQDHAFLCF APSLVAAACV AASRLILHLS PTWPPRLQRL TGYTWENLIP
     CAEKLLIAHD SDVKEANKQK CQQPNQQQQQ GETVYHTSAQ YLNQPSVQYS QQPPQPGPAP
     GHRPASYLSH STASLQAPNG PQNINTQTIA TSLEPKSNIP SRAFQVSMHY SCAAPCFDR
//
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