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Database: UniProt
Entry: A0A087XVQ8_POEFO
LinkDB: A0A087XVQ8_POEFO
Original site: A0A087XVQ8_POEFO 
ID   A0A087XVQ8_POEFO        Unreviewed;       283 AA.
AC   A0A087XVQ8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Cyclin-C {ECO:0000256|ARBA:ARBA00019492};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000009861.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000009861.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       regulated gene transcription of nearly all RNA polymerase II-dependent
CC       genes. Mediator functions as a bridge to convey information from gene-
CC       specific regulatory proteins to the basal RNA polymerase II
CC       transcription machinery. Mediator is recruited to promoters by direct
CC       interactions with regulatory proteins and serves as a scaffold for the
CC       assembly of a functional preinitiation complex with RNA polymerase II
CC       and the general transcription factors. Binds to and activates cyclin-
CC       dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain)
CC       of the large subunit of RNA polymerase II (RNAp II), which may inhibit
CC       the formation of a transcription initiation complex.
CC       {ECO:0000256|ARBA:ARBA00025028}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC       {ECO:0000256|ARBA:ARBA00008638}.
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DR   EMBL; AYCK01008691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007561012.1; XM_007560950.2.
DR   AlphaFoldDB; A0A087XVQ8; -.
DR   STRING; 48698.ENSPFOP00000009861; -.
DR   Ensembl; ENSPFOT00000009876.2; ENSPFOP00000009861.2; ENSPFOG00000009757.2.
DR   GeneID; 103144130; -.
DR   KEGG; pfor:103144130; -.
DR   CTD; 892; -.
DR   eggNOG; KOG0794; Eukaryota.
DR   GeneTree; ENSGT00940000155625; -.
DR   OMA; TTCQTVI; -.
DR   OrthoDB; 102875at2759; -.
DR   Proteomes; UP000028760; 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; cd20513; CYCLIN_CCNC_rpt1; 1.
DR   CDD; cd20514; CYCLIN_CCNC_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; IPR031658; Cyclin_C_2.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF7; CYCLIN-C; 1.
DR   Pfam; PF16899; Cyclin_C_2; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF028758; Cyclin, C/H/G types; 1.
DR   SMART; SM00385; CYCLIN; 2.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT   DOMAIN          46..144
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          161..236
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          254..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  33219 MW;  08AE02D5AB5D095F CRC64;
     MAGNFWQSSH YLQWVLDKQD LMKERQKDLK FLTEDEYWKL QIFFANVIQA LGEHLKLRQQ
     VIATATVYFK RFYARYSLKS IDPVLMAPTC VFLASKVEEF GVVSNTRLIS AATSVLKTRF
     SYAFPKEFPY RMNHILECEF YLLELMDCCL IVYHPYRPLL QYVQDMGQED MLLPLAWRIV
     NDTYRTDLCL LYPPFMIALA CLHVACVVQQ KDARQWFAEL SVDMDKILEI IRVILKLYDQ
     WKNFDDRKEI AAVLNKMPKP KPPPNSESDQ SSNGNQSNSY SQS
//
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