ID A0A1C1CKI7_9EURO Unreviewed; 526 AA.
AC A0A1C1CKI7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cyclin domain containing protein {ECO:0000313|EMBL:OCT49007.1};
GN ORFNames=CLCR_04805 {ECO:0000313|EMBL:OCT49007.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT49007.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC regulatory module of the Mediator complex which is itself involved in
CC regulation of basal and activated RNA polymerase II-dependent
CC transcription. The SRB8-11 complex may be involved in the
CC transcriptional repression of a subset of genes regulated by Mediator.
CC It may inhibit the association of the Mediator complex with RNA
CC polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC RNA polymerase II. {ECO:0000256|ARBA:ARBA00025278}.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCT49007.1}.
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DR EMBL; LGRB01000011; OCT49007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CKI7; -.
DR STRING; 86049.A0A1C1CKI7; -.
DR VEuPathDB; FungiDB:CLCR_04805; -.
DR VEuPathDB; FungiDB:G647_02904; -.
DR Proteomes; UP000094526; 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; cd20545; CYCLIN_SpCG1C-like_rpt1; 1.
DR CDD; cd20546; CYCLIN_SpCG1C_ScCTK2-like_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; PF00134; Cyclin_N; 1.
DR Pfam; PF21797; CycT2-like_C; 1.
DR PIRSF; PIRSF036580; Cyclin_L; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 60..165
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 178..307
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 178..265
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 295..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 58643 MW; FCFFCF3D472A8CE0 CRC64;
MPSFQETTRH DASPSFSKNA VLERTQSQWL FTPQELLLSP SILDGMPVAQ ELANRQKGVN
FITQVGIMLK LPQLTLATAS VYLHRFFMRH AMVQNNKPGL HHYSVAATAI FLATKVEENY
RKMKELVVAC CRVAQKSPNL VIDDQSKEYW KWRDTILHNE DLLLEALCFD LQLEQPYRLL
LDFLRYYDVQ ANKQLRNTSW AFLNDSLVTT MCLQLTPSTI AGSALYMGVK FAGIALPDDE
RGRPWWEQLG LDMHEIQRGC NLMAEVYENP ALPRQGQKDA YTKDDDLAMF DRTRHPATPQ
ADQSPTVSAR SGSQGVKRDR DVADDQQSGE WGASVPSERP GGDYHLAPSP KRMRRDSTED
NPSLSQRSSQ RGPPHPADGR PPNESAVSGD DVQKRIDEII NASSSRVPQP NLVRRPSAQP
SQPSYQSSSS RRHSSGASNW NNPPSTYSNG QPDKSQPASR PESRDNGVYG QAESNEHARV
VRRVPFGPPA NEGPAQSTGR AASTSNVTND IDDAEKVDYG SEEGEL
//
