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Database: UniProt
Entry: S7ZM21_PENO1
LinkDB: S7ZM21_PENO1
Original site: S7ZM21_PENO1 
ID   S7ZM21_PENO1            Unreviewed;       480 AA.
AC   S7ZM21;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN   ORFNames=PDE_04696 {ECO:0000313|EMBL:EPS29746.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS29746.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS29746.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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   -!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of the
CC       Mediator complex. {ECO:0000256|ARBA:ARBA00011612}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; KB644412; EPS29746.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7ZM21; -.
DR   STRING; 933388.S7ZM21; -.
DR   eggNOG; KOG0834; Eukaryota.
DR   HOGENOM; CLU_022000_7_2_1; -.
DR   OrthoDB; 4848277at2759; -.
DR   PhylomeDB; S7ZM21; -.
DR   Proteomes; UP000019376; 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; 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; 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   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT   DOMAIN          60..169
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          182..269
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          297..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  54036 MW;  29E5289A2D90156F CRC64;
     MEASGSQASS KRRIPGLPNP VIAATQSKWL FTDEELERTP SRTDKIDREK EDYIRHRAVE
     FIWQVSMMLK MPPQTSMTAT VLMHRFLMRY SLRGQYPEMG ADLMHPKVIA AVALFVAFKV
     DETMRRMKDF VVACCRVAMK QPDLVVDEQS KDYWKWRDLI LQNESVMLEF LCFDLQLESP
     YRILWDYSLF LGVGDNRPLR HSAYAFLNDS TYTVLCLQFQ PRVIAAAALY AAARHCKVAF
     PDDAEGRPWW EQLDVNVGEL IRACKLIVNI YERVQQNLSK GYPDFTFSDA DANDPTRLFN
     NNPLADPILT PRLDTPSSSA ATNGRKRSRE PESHLNEHNQ PTPPAQDPSS LNGDRSPKRQ
     RTISPHPANI ATASPSGPAR PRIPVRAVEL LRQNKATDQT PGDKHDQNSA PQQPPSAHNL
     QPTPHPDETS AEEGEVSDDK KDDTPTIQRS HDTEQSGPHA TAKVNGVNSD EGDGSEEGEI
//
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