ID   SSN8_MAGO7              Reviewed;         363 AA.
AC   A4RD79; G4NCI7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=RNA polymerase II holoenzyme cyclin-like subunit;
GN   Name=SSN8; ORFNames=MGG_01071;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of the
CC       Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CM001235; EHA48284.1; -; Genomic_DNA.
DR   RefSeq; XP_003717868.1; XM_003717820.1.
DR   AlphaFoldDB; A4RD79; -.
DR   SMR; A4RD79; -.
DR   STRING; 318829.MGG_01071T0; -.
DR   EnsemblFungi; MGG_01071T0; MGG_01071T0; MGG_01071.
DR   GeneID; 2674146; -.
DR   KEGG; mgr:MGG_01071; -.
DR   VEuPathDB; FungiDB:MGG_01071; -.
DR   eggNOG; KOG0794; Eukaryota.
DR   HOGENOM; CLU_034754_2_0_1; -.
DR   InParanoid; A4RD79; -.
DR   OMA; SHHQQWL; -.
DR   OrthoDB; 1079428at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
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; cd00043; CYCLIN; 1.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR028367; CyclinC/Ssn8.
DR   PANTHER; PTHR10026; PTHR10026; 1.
DR   PANTHER; PTHR10026:SF7; PTHR10026:SF7; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
PE   3: Inferred from homology;
KW   Activator; Cyclin; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..363
FT                   /note="RNA polymerase II holoenzyme cyclin-like subunit"
FT                   /id="PRO_0000314278"
FT   DOMAIN          53..143
FT                   /note="Cyclin N-terminal"
FT   REGION          252..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  41256 MW;  71B9A5497208AA4F CRC64;
     MAANFWESTQ RRNWLFTKEE LAARRQQLEN EDPSLVTMYP LPEWRHLYNY FNYQMLRLAK
     NLSIRQQAIA TAQVYMKRFY TRVEIRSTNP TLVLVTAVYL ACKMEEMPLH IRNVSLEAKK
     VWPMETPSLE IAKIGECEFW LISEMSAQLI VHQPYRTLTA LQQDFQLAND DHVLAVSFLN
     DHFMTDLPLL YAPHTIALAA IMLALVLRLS KASSSNNAAA GQQGGAQAGP LGITLASGLS
     MFQQAVAAKA MTPGGSGSPA MSSPIQQNPP NQAYQLTPQQ QEMFRQQQMQ QQNRQPETQA
     KDSPQKEKSK LQRFAAWLSE SGVDIEAMID CTQELIAFYE CQESYNEQIT RDQINRFVKA
     RGL