ID   SSN3_PHANO              Reviewed;         443 AA.
AC   Q0TWJ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Serine/threonine-protein kinase SSN3;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=Cyclin-dependent kinase 8;
GN   Name=SSN3; Synonyms=CDK8; ORFNames=SNOG_16136;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Component of the srb8-11 complex. The srb8-11 complex is a
CC       regulatory module of the Mediator complex which is itself 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={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 protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT76508.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445367; EAT76508.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001806263.1; XM_001806211.1.
DR   AlphaFoldDB; Q0TWJ7; -.
DR   SMR; Q0TWJ7; -.
DR   STRING; 321614.Q0TWJ7; -.
DR   GeneID; 5983193; -.
DR   KEGG; pno:SNOG_16136; -.
DR   VEuPathDB; FungiDB:JI435_161360; -.
DR   eggNOG; KOG0666; Eukaryota.
DR   InParanoid; Q0TWJ7; -.
DR   OMA; YFKNGGP; -.
DR   OrthoDB; 46620at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07842; STKc_CDK8_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF495; CYCLIN-DEPENDENT KINASE 8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repressor;
KW   Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..443
FT                   /note="Serine/threonine-protein kinase SSN3"
FT                   /id="PRO_0000312949"
FT   DOMAIN          54..384
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         60..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   443 AA;  49756 MW;  5FE8CBD16BF4247B CRC64;
     MERKRGREMN PPSADPPSAT PVARANLPGS VAAAFHGRPC SQGTTTLKRV NERYKIVGFI
     SSGTYGRVYK AEGKNGRTGE FAIKKFKPDK EGELQYSGIS QSAIREMALC TELAHPNVVH
     TVEIILEEKC IFIVFEYAEH DLLQIIHHHN QPQRQAIPAR TIKSILYQLL QGLVYLHRNW
     VMHRDLKPAN IMVTSAGKVK IGDLGLARLF YKPLQSLFSG DKVVVTIWYR APELLLGSRH
     YTPAVDLWAV GCIFAELLSL RPIFKGEEAK MDSKKTVPFQ RNQMQKIVEI MGMPSKDRWP
     LLTAMPEYPQ LSSLIAGNAA RFARPQGGDG LDRWYNQTLI NNQYPAGPGP ETPGAEGLAL
     LKQLLEYDPQ KRLTAEKALE HRYFTEHGKP SDNCFEDSKI KYPVRRVSQE DNDIRTSSLP
     GTKRSGLPDD SLMGRPAKRL KEG
//