SSN3_GIBMO
ID SSN3_GIBMO Reviewed; 450 AA.
AC Q4FCZ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
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, FCK1;
OS Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusarium
OS verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=117187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH SSN8.
RX PubMed=16504555; DOI=10.1016/j.fgb.2005.09.006;
RA Bluhm B.H., Woloshuk C.P.;
RT "Fck1, a C-type cyclin-dependent kinase, interacts with Fcc1 to regulate
RT development and secondary metabolism in Fusarium verticillioides.";
RL Fungal Genet. Biol. 43:146-154(2006).
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). Required for normal growth and
CC secondary metabolism. {ECO:0000250, ECO:0000269|PubMed:16504555}.
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 (By similarity). Interacts with SSN8/FCC1.
CC {ECO:0000250, ECO:0000269|PubMed:16504555}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ091181; AAY99646.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4FCZ5; -.
DR SMR; Q4FCZ5; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Repressor; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..450
FT /note="Serine/threonine-protein kinase SSN3"
FT /id="PRO_0000312945"
FT DOMAIN 40..393
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 307..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..327
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 450 AA; 50892 MW; 0DDBF7B8C07F2334 CRC64;
MPLRPHIGLG FPAHAYQKRH VEPHDRSTGY QPKVRITDRY RIIGFISSGT YGRVYKAVGR
NGKPVGEFAI KKFKPDKEGE QISYTGISQS AIREMSLCSE LHHINVIRLC EIVLEDKCIF
MVFEYAEHDL LQIIHHHTQQ PRHPIPPATI KSIMFQLLNG CQYLHINWVL HRDLKPANIM
VTSSGEVKIG DLGLARRFDK PLHSLFSGDK VVVTIWYRAP ELILGSYHYT PAIDMWAVGC
IFAELLSLRP IFKGEEAKMD SKKTVPFRRN QMQKIIEIMG VPTKDKWPLL STMPEYNQLN
TLANSMASSH HNHHSHHHPH HHHGHYGSRN PPPPGGSNLE KWYYSTINHT SAPGGTPPLA
SLGSEGYKLL AGLLEYDPSK RLTAAQALQS PFFSTGDRVS ANCFEGCKNE YPCRRVSQDD
NDIRTSSLPG TKRSGLPDDS LIRPAKRQKE
