ID   SSN3_SCHPO              Reviewed;         369 AA.
AC   O13958;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Serine/threonine-protein kinase srb10;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=Cyclin-dependent kinase 8;
DE   AltName: Full=Suppressor of RNA polymerase B srb10;
GN   Name=srb10; Synonyms=cdk8, prk1; ORFNames=SPAC23H4.17c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9559556;
RX   DOI=10.1002/(sici)1097-0061(19980330)14:5<485::aid-yea239>3.0.co;2-v;
RA   Watson P., Davey J.;
RT   "Characterization of the prk1 protein kinase from Schizosaccharomyces
RT   pombe.";
RL   Yeast 14:485-492(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [4]
RP   IDENTIFICATION IN MEDIATOR COMPLEX.
RX   PubMed=12738880; DOI=10.1073/pnas.1030497100;
RA   Samuelsen C.O., Baraznenok V., Khorosjutina O., Spaehr H., Kieselbach T.,
RA   Holmberg S., Gustafsson C.M.;
RT   "TRAP230/ARC240 and TRAP240/ARC250 Mediator subunits are functionally
RT   conserved through evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6422-6427(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA   Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA   Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT   "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT   transcription in vitro.";
RL   J. Biol. Chem. 278:51301-51306(2003).
RN   [6]
RP   ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE
RP   II, INTERACTION WITH MED17 AND MED18, AND MUTAGENESIS OF ASP-158.
RX   PubMed=17043218; DOI=10.1073/pnas.0607483103;
RA   Elmlund H., Baraznenok V., Lindahl M., Samuelsen C.O., Koeck P.J.B.,
RA   Holmberg S., Hebert H., Gustafsson C.M.;
RT   "The cyclin-dependent kinase 8 module sterically blocks Mediator
RT   interactions with RNA polymerase II.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15788-15793(2006).
CC   -!- FUNCTION: Catalytic component of the Cdk8 module/Srb8-11 module which
CC       is a regulatory module of the Mediator complex that regulates basal RNA
CC       polymerase II transcription. The Cdk8 module may sterically hinder the
CC       interaction between Mediator and RNA polymerase II leading to
CC       transcriptional repression of a subset of genes regulated by Mediator.
CC       {ECO:0000269|PubMed:14534314}.
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   -!- SUBUNIT: Component of the Cdk8 module of the Mediator complex. The Cdk8
CC       module is composed of srb8, srb9, srb10 and srb11. Interacts with med17
CC       and med18. {ECO:0000269|PubMed:12738880, ECO:0000269|PubMed:17043218}.
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}.
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DR   EMBL; CU329670; CAB11671.2; -; Genomic_DNA.
DR   PIR; T38311; T38311.
DR   RefSeq; NP_593389.2; NM_001018821.2.
DR   AlphaFoldDB; O13958; -.
DR   SMR; O13958; -.
DR   BioGRID; 278390; 252.
DR   STRING; 284812.O13958; -.
DR   iPTMnet; O13958; -.
DR   MaxQB; O13958; -.
DR   PaxDb; 4896-SPAC23H4-17c-1; -.
DR   EnsemblFungi; SPAC23H4.17c.1; SPAC23H4.17c.1:pep; SPAC23H4.17c.
DR   GeneID; 2541900; -.
DR   KEGG; spo:SPAC23H4.17c; -.
DR   PomBase; SPAC23H4.17c; srb10.
DR   VEuPathDB; FungiDB:SPAC23H4.17c; -.
DR   eggNOG; KOG0666; Eukaryota.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; O13958; -.
DR   OMA; YFKNGGP; -.
DR   BRENDA; 2.7.11.22; 5613.
DR   PRO; PR:O13958; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000791; C:euchromatin; IDA:PomBase.
DR   GO; GO:0016592; C:mediator complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:PomBase.
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:0003713; F:transcription coactivator activity; IC:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IC:PomBase.
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   1: Evidence at protein level;
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..369
FT                   /note="Serine/threonine-protein kinase srb10"
FT                   /id="PRO_0000086580"
FT   DOMAIN          5..319
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         11..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         158
FT                   /note="D->A: Abrogates kinase activity."
FT                   /evidence="ECO:0000269|PubMed:17043218"
SQ   SEQUENCE   369 AA;  42585 MW;  C7F9AC9F73FFD30E CRC64;
     MKDGYKIIGF ISSGTYGKVY KAVSSNSNDK RLFAIKKFKA ESKQVSSNAQ QTGVSQSAIR
     EMMLCREIQH ENIVSLVQVL LKDGTISMVF EYAEHDLLQI IHFHSRSRTR QIPPSILKSI
     LWQIINGVAY LHENWIMHRD LKPANIMITA TGKVKIGDLG LGRLIRDPIL PFYSSDRVVV
     TIWYRAPELL LGAHDYTPAI DVWAIGCIYG EMLALSPLFK GDEIKMEDKK VVPFQSTQML
     RIMELLGTPT EERWPGLKNY PEYYQLSSFE VRYWNNLLPQ WYQTVKNRDP QGLDLLMKML
     QYDPKSRITA KQALEHVFFT SDKLWTTSPF LNQPIHYPER RISEDDSEVS SKRVLSTSLR
     SESKRFKGN
//