ID   CDK9_SCHPO              Reviewed;         591 AA.
AC   Q96WV9; O13607;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Probable cyclin-dependent kinase 9;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=Cell division protein kinase 9;
GN   Name=cdk9; ORFNames=pi014, SPBC32H8.10;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
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   FUNCTION, INTERACTION WITH PCH1 AND PCT1, AND MUTAGENESIS OF LYS-65;
RP   GLU-83; ASP-184 AND THR-212.
RX   PubMed=12475973; DOI=10.1074/jbc.m211713200;
RA   Pei Y., Schwer B., Shuman S.;
RT   "Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA
RT   capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality
RT   control.";
RL   J. Biol. Chem. 278:7180-7188(2003).
RN   [4]
RP   INTERACTION WITH PCM1.
RX   PubMed=16428435; DOI=10.1128/mcb.26.3.777-788.2006;
RA   Pei Y., Du H., Singer J., Saint Amour C., Granitto S., Shuman S.,
RA   Fisher R.P.;
RT   "Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-
RT   activating kinase Csk1, overlaps functionally with the TFIIH-associated
RT   kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in
RT   vivo.";
RL   Mol. Cell. Biol. 26:777-788(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; THR-212; THR-565 AND
RP   SER-577, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Component of the positive transcription elongation factor b
CC       (P-TEFb) which consists of cdk9 and pch1, and which phosphorylates the
CC       C-terminal domain (CTD) of RNA polymerase II and spt5.
CC       {ECO:0000269|PubMed:12475973}.
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   -!- ACTIVITY REGULATION: May be activated by autophosphorylation or
CC       phosphorylation by a separate activating kinase.
CC   -!- SUBUNIT: Interacts with pch1 cyclin via its N-terminal domain. Via its
CC       C-terminal domain, interacts with RNA triphosphatase pct1 which is
CC       involved in mRNA capping. Interacts also with pcm1.
CC       {ECO:0000269|PubMed:12475973, ECO:0000269|PubMed:16428435}.
CC   -!- INTERACTION:
CC       Q96WV9; O74627: pch1; NbExp=2; IntAct=EBI-443557, EBI-443575;
CC       Q96WV9; Q9P6Q6: pct1; NbExp=2; IntAct=EBI-443557, EBI-443547;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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=BAA21391.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB004534; BAA21391.2; ALT_INIT; Genomic_DNA.
DR   EMBL; CU329671; CAC37500.1; -; Genomic_DNA.
DR   RefSeq; NP_595616.1; NM_001021511.2.
DR   AlphaFoldDB; Q96WV9; -.
DR   SMR; Q96WV9; -.
DR   BioGRID; 276771; 33.
DR   IntAct; Q96WV9; 2.
DR   MINT; Q96WV9; -.
DR   STRING; 284812.Q96WV9; -.
DR   iPTMnet; Q96WV9; -.
DR   MaxQB; Q96WV9; -.
DR   PaxDb; 4896-SPBC32H8-10-1; -.
DR   EnsemblFungi; SPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
DR   GeneID; 2540239; -.
DR   KEGG; spo:SPBC32H8.10; -.
DR   PomBase; SPBC32H8.10; cdk9.
DR   VEuPathDB; FungiDB:SPBC32H8.10; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_000288_181_21_1; -.
DR   InParanoid; Q96WV9; -.
DR   OMA; YTQGGQY; -.
DR   PhylomeDB; Q96WV9; -.
DR   BRENDA; 2.7.11.23; 5613.
DR   Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:Q96WV9; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0070691; C:P-TEFb complex; IPI:PomBase.
DR   GO; GO:0070693; C:P-TEFb-cap methyltransferase complex; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; EXP:PomBase.
DR   GO; GO:0140836; F:RNA polymerase II CTD heptapeptide repeat S5 kinase activity; IDA:PomBase.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   CDD; cd07866; STKc_BUR1; 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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF584; SERINE_THREONINE-PROTEIN KINASE BUR1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..591
FT                   /note="Probable cyclin-dependent kinase 9"
FT                   /id="PRO_0000085808"
FT   DOMAIN          36..339
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..385
FT                   /note="Interaction with pch1"
FT   REGION          341..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..523
FT                   /note="Binds to pct1"
FT   REGION          549..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         42..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         211
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         212
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         565
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MUTAGEN         65
FT                   /note="K->A: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:12475973"
FT   MUTAGEN         83
FT                   /note="E->A: Defective kinase activity."
FT                   /evidence="ECO:0000269|PubMed:12475973"
FT   MUTAGEN         184
FT                   /note="D->N: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:12475973"
FT   MUTAGEN         212
FT                   /note="T->A: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:12475973"
SQ   SEQUENCE   591 AA;  68029 MW;  28DFF6032388E16A CRC64;
     MKRSSSVSVE DEKSARRKLD VVPKLHFVGC SHLTDYHLME KLGEGTFGEV YKSQRRKDGK
     VYALKRILMH TEKEGFPITA IREIKILKSI KHENIIPLSD MTVVRADKKH RRRGSIYMVT
     PYMDHDLSGL LENPSVKFTE PQIKCYMKQL FAGTKYLHDQ LILHRDLKAA NLLIDNHGIL
     KIADFGLARV ITEESYANKN PGLPPPNRRE YTGCVVTRWY RSPELLLGER RYTTAIDMWS
     VGCIMAEMYK GRPILQGSSD LDQLDKIFRL CGSPTQATMP NWEKLPGCEG VRSFPSHPRT
     LETAFFTFGK EMTSLCGAIL TLNPDERLSA SMALEHEYFT TPPYPANPSE LQSYSASHEY
     DKRRKREQRD ANSHAFEQTA NGKRQFRFMT RGPSDPWYGI RRPNYNSQPQ YQRGSYNREG
     GNMDRSRNVN YQPKRQQNFK PLTSDLPQKN SEFSETNAMN QTSNHSHADG QRYYRPEQDR
     SQRLRNPSDY GRQGRQSSQS QQPAWNVSSR YQNNSKVQTT SRASENADTN KTQHNIKYID
     SYVPEYSIAR QSANQKTNEQ HPSSTSLHQQ STSDLKSPSF HENSNVDDTP K
//