ID   CTK1_ENCCU              Reviewed;         329 AA.
AC   Q8SQW2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable CTD kinase subunit alpha homolog;
DE            Short=CTDK-I subunit alpha;
DE            EC=2.7.11.23;
DE   AltName: Full=CTD kinase subunit 1;
GN   Name=CTK1; OrderedLocusNames=ECU11_0960;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA   Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA   Barton G.J.;
RT   "The complement of protein kinases of the microsporidium Encephalitozoon
RT   cuniculi in relation to those of Saccharomyces cerevisiae and
RT   Schizosaccharomyces pombe.";
RL   BMC Genomics 8:309-309(2007).
CC   -!- FUNCTION: Catalytic subunit of the CTDK-I complex, which
CC       hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of
CC       the largest RNA polymerase II subunit. Involved in RNA polymerase II
CC       transcriptional elongation and pre-mRNA 3'-end processing (By
CC       similarity). {ECO:0000250}.
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 CTDK-I complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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; AL590450; CAD26006.1; -; Genomic_DNA.
DR   RefSeq; NP_586402.1; NM_001042235.1.
DR   AlphaFoldDB; Q8SQW2; -.
DR   SMR; Q8SQW2; -.
DR   STRING; 284813.Q8SQW2; -.
DR   GeneID; 860055; -.
DR   KEGG; ecu:ECU11_0960; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0960; -.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q8SQW2; -.
DR   OMA; FEMSVQT; -.
DR   OrthoDB; 925637at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; mRNA processing; Nucleotide-binding; Nucleus;
KW   Reference proteome; Serine/threonine-protein kinase; Transcription;
KW   Transferase.
FT   CHAIN           1..329
FT                   /note="Probable CTD kinase subunit alpha homolog"
FT                   /id="PRO_0000385504"
FT   DOMAIN          22..297
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         28..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   329 AA;  37291 MW;  6E0D80A2ABFEED68 CRC64;
     MEPAEEGEIL AHRRFTATKM EYEKIRIIGE GTFGQVILAR KGRARYALKK VSKEKEGLSV
     TTIREVQVLR AMGHPSIVRL IEVVVEPGGD IYMVFPYFPY DLNRFIRSNK MTCSEIKHIF
     YQIAQGVCYI HSKGIMHRDL KSANILLDQK LNASIADFGM ARYTTKTGAY TPGMVTLWYR
     APEILLGSSS YTYAVDIWSL GCILTEMYLG HMIFQGSTEM LQLEMVIHAC GSINENSYPG
     VQDLPGFRNF RLPQSPRRIE GIIRKHDASA VELVSKMLCL DPSKRITVEQ VVGSKYFEHE
     ARRDASSAGL QGCSYREDRL SLSKRKNVD