ID   KIN28_ENCCU             Reviewed;         308 AA.
AC   Q8SW92;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable serine/threonine-protein kinase KIN28 homolog;
DE            EC=2.7.11.23;
GN   Name=KIN28; OrderedLocusNames=ECU02_1450;
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: Protein kinase component of transcription factor IIH (TFIIH)
CC       which phosphorylates the C-terminal domain of RNA polymerase II during
CC       transition from transcription to elongation after preinitiation complex
CC       (PIC) formation, thereby positively regulating transcription. Essential
CC       for both basal and activated transcription, and is involved in
CC       nucleotide excision repair (NER) of damaged DNA (By similarity).
CC       {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 TFIIH holo complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {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; AL590442; CAD25174.1; -; Genomic_DNA.
DR   RefSeq; NP_584670.1; NM_001040859.1.
DR   AlphaFoldDB; Q8SW92; -.
DR   SMR; Q8SW92; -.
DR   STRING; 284813.Q8SW92; -.
DR   GeneID; 858660; -.
DR   KEGG; ecu:ECU02_1450; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_1450; -.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; Q8SW92; -.
DR   OMA; GIHHCHR; -.
DR   OrthoDB; 1367115at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
DR   GO; GO:0005634; C:nucleus; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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; 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   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Nucleotide-binding;
KW   Nucleus; Reference proteome; Serine/threonine-protein kinase;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..308
FT                   /note="Probable serine/threonine-protein kinase KIN28
FT                   homolog"
FT                   /id="PRO_0000384427"
FT   DOMAIN          4..294
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         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   308 AA;  34949 MW;  CE679BF63EED7879 CRC64;
     MKTYIRERRL GEGTYAVIYL GYRALPQDKP LVSSGTRIED VPVAIKKIKP TKYTQGHEIS
     AIREIKSLKR IDSKYVVRLI DTFVYDKCVH IVLEYVETNL ENVIRNSDKI IMPGDIKAWI
     LMVLRGVYEC HRLFIIHRDI KPNNILITSE GMVKLADFGL TRGIGNRMTP QAVTRWYRAP
     ELLMGSRDYG SPVDMWSVGC VFAELFLRVP LFAGDTDIQQ LDMIFRALGT PVEREWPGVS
     TLPEFLDFQQ YPKASLNGLF SAASSDALDL LEKLLTLNPC NRISCDDAIK HPYFKSSPPP
     TPIGKLPV