ID CTK1_YEAST Reviewed; 528 AA. AC Q03957; D6VX57; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 212. DE RecName: Full=CTD kinase subunit alpha; DE Short=CTDK-I subunit alpha; DE EC=2.7.11.23; DE AltName: Full=CTD kinase 58 kDa subunit; DE AltName: Full=CTD kinase subunit 1; GN Name=CTK1; OrderedLocusNames=YKL139W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1820212; RA Lee J.M., Greenleaf A.L.; RT "CTD kinase large subunit is encoded by CTK1, a gene required for normal RT growth of Saccharomyces cerevisiae."; RL Gene Expr. 1:149-167(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP CTD KINASE ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE. RX PubMed=7565723; DOI=10.1128/mcb.15.10.5716; RA Sterner D.E., Lee J.M., Hardin S.E., Greenleaf A.L.; RT "The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent RT cyclin-cyclin-dependent kinase complex."; RL Mol. Cell. Biol. 15:5716-5724(1995). RN [5] RP FUNCTION IN RNA POLYMERASE II TRANSCRIPTION. RX PubMed=9110987; DOI=10.1074/jbc.272.17.10990; RA Lee J.M., Greenleaf A.L.; RT "Modulation of RNA polymerase II elongation efficiency by C-terminal RT heptapeptide repeat domain kinase I."; RL J. Biol. Chem. 272:10990-10993(1997). RN [6] RP FUNCTION IN PHOSPHORYLATION REGULATION, AND DISRUPTION PHENOTYPE. RX PubMed=10488128; DOI=10.1074/jbc.274.39.27823; RA Patturajan M., Conrad N.K., Bregman D.B., Corden J.L.; RT "Yeast carboxyl-terminal domain kinase I positively and negatively RT regulates RNA polymerase II carboxyl-terminal domain phosphorylation."; RL J. Biol. Chem. 274:27823-27828(1999). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=11311553; DOI=10.1016/s0378-1119(01)00389-4; RA Jona G., Wittschieben B.O., Svejstrup J.Q., Gileadi O.; RT "Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in RT transcription elongation in vivo."; RL Gene 267:31-36(2001). RN [8] RP ACTIVATION, AND INTERACTION WITH CTK2 AND CTK3. RX PubMed=11118453; DOI=10.1074/jbc.m010162200; RA Hautbergue G., Goguel V.; RT "Activation of the cyclin-dependent kinase CTDK-I requires the RT heterodimerization of two unstable subunits."; RL J. Biol. Chem. 276:8005-8013(2001). RN [9] RP FUNCTION IN PRE-MRNA END PROCESSING. RX PubMed=12504017; DOI=10.1016/s1097-2765(02)00731-1; RA Skaar D.A., Greenleaf A.L.; RT "The RNA polymerase II CTD kinase CTDK-I affects pre-mRNA 3' RT cleavage/polyadenylation through the processing component Pti1p."; RL Mol. Cell 10:1429-1439(2002). RN [10] RP FUNCTION, MUTAGENESIS OF ASP-324, AND DISRUPTION PHENOTYPE. RX PubMed=12684377; DOI=10.1128/ec.2.2.274-283.2003; RA Ostapenko D., Solomon M.J.; RT "Budding yeast CTDK-I is required for DNA damage-induced transcription."; RL Eukaryot. Cell 2:274-283(2003). RN [11] RP FUNCTION IN H3K36 METHYLATION. RX PubMed=12629047; DOI=10.1101/gad.1055503; RA Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H., RA Strahl B.D.; RT "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in RT yeast."; RL Genes Dev. 17:654-663(2003). RN [12] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [13] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [14] RP FUNCTION OF THE CTDK-I COMPLEX IN PHOSPHORYLATION. RX PubMed=15047695; DOI=10.1074/jbc.m402218200; RA Jones J.C., Phatnani H.P., Haystead T.A., MacDonald J.A., Alam S.M., RA Greenleaf A.L.; RT "C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA RT polymerase II C-terminal domain repeats."; RL J. Biol. Chem. 279:24957-24964(2004). RN [15] RP FUNCTION IN RNA POLYMERASE I TRANSCRIPTION, INTERACTION WITH RNA POLYMERASE RP I, AND SUBCELLULAR LOCATION. RX PubMed=15520468; DOI=10.1093/nar/gkh927; RA Bouchoux C., Hautbergue G., Grenetier S., Carles C., Riva M., Goguel V.; RT "CTD kinase I is involved in RNA polymerase I transcription."; RL Nucleic Acids Res. 32:5851-5860(2004). RN [16] RP FUNCTION IN TELOMERE MAINTENANCE. RX PubMed=15161972; DOI=10.1073/pnas.0401263101; RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C., RA Krauskopf A., Kupiec M., McEachern M.J.; RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that RT affect telomere length."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004). RN [17] RP FUNCTION IN RESPONSE TO GLUCOSE LIMITATION, AND INTERACTION WITH SNF1. RX PubMed=16182287; DOI=10.1016/j.febslet.2005.08.057; RA Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.; RT "Glucose deprivation mediates interaction between CTDK-I and Snf1 in RT Saccharomyces cerevisiae."; RL FEBS Lett. 579:5318-5324(2005). RN [18] RP PHOSPHORYLATION AT THR-338 BY CAK1, AND MUTAGENESIS OF ASP-324 AND THR-338. RX PubMed=15870265; DOI=10.1128/mcb.25.10.3906-3913.2005; RA Ostapenko D., Solomon M.J.; RT "Phosphorylation by Cak1 regulates the C-terminal domain kinase Ctk1 in RT Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 25:3906-3913(2005). RN [19] RP FUNCTION. RX PubMed=16984969; DOI=10.1093/nar/gkl493; RA Grenetier S., Bouchoux C., Goguel V.; RT "CTD kinase I is required for the integrity of the rDNA tandem array."; RL Nucleic Acids Res. 34:4996-5006(2006). RN [20] RP FUNCTION IN TRANSLATION, AND INTERACTION WITH RIBOSOMES. RX PubMed=17545469; DOI=10.1101/gad.428407; RA Roether S., Straesser K.; RT "The RNA polymerase II CTD kinase Ctk1 functions in translation RT elongation."; RL Genes Dev. 21:1409-1421(2007). RN [21] RP FUNCTION IN H3K4 METHYLATION. RX PubMed=17088384; DOI=10.1128/mcb.01628-06; RA Xiao T., Shibata Y., Rao B., Laribee R.N., O'Rourke R., Buck M.J., RA Greenblatt J.F., Krogan N.J., Lieb J.D., Strahl B.D.; RT "The RNA polymerase II kinase Ctk1 regulates positioning of a 5' histone RT methylation boundary along genes."; RL Mol. Cell. Biol. 27:721-731(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. CTDK-I phosphorylates 'Ser-5' if CC the CTD substrate is not phosphorylated at 'Ser-5', but will CC phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already CC phosphorylated. CTDK-I is also more reactive toward substrates that are CC prephosphorylated at 'Ser-2' or 'Ser-5' compared with an CC unphosphorylated CTD substrate, therefore efficiently creating doubly CC phosphorylated CTD repeats. Involved in RNA polymerase II CC transcriptional elongation, and through PTI1, pre-mRNA 3'-end CC processing. Participates in both positive and negative regulation of CC CTD phosphorylation. Required for DNA damage induced transcription, CC including the expression of the RNR genes, and reprogramming of gene CC expression upon amino acid starvation. Required for SET2 mediated H3K36 CC methylation. Also regulates H3K4 methylation. Controls the maintenance CC of suppressive chromatin in the coding regions of genes by both CC promoting H3K36 methylation, which leads to histone deacetylation, and CC catalyzing phosphorylation of the CTD required to localize H3K4 CC chromatin modification specifically to the 5' ends of genes, thereby CC creating a boundary for H3K4 methylation that prevents a mark CC associated with transcriptional initiation from spreading into the CC bodies of genes. Involved in RNA polymerase I transcription. Involved CC in telomere maintenance. Acts together with SNF1 to induce GSY2 CC transcription in response to glucose limitation. Involved in the CC adaptation to alternative carbon sources, including galactose, glycerol CC and ethanol, but not raffinose. Required for the integrity of the rDNA CC locus. Functions in translation elongation by enhancing decoding CC fidelity. Needed for translational accuracy by phosphorylating RPS2. CC {ECO:0000269|PubMed:10488128, ECO:0000269|PubMed:12504017, CC ECO:0000269|PubMed:12629047, ECO:0000269|PubMed:12684377, CC ECO:0000269|PubMed:15047695, ECO:0000269|PubMed:15161972, CC ECO:0000269|PubMed:15520468, ECO:0000269|PubMed:16182287, CC ECO:0000269|PubMed:16984969, ECO:0000269|PubMed:17088384, CC ECO:0000269|PubMed:17545469, ECO:0000269|PubMed:9110987}. 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: CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also CC called alpha, beta and gamma). Interacts directly with the CTK2 and CC CTK3 subunits, this interaction is required for kinase activity. CC Interacts with RNA polymerase I. Interacts with SNF1, but only at low CC glucose concentrations. Interacts with translating ribosomes. CC {ECO:0000269|PubMed:11118453, ECO:0000269|PubMed:15520468, CC ECO:0000269|PubMed:16182287, ECO:0000269|PubMed:17545469, CC ECO:0000269|PubMed:7565723}. CC -!- INTERACTION: CC Q03957; P46962: CTK2; NbExp=9; IntAct=EBI-5230, EBI-5236; CC Q03957; P46963: CTK3; NbExp=7; IntAct=EBI-5230, EBI-5241; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. CC -!- PTM: Phosphorylated on Thr-338 by CAK1. Phosphorylation is essential CC for the elevated CTD Ser-2 phosphorylation and required to activate CC transcription of stationary-phase genes during the diauxic shift. CC {ECO:0000269|PubMed:15870265}. CC -!- DISRUPTION PHENOTYPE: Null mutants are viable, but grow more slowly CC than wild-type cells at 30 degrees Celsius. They are cold-sensitive, CC failing to grow at 12 degrees Celsius. They display flocculent growth CC in liquid media and they show abnormal cell morphologies, for example, CC a significant fraction of the cells are greatly enlarged. Deletion CC mutant has increased phosphorylation of 'Ser-5' of the CTD repeat CC during logarithmic growth. Deletion eliminates transient increase in CC CTD 'Ser-2' phosphorylation observed during diauxic shift. Deletion CC mutant is synthetically lethal when combined with deletion of DST1 or CC ELP genes. Deletion mutants are modestly sensitive to the uracil analog CC 6-azauracil (6AU), which inhibits elongation by depleting nucleotide CC pools. Deletion mutant is sensitive to the DNA synthesis inhibitor CC hydroxyurea (HU) and UV irradiation. 'Ser-2' phosphorylation within the CC CTD repeats is not increased in deletion mutants upon treatment with CC DNA-damaging agents. {ECO:0000269|PubMed:10488128, CC ECO:0000269|PubMed:11311553, ECO:0000269|PubMed:12684377, CC ECO:0000269|PubMed:7565723}. CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; M69024; AAC41642.1; -; Genomic_DNA. DR EMBL; Z28139; CAA81980.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09023.1; -; Genomic_DNA. DR PIR; S32593; S32593. DR RefSeq; NP_012783.1; NM_001179705.1. DR PDB; 7JV7; X-ray; 1.85 A; A=159-508. DR PDBsum; 7JV7; -. DR AlphaFoldDB; Q03957; -. DR SMR; Q03957; -. DR BioGRID; 33997; 894. DR ComplexPortal; CPX-1710; Carboxy-terminal domain protein kinase complex. DR DIP; DIP-6631N; -. DR IntAct; Q03957; 39. DR MINT; Q03957; -. DR STRING; 4932.YKL139W; -. DR iPTMnet; Q03957; -. DR MaxQB; Q03957; -. DR PaxDb; 4932-YKL139W; -. DR PeptideAtlas; Q03957; -. DR EnsemblFungi; YKL139W_mRNA; YKL139W; YKL139W. DR GeneID; 853718; -. DR KEGG; sce:YKL139W; -. DR AGR; SGD:S000001622; -. DR SGD; S000001622; CTK1. DR VEuPathDB; FungiDB:YKL139W; -. DR eggNOG; KOG0600; Eukaryota. DR GeneTree; ENSGT00940000176088; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; Q03957; -. DR OMA; PSCHEYR; -. DR OrthoDB; 22668at2759; -. DR BioCyc; YEAST:G3O-31916-MONOMER; -. DR BRENDA; 2.7.11.22; 984. DR BRENDA; 2.7.11.23; 984. DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 853718; 4 hits in 13 CRISPR screens. DR PRO; PR:Q03957; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; Q03957; Protein. DR GO; GO:0032806; C:carboxy-terminal domain protein kinase complex; IPI:ComplexPortal. DR GO; GO:0070692; C:CTDK-1 complex; IDA:SGD. DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005654; C:nucleoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:SGD. DR GO; GO:0004672; F:protein kinase activity; HDA:SGD. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central. DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW. DR GO; GO:0031124; P:mRNA 3'-end processing; IDA:ComplexPortal. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:SGD. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IBA:GO_Central. DR GO; GO:0045903; P:positive regulation of translational fidelity; IMP:SGD. DR GO; GO:0006413; P:translational initiation; IMP:SGD. DR CDD; cd07840; STKc_CDK9_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; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF546; CYCLIN-DEPENDENT KINASE 9; 1. DR Pfam; PF12330; Haspin_kinase; 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 3D-structure; ATP-binding; Cytoplasm; DNA damage; Kinase; mRNA processing; KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis; KW Reference proteome; Serine/threonine-protein kinase; Stress response; KW Transcription; Transferase. FT CHAIN 1..528 FT /note="CTD kinase subunit alpha" FT /id="PRO_0000085906" FT DOMAIN 183..469 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..528 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 37..44 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 1..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..104 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..128 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..148 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 499..521 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 306 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 189..197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 14 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 338 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15870265" FT MUTAGEN 324 FT /note="D->N: Cold-sensitive. Sensitive to hydroxyurea and FT UV irradiation. Interferes with ATP-binding." FT /evidence="ECO:0000269|PubMed:12684377, FT ECO:0000269|PubMed:15870265" FT MUTAGEN 338 FT /note="T->A: Cold-sensitive. Abolishes kinase activity. FT Delayed growth at early stationary phase. Shows no increase FT in CTDSer-2 phosphorylation in the transition from rapid FT growth to stationary phase. Has compromised transcriptional FT activation of two stationary-phase genes CTT1 and SPI1." FT /evidence="ECO:0000269|PubMed:15870265" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 182..190 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:7JV7" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 225..234 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:7JV7" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 255..261 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 267..271 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 280..299 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 349..352 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 361..376 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 386..397 FT /evidence="ECO:0007829|PDB:7JV7" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 414..417 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:7JV7" FT TURN 434..436 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 440..449 FT /evidence="ECO:0007829|PDB:7JV7" FT TURN 454..456 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 460..464 FT /evidence="ECO:0007829|PDB:7JV7" FT HELIX 467..470 FT /evidence="ECO:0007829|PDB:7JV7" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:7JV7" SQ SEQUENCE 528 AA; 60501 MW; 9862EB10FD476F6B CRC64; MSYNNGNTYS KSYSRNNKRP LFGKRSPNPQ SLARPPPPKR IRTDSGYQSN MDNISSHRVN SNDQPGHTKS RGNNNLSRYN DTSFQTSSRY QGSRYNNNNT SYENRPKSIK RDETKAEFLS HLPKGPKSVE KSRYNNSSNT SNDIKNGYHA SKYYNHKGQE GRSVIAKKVP VSVLTQQRST SVYLRIMQVG EGTYGKVYKA KNTNTEKLVA LKKLRLQGER EGFPITSIRE IKLLQSFDHP NVSTIKEIMV ESQKTVYMIF EYADNDLSGL LLNKEVQISH SQCKHLFKQL LLGMEYLHDN KILHRDVKGS NILIDNQGNL KITDFGLARK MNSRADYTNR VITLWYRPPE LLLGTTNYGT EVDMWGCGCL LVELFNKTAI FQGSNELEQI ESIFKIMGTP TINSWPTLYD MPWFFMIMPQ QTTKYVNNFS EKFKSVLPSS KCLQLAINLL CYDQTKRFSA TEALQSDYFK EEPKPEPLVL DGLVSCHEYE VKLARKQKRP NILSTNTNNK GNGNSNNNNN NNNDDDDK //