CTK1_YEAST
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 03-AUG-2022, entry version 205.
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}.
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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; 889.
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; Q03957; -.
DR PRIDE; Q03957; -.
DR EnsemblFungi; YKL139W_mRNA; YKL139W; YKL139W.
DR GeneID; 853718; -.
DR KEGG; sce:YKL139W; -.
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; CHEYEVK; -.
DR BioCyc; YEAST:G3O-31916-MON; -.
DR BRENDA; 2.7.11.22; 984.
DR BRENDA; 2.7.11.23; 984.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
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:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
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:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0031124; P:mRNA 3'-end processing; IDA:ComplexPortal.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IMP:SGD.
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 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 CTD Ser-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
