KIN28_YEAST
ID KIN28_YEAST Reviewed; 306 AA.
AC P06242; D6VRP2;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Serine/threonine-protein kinase KIN28;
DE EC=2.7.11.23;
GN Name=KIN28; OrderedLocusNames=YDL108W; ORFNames=D2330;
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=3536482; DOI=10.1002/j.1460-2075.1986.tb04553.x;
RA Simon M., Seraphin B., Faye G.;
RT "KIN28, a yeast split gene coding for a putative protein kinase homologous
RT to CDC28.";
RL EMBO J. 5:2697-2701(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896274;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1077::aid-yea8>3.0.co;2-z;
RA Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT genes, and six new open reading frames.";
RL Yeast 12:1077-1084(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP INTERACTION WITH CCL1.
RX PubMed=8230216; DOI=10.1006/jmbi.1993.1587;
RA Valay J.G., Simon M., Faye G.;
RT "The kin28 protein kinase is associated with a cyclin in Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 234:307-310(1993).
RN [6]
RP SUBUNIT, AND INTERACTION WITH TFB3.
RC STRAIN=DBY2019;
RX PubMed=9235928; DOI=10.1074/jbc.272.31.19319;
RA Feaver W.J., Henry N.L., Wang Z., Wu X., Svejstrup J.Q., Bushnell D.A.,
RA Friedberg E.C., Kornberg R.D.;
RT "Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair
RT factor IIH. Homology to human cyclin-dependent kinase activating kinase and
RT IIH subunits.";
RL J. Biol. Chem. 272:19319-19327(1997).
RN [7]
RP PHOSPHORYLATION AT THR-162, AND MUTAGENESIS OF THR-162.
RX PubMed=9774652; DOI=10.1128/mcb.18.11.6365;
RA Espinoza F.H., Farrell A., Nourse J.L., Chamberlin H.M., Gileadi O.,
RA Morgan D.O.;
RT "Cak1 is required for Kin28 phosphorylation and activation in vivo.";
RL Mol. Cell. Biol. 18:6365-6373(1998).
RN [8]
RP PHOSPHORYLATION AT THR-162, AND MUTAGENESIS OF ASP-147; 17-THR-TYR-18 AND
RP THR-162.
RX PubMed=10373527; DOI=10.1128/mcb.19.7.4774;
RA Kimmelman J., Kaldis P., Hengartner C.J., Laff G.M., Koh S.S., Young R.A.,
RA Solomon M.J.;
RT "Activating phosphorylation of the Kin28p subunit of yeast TFIIH by
RT Cak1p.";
RL Mol. Cell. Biol. 19:4774-4787(1999).
RN [9]
RP INTERACTION WITH HNT1.
RX PubMed=10958787; DOI=10.1074/jbc.c000505200;
RA Korsisaari N., Makela T.P.;
RT "Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad
RT proteins.";
RL J. Biol. Chem. 275:34837-34840(2000).
RN [10]
RP FUNCTION.
RX PubMed=10594013; DOI=10.1128/mcb.20.1.104-112.2000;
RA Rodriguez C.R., Cho E.-J., Keogh M.-C., Moore C.L., Greenleaf A.L.,
RA Buratowski S.;
RT "Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates
RT the recruitment of mRNA processing machinery to RNA polymerase II.";
RL Mol. Cell. Biol. 20:104-112(2000).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH CCL1 AND TFB3, PHOSPHORYLATION AT THR-162,
RP AND MUTAGENESIS OF THR-17; LYS-36; GLU-54; ASP-147; THR-162 AND SER-163.
RX PubMed=11839796; DOI=10.1128/mcb.22.5.1288-1297.2002;
RA Keogh M.-C., Cho E.-J., Podolny V., Buratowski S.;
RT "Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex with
RT differential sensitivities to T-loop phosphorylation.";
RL Mol. Cell. Biol. 22:1288-1297(2002).
RN [12]
RP INTERACTION WITH HOG1.
RX PubMed=12743037; DOI=10.1093/emboj/cdg243;
RA Alepuz P.M., de Nadal E., Zapater M., Ammerer G., Posas F.;
RT "Osmostress-induced transcription by Hot1 depends on a Hog1-mediated
RT recruitment of the RNA Pol II.";
RL EMBO J. 22:2433-2442(2003).
RN [13]
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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Catalytic component of the TFIIK complex (KIN28-CCL1 dimer)
CC which is the protein kinase component of transcription factor IIH
CC (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II
CC during transition from transcription to elongation after preinitiation
CC complex (PIC) formation, thereby positively regulating transcription.
CC TFIIH (or factor B) is essential for both basal and activated
CC transcription, and is involved in nucleotide excision repair (NER) of
CC damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential
CC for polymerase II transcription in vitro. Essential for cell
CC proliferation. {ECO:0000269|PubMed:10594013}.
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: CCL1 and KIN28 form the TFIIK complex, a component of the
CC TFIIH holo complex. Component of a complex consisting of KIN28, CCL1
CC and TFB3. Interacts with TFB3. Also interacts with HNT1 and HOG1.
CC {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:11839796,
CC ECO:0000269|PubMed:12743037, ECO:0000269|PubMed:8230216,
CC ECO:0000269|PubMed:9235928}.
CC -!- INTERACTION:
CC P06242; P37366: CCL1; NbExp=7; IntAct=EBI-9691, EBI-4385;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylation of Thr-162 regulates the affinity of interaction
CC between CCL1, KIN28 and TFB3. Thr-162 phosphorylation does not vary
CC through the cell cycle and is necessary for full kinase activity.
CC {ECO:0000269|PubMed:10373527, ECO:0000269|PubMed:11839796,
CC ECO:0000269|PubMed:9774652}.
CC -!- MISCELLANEOUS: Present with 4400 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; X04423; CAA28019.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64904.1; -; Genomic_DNA.
DR EMBL; Z74156; CAA98675.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11752.1; -; Genomic_DNA.
DR PIR; A25698; A25698.
DR RefSeq; NP_010175.1; NM_001180167.1.
DR PDB; 6XI8; EM; 3.64 A; A=3-303.
DR PDB; 7KUE; EM; 3.50 A; A=1-306.
DR PDBsum; 6XI8; -.
DR PDBsum; 7KUE; -.
DR AlphaFoldDB; P06242; -.
DR SMR; P06242; -.
DR BioGRID; 31954; 554.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR ComplexPortal; CPX-1660; General transcription factor complex TFIIK.
DR DIP; DIP-2259N; -.
DR IntAct; P06242; 13.
DR MINT; P06242; -.
DR STRING; 4932.YDL108W; -.
DR BindingDB; P06242; -.
DR ChEMBL; CHEMBL5370; -.
DR iPTMnet; P06242; -.
DR MaxQB; P06242; -.
DR PaxDb; P06242; -.
DR PRIDE; P06242; -.
DR EnsemblFungi; YDL108W_mRNA; YDL108W; YDL108W.
DR GeneID; 851450; -.
DR KEGG; sce:YDL108W; -.
DR SGD; S000002266; KIN28.
DR VEuPathDB; FungiDB:YDL108W; -.
DR eggNOG; KOG0659; Eukaryota.
DR GeneTree; ENSGT00940000155179; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P06242; -.
DR OMA; LLMSMCA; -.
DR BioCyc; YEAST:G3O-29509-MON; -.
DR BRENDA; 2.7.11.22; 984.
DR BRENDA; 2.7.11.23; 984.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SCE-69231; Cyclin D associated events in G1.
DR Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:P06242; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P06242; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:SGD.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:1901921; P:phosphorylation of RNA polymerase II C-terminal domain involved in recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex; IMP:SGD.
DR GO; GO:1903654; P:phosphorylation of RNA polymerase II C-terminal domain serine 5 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:1900018; P:phosphorylation of RNA polymerase II C-terminal domain serine 5 residues involved in recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex; IMP:SGD.
DR GO; GO:1905866; P:positive regulation of Atg1/ULK1 kinase complex assembly; IMP:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR CDD; cd07841; STKc_CDK7; 1.
DR InterPro; IPR037770; CDK7.
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; Cell cycle; Cell division; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..306
FT /note="Serine/threonine-protein kinase KIN28"
FT /id="PRO_0000086132"
FT DOMAIN 7..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 162
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000269|PubMed:10373527,
FT ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:9774652"
FT MUTAGEN 17..18
FT /note="TY->AF: No effect on phosphorylation; no effect on
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:10373527"
FT MUTAGEN 17
FT /note="T->D: Slow growth."
FT /evidence="ECO:0000269|PubMed:11839796"
FT MUTAGEN 17
FT /note="T->E,Q,V: Normal growth."
FT /evidence="ECO:0000269|PubMed:11839796"
FT MUTAGEN 36
FT /note="K->A: Slow growth."
FT /evidence="ECO:0000269|PubMed:11839796"
FT MUTAGEN 54
FT /note="E->Q: Non-viable."
FT /evidence="ECO:0000269|PubMed:11839796"
FT MUTAGEN 147
FT /note="D->N: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:10373527,
FT ECO:0000269|PubMed:11839796"
FT MUTAGEN 162
FT /note="T->A: Diminishes phosphorylation; 75-80% loss in
FT kinase activity; no effect on survival."
FT /evidence="ECO:0000269|PubMed:10373527,
FT ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:9774652"
FT MUTAGEN 162
FT /note="T->S,D,E: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:10373527,
FT ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:9774652"
FT MUTAGEN 163
FT /note="S->A: Normal growth."
FT /evidence="ECO:0000269|PubMed:11839796"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 105..122
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:7KUE"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:7KUE"
SQ SEQUENCE 306 AA; 35247 MW; 763A5720A1D9ACF3 CRC64;
MKVNMEYTKE KKVGEGTYAV VYLGCQHSTG RKIAIKEIKT SEFKDGLDMS AIREVKYLQE
MQHPNVIELI DIFMAYDNLN LVLEFLPTDL EVVIKDKSIL FTPADIKAWM LMTLRGVYHC
HRNFILHRDL KPNNLLFSPD GQIKVADFGL ARAIPAPHEI LTSNVVTRWY RAPELLFGAK
HYTSAIDIWS VGVIFAELML RIPYLPGQND VDQMEVTFRA LGTPTDRDWP EVSSFMTYNK
LQIYPPPSRD ELRKRFIAAS EYALDFMCGM LTMNPQKRWT AVQCLESDYF KELPPPSDPS
SIKIRN
