KAIC_SYNE7
ID KAIC_SYNE7 Reviewed; 519 AA.
AC Q79PF4; Q31NX3; Q9Z3H2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Circadian clock protein kinase KaiC;
DE EC=2.7.11.1;
GN Name=kaiC; OrderedLocusNames=Synpcc7942_1216; ORFNames=see0011;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTANTS KAIC1; KAIC2;
RP KAIC3; KAIC4; KAIC5; KAIC6; KAIC7; KAIC8; KAIC9; KAIC10; KAIC11; KAIC12;
RP KAIC13 AND KAIC14.
RX PubMed=9727980; DOI=10.1126/science.281.5382.1519;
RA Ishiura M., Kutsuna S., Aoki S., Iwasaki H., Andersson C.R., Tanabe A.,
RA Golden S.S., Johnson C.H., Kondo T.;
RT "Expression of a gene cluster kaiABC as a circadian feedback process in
RT cyanobacteria.";
RL Science 281:1519-1523(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S.,
RA Gonzalez A., Salinas I., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 7G3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH KAIA AND KAIB.
RX PubMed=10064581; DOI=10.1093/emboj/18.5.1137;
RA Iwasaki H., Taniguchi Y., Ishiura M., Kondo T.;
RT "Physical interactions among circadian clock proteins KaiA, KaiB and KaiC
RT in cyanobacteria.";
RL EMBO J. 18:1137-1145(1999).
RN [5]
RP ATP-BINDING, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-52; GLY-71;
RP GLY-114; GLN-115 AND LYS-294.
RX PubMed=10618446; DOI=10.1073/pnas.97.1.495;
RA Nishiwaki T., Iwasaki H., Ishiura M., Kondo T.;
RT "Nucleotide binding and autophosphorylation of the clock protein KaiC as a
RT circadian timing process of cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:495-499(2000).
RN [6]
RP INTERACTION WITH SASA.
RX PubMed=10786837; DOI=10.1016/s0092-8674(00)80832-6;
RA Iwasaki H., Williams S.B., Kitayama Y., Ishiura M., Golden S.S., Kondo T.;
RT "A kaiC-interacting sensory histidine kinase, SasA, necessary to sustain
RT robust circadian oscillation in cyanobacteria.";
RL Cell 101:223-233(2000).
RN [7]
RP INTERACTION WITH KAIA, AND MUTANTS KAIC3; KAIC6; KAIC11 AND KAIC12.
RX PubMed=11356188; DOI=10.1016/s0014-5793(01)02408-5;
RA Taniguchi Y., Yamaguchi A., Hijikata A., Iwasaki H., Kamagata K.,
RA Ishiura M., Go M., Kondo T.;
RT "Two KaiA-binding domains of cyanobacterial circadian clock protein KaiC.";
RL FEBS Lett. 496:86-90(2001).
RN [8]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND MUTANT KAIC15.
RX PubMed=12391300; DOI=10.1073/pnas.222467299;
RA Iwasaki H., Nishiwaki T., Kitayama Y., Nakajima M., Kondo T.;
RT "KaiA-stimulated KaiC phosphorylation in circadian timing loops in
RT cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15788-15793(2002).
RN [9]
RP HEXAMERIZATION, DNA-BINDING, AND ATP-BINDING.
RX PubMed=12477935; DOI=10.1073/pnas.262578499;
RA Mori T., Saveliev S.V., Xu Y., Stafford W.F., Cox M.M., Inman R.B.,
RA Johnson C.H.;
RT "Circadian clock protein KaiC forms ATP-dependent hexameric rings and binds
RT DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17203-17208(2002).
RN [10]
RP ACTIVITY REGULATION, PHOSPHORYLATION, AND INTERACTION WITH KAIB.
RX PubMed=12727878; DOI=10.1093/emboj/cdg168;
RA Xu Y., Mori T., Johnson C.H.;
RT "Cyanobacterial circadian clockwork: roles of KaiA, KaiB and the kaiBC
RT promoter in regulating KaiC.";
RL EMBO J. 22:2117-2126(2003).
RN [11]
RP ACTIVITY REGULATION, PHOSPHORYLATION, AND INTERACTION WITH KAIB.
RX PubMed=12727879; DOI=10.1093/emboj/cdg212;
RA Kitayama Y., Iwasaki H., Nishiwaki T., Kondo T.;
RT "KaiB functions as an attenuator of KaiC phosphorylation in the
RT cyanobacterial circadian clock system.";
RL EMBO J. 22:2127-2134(2003).
RN [12]
RP FUNCTION OF THE KAIABC COMPLEX, AND INDUCTION.
RX PubMed=14709675; DOI=10.1073/pnas.0307411100;
RA Nakahira Y., Katayama M., Miyashita H., Kutsuna S., Iwasaki H., Oyama T.,
RA Kondo T.;
RT "Global gene repression by KaiC as a master process of prokaryotic
RT circadian system.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:881-885(2004).
RN [13]
RP STOICHIOMETRY OF THE COMPLEX FORMED WITH KAIA.
RX PubMed=15003530; DOI=10.1016/j.bbrc.2004.02.034;
RA Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M.;
RT "Stoichiometric interactions between cyanobacterial clock proteins KaiA and
RT KaiC.";
RL Biochem. Biophys. Res. Commun. 316:195-202(2004).
RN [14]
RP DEVELOPMENTAL STAGE.
RX PubMed=15229218; DOI=10.1074/jbc.m405861200;
RA Imai K., Nishiwaki T., Kondo T., Iwasaki H.;
RT "Circadian rhythms in the synthesis and degradation of a master clock
RT protein kaiC in cyanobacteria.";
RL J. Biol. Chem. 279:36534-36539(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF HEXAMER, COFACTOR, PHOSPHORYLATION
RP AT THR-432, AND MUTAGENESIS OF THR-432.
RX PubMed=15304218; DOI=10.1016/j.molcel.2004.07.013;
RA Pattanayek R., Wang J., Mori T., Xu Y., Johnson C.H., Egli M.;
RT "Visualizing a circadian clock protein; crystal structure of kaiC and
RT functional insights.";
RL Mol. Cell 15:375-388(2004).
CC -!- FUNCTION: Core component of the KaiABC clock protein complex, which
CC constitutes the main circadian regulator in cyanobacteria. Binds to
CC DNA. The KaiABC complex may act as a promoter-nonspecific transcription
CC regulator that represses transcription, possibly by acting on the state
CC of chromosome compaction. {ECO:0000269|PubMed:14709675,
CC ECO:0000269|PubMed:9727980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15304218};
CC -!- ACTIVITY REGULATION: The interaction with KaiA enhances its
CC phosphorylation status, while the interaction with KaiB decreases it. A
CC KaiA dimer is sufficient to enhance KaiC phosphorylation.
CC {ECO:0000269|PubMed:12391300, ECO:0000269|PubMed:12727878,
CC ECO:0000269|PubMed:12727879}.
CC -!- SUBUNIT: Homohexamer; hexamerization is dependent on ATP-binding. Core
CC component of the KaiABC complex, at least composed of a KaiC
CC homohexamer, a KaiB dimer and two KaiA dimers. Interacts directly with
CC SasA. {ECO:0000269|PubMed:10064581, ECO:0000269|PubMed:10786837,
CC ECO:0000269|PubMed:11356188, ECO:0000269|PubMed:12727878,
CC ECO:0000269|PubMed:12727879}.
CC -!- INTERACTION:
CC Q79PF4; Q79PF6: kaiA; NbExp=22; IntAct=EBI-592287, EBI-592281;
CC Q79PF4; Q79PF5: kaiB; NbExp=12; IntAct=EBI-592287, EBI-619150;
CC Q79PF4; Q79PF4: kaiC; NbExp=12; IntAct=EBI-592287, EBI-592287;
CC Q79PF4; Q06904: sasA; NbExp=6; IntAct=EBI-592287, EBI-626872;
CC -!- DEVELOPMENTAL STAGE: Accumulates in a circadian fashion, peaking at
CC circadian time (CT) 15-18. {ECO:0000269|PubMed:15229218}.
CC -!- INDUCTION: Down-regulated by itself. {ECO:0000269|PubMed:14709675}.
CC -!- DOMAIN: The KaiC domains mediate the interaction with KaiA.
CC -!- PTM: Phosphorylated on serine/threonine residues by autocatalysis. Both
CC phosphorylated and unphosphorylated forms exist. Can probably
CC autophosphorylate and autodephosphorylate. Phosphorylated form
CC correlates with clock speed. {ECO:0000269|PubMed:12391300,
CC ECO:0000269|PubMed:12727878, ECO:0000269|PubMed:12727879}.
CC -!- MISCELLANEOUS: 'Kai' means 'cycle' in Japanese.
CC -!- SIMILARITY: Belongs to the KaiC family. {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; AB010691; BAA37103.1; -; Genomic_DNA.
DR EMBL; AY120853; AAM82686.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57246.1; -; Genomic_DNA.
DR PIR; T44269; T44269.
DR RefSeq; WP_011242648.1; NC_007604.1.
DR PDB; 1TF7; X-ray; 2.80 A; A/B/C/D/E/F=1-519.
DR PDB; 1U9I; X-ray; 2.80 A; A/B/C/D/E/F=1-519.
DR PDB; 2GBL; X-ray; 2.80 A; A/B/C/D/E/F=1-519.
DR PDB; 3DVL; X-ray; 2.80 A; A/B/C/D/E/F=1-519.
DR PDB; 3JZM; X-ray; 2.90 A; A/B/C/D/E/F=1-519.
DR PDB; 3K09; X-ray; 3.20 A; A/B/C/D/E/F=1-519.
DR PDB; 3K0A; X-ray; 3.00 A; A/B/C/D/E/F=1-519.
DR PDB; 3K0C; X-ray; 3.30 A; A/B/C/D/E/F=1-519.
DR PDB; 3K0E; X-ray; 3.20 A; A/B/C/D/E/F=1-519.
DR PDB; 3K0F; X-ray; 3.00 A; A/B/C/D/E/F=1-519.
DR PDB; 3S1A; X-ray; 3.00 A; A/B/C/D/E/F=1-519.
DR PDB; 4DUG; X-ray; 3.30 A; A/B/C/D/E/F=1-519.
DR PDB; 4IJM; X-ray; 3.35 A; A/B/C/D/E/F=14-519.
DR PDB; 4TL6; X-ray; 1.76 A; A/B/C=1-253.
DR PDB; 4TL7; X-ray; 1.94 A; A/B/C/D/E/F=1-253.
DR PDB; 4TL8; X-ray; 1.86 A; A/B/C/D/E/F=1-253.
DR PDB; 4TL9; X-ray; 1.82 A; A/B/C/D/E/F=1-253.
DR PDB; 4TLA; X-ray; 1.80 A; A/B/C/D/E/F=1-253.
DR PDB; 4TLB; X-ray; 1.98 A; A/B/C/D/E/F=1-253.
DR PDB; 4TLC; X-ray; 2.09 A; A/B/C/D/E/F=1-253.
DR PDB; 4TLD; X-ray; 1.95 A; A/B/C/D/E/F=1-253.
DR PDB; 4TLE; X-ray; 1.94 A; A/B/C/D/E/F=1-253.
DR PDB; 5C5E; X-ray; 2.82 A; G/H=500-519.
DR PDB; 5N8Y; EM; 4.70 A; A/B/C/D/E/F=1-519.
DR PDB; 5YZ8; X-ray; 2.81 A; A/B/C/D/E/F=1-254.
DR PDB; 7S65; EM; 3.20 A; A/B/C/D/E/F=1-519.
DR PDB; 7S66; EM; 2.80 A; A/B/C/D/E/F=1-519.
DR PDB; 7S67; EM; 3.80 A; A/B/C/D/E/F=1-519.
DR PDBsum; 1TF7; -.
DR PDBsum; 1U9I; -.
DR PDBsum; 2GBL; -.
DR PDBsum; 3DVL; -.
DR PDBsum; 3JZM; -.
DR PDBsum; 3K09; -.
DR PDBsum; 3K0A; -.
DR PDBsum; 3K0C; -.
DR PDBsum; 3K0E; -.
DR PDBsum; 3K0F; -.
DR PDBsum; 3S1A; -.
DR PDBsum; 4DUG; -.
DR PDBsum; 4IJM; -.
DR PDBsum; 4TL6; -.
DR PDBsum; 4TL7; -.
DR PDBsum; 4TL8; -.
DR PDBsum; 4TL9; -.
DR PDBsum; 4TLA; -.
DR PDBsum; 4TLB; -.
DR PDBsum; 4TLC; -.
DR PDBsum; 4TLD; -.
DR PDBsum; 4TLE; -.
DR PDBsum; 5C5E; -.
DR PDBsum; 5N8Y; -.
DR PDBsum; 5YZ8; -.
DR PDBsum; 7S65; -.
DR PDBsum; 7S66; -.
DR PDBsum; 7S67; -.
DR AlphaFoldDB; Q79PF4; -.
DR SASBDB; Q79PF4; -.
DR SMR; Q79PF4; -.
DR DIP; DIP-33330N; -.
DR IntAct; Q79PF4; 3.
DR MINT; Q79PF4; -.
DR STRING; 1140.Synpcc7942_1216; -.
DR iPTMnet; Q79PF4; -.
DR PRIDE; Q79PF4; -.
DR EnsemblBacteria; ABB57246; ABB57246; Synpcc7942_1216.
DR KEGG; syf:Synpcc7942_1216; -.
DR eggNOG; COG0467; Bacteria.
DR HOGENOM; CLU_023669_4_1_3; -.
DR OMA; MGSHSIT; -.
DR OrthoDB; 271085at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1216-MON; -.
DR EvolutionaryTrace; Q79PF4; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
DR GO; GO:0009649; P:entrainment of circadian clock; IDA:UniProtKB.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:CACAO.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0070297; P:regulation of phosphorelay signal transduction system; IDA:CACAO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01836; KaiC; 1.
DR InterPro; IPR013503; Circadian_KaiC_bact.
DR InterPro; IPR030665; KaiC.
DR InterPro; IPR014774; KaiC-like_dom.
DR InterPro; IPR010624; KaiC_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF06745; ATPase; 2.
DR PIRSF; PIRSF039117; KaiC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR02655; circ_KaiC; 1.
DR PROSITE; PS51146; KAIC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biological rhythms; DNA-binding; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW Repressor; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..519
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217782"
FT DOMAIN 19..260
FT /note="KaiC 1"
FT DOMAIN 261..493
FT /note="KaiC 2"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 288..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 432
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15304218"
FT MUTAGEN 52
FT /note="K->A: Induces an arrhythmic phenotype."
FT /evidence="ECO:0000269|PubMed:10618446"
FT MUTAGEN 71
FT /note="G->A: Lowers the amplitude and distords the waveform
FT of the circadian rhythm."
FT /evidence="ECO:0000269|PubMed:10618446"
FT MUTAGEN 87
FT /note="A->V: In kaiC1; shortens the period of the circadian
FT rhythm to 22 hours."
FT MUTAGEN 114
FT /note="G->A: Extends the period of the circadian rhythm to
FT 27 hours."
FT /evidence="ECO:0000269|PubMed:10618446"
FT MUTAGEN 115
FT /note="Q->A: Abolishes the circadian rhythm."
FT /evidence="ECO:0000269|PubMed:10618446"
FT MUTAGEN 157
FT /note="S->C: In kaiC2; extends the period of the circadian
FT rhythm to 29 hours."
FT MUTAGEN 215
FT /note="R->C: In kaiC3; shortens the period of the circadian
FT rhythm to 16 hours and decreases the interaction with
FT KaiA."
FT MUTAGEN 236
FT /note="P->S: In kaiC4; extends the period of the circadian
FT rhythm to 28 hours."
FT MUTAGEN 248
FT /note="P->L: In kaiC6; induces a low amplitude phenotype
FT and decreases the interaction with KaiA."
FT MUTAGEN 248
FT /note="P->S: In kaiC5; induces an arrhythmic phenotype."
FT MUTAGEN 253
FT /note="R->H: In kaiC7; extends the period of the circadian
FT rhythm to 40 hours."
FT MUTAGEN 273
FT /note="M->I: In kaiC8; extends the period of the circadian
FT rhythm to 37 hours."
FT MUTAGEN 294
FT /note="K->A: Induces a long period phenotype."
FT /evidence="ECO:0000269|PubMed:10618446"
FT MUTAGEN 321
FT /note="R->Q: In kaiC9; shortens the period of the circadian
FT rhythm to 21 hours."
FT MUTAGEN 409
FT /note="T->A: In kaiC10; extends the period of the circadian
FT rhythm to 27 hours."
FT MUTAGEN 421
FT /note="G->R: In kaiC11; extends the period of the circadian
FT rhythm to 44 hours and increases the interaction with
FT KaiA."
FT MUTAGEN 422
FT /note="A->T: In kaiC15; able to suppress the kaiA2 extended
FT phenotype."
FT MUTAGEN 432
FT /note="T->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15304218"
FT MUTAGEN 442
FT /note="Y->H: In kaiC12; extends the period of the circadian
FT rhythm to 60 hours and increases the interaction with
FT KaiA."
FT MUTAGEN 460
FT /note="G->E: In kaiC13; induces an arrhythmic phenotype."
FT MUTAGEN 495
FT /note="T->A: In kaiC14; induces an arrhythmic phenotype."
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:4TL6"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:4TL6"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:4TL6"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4TL6"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1U9I"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4TL6"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:4TL6"
FT HELIX 157..174
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4TL7"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:4TLA"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7S65"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4TL6"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:4TL6"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:1TF7"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:1TF7"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:7S66"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1TF7"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:3K0A"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 435..445
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 448..461
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:1TF7"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:3K0F"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:3K0A"
FT HELIX 501..512
FT /evidence="ECO:0007829|PDB:5C5E"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:2GBL"
SQ SEQUENCE 519 AA; 58003 MW; 855DFE131EFFF3CF CRC64;
MTSAEMTSPN NNSEHQAIAK MRTMIEGFDD ISHGGLPIGR STLVSGTSGT GKTLFSIQFL
YNGIIEFDEP GVFVTFEETP QDIIKNARSF GWDLAKLVDE GKLFILDASP DPEGQEVVGG
FDLSALIERI NYAIQKYRAR RVSIDSVTSV FQQYDASSVV RRELFRLVAR LKQIGATTVM
TTERIEEYGP IARYGVEEFV SDNVVILRNV LEGERRRRTL EILKLRGTSH MKGEYPFTIT
DHGINIFPLG AMRLTQRSSN VRVSSGVVRL DEMCGGGFFK DSIILATGAT GTGKTLLVSR
FVENACANKE RAILFAYEES RAQLLRNAYS WGMDFEEMER QNLLKIVCAY PESAGLEDHL
QIIKSEINDF KPARIAIDSL SALARGVSNN AFRQFVIGVT GYAKQEEITG LFTNTSDQFM
GAHSITDSHI STITDTIILL QYVEIRGEMS RAINVFKMRG SWHDKAIREF MISDKGPDIK
DSFRNFERII SGSPTRITVD EKSELSRIVR GVQEKGPES
