ZRK1_ARATH
ID ZRK1_ARATH Reviewed; 351 AA.
AC Q9SVY5; A0A178VAP6; Q56YF3; U5LR94;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase ZRK1 {ECO:0000303|PubMed:26355215};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein RESISTANCE RELATED KINASE 1 {ECO:0000303|PubMed:24068949};
DE AltName: Full=Quantitative resistance to Xanthomonas campestris pv. campestris 568 {ECO:0000303|PubMed:24068949};
DE Short=Quantitative resistance to Xcc568 {ECO:0000303|PubMed:24068949};
GN Name=ZRK1 {ECO:0000303|PubMed:26355215};
GN Synonyms=QRX3 {ECO:0000303|PubMed:24068949},
GN RKS1 {ECO:0000303|PubMed:24068949};
GN OrderedLocusNames=At3g57710 {ECO:0000312|Araport:AT3G57710};
GN ORFNames=F15B8.100 {ECO:0000312|EMBL:CAB41184.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, VARIANT
RP PHE-211, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Ag-0, cv. Bor-1, cv. Bor-4, cv. CIBC-17, cv. Columbia,
RC cv. Kas-1, cv. KNO-18, cv. Kon, cv. Ler-1, cv. Lov-1, cv. Lov-5, cv. Mt-0,
RC cv. Mz-0, cv. N13 Konchezero, cv. Omo2-1, cv. Omo2-3, cv. Pro-0,
RC cv. Pu2-23, cv. Pu2-7, cv. Ra-0, cv. Sorbo, cv. Tamm-2, cv. Tamm-27,
RC cv. Tsu-1, cv. Ull2-5, cv. Uod-1, cv. Var2-1, cv. Var2-6, cv. Wa-1,
RC cv. Wassilewskija-2, and cv. Wt-5;
RX PubMed=24068949; DOI=10.1371/journal.pgen.1003766;
RA Huard-Chauveau C., Perchepied L., Debieu M., Rivas S., Kroj T., Kars I.,
RA Bergelson J., Roux F., Roby D.;
RT "An atypical kinase under balancing selection confers broad-spectrum
RT disease resistance in Arabidopsis.";
RL PLoS Genet. 9:E1003766-E1003766(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, MUTAGENESIS OF LEU-179, DISRUPTION PHENOTYPE, SUBUNIT,
RP INTERACTION WITH RPP13L4/ZAR1, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=26355215; DOI=10.1016/j.chom.2015.08.004;
RA Wang G., Roux B., Feng F., Guy E., Li L., Li N., Zhang X., Lautier M.,
RA Jardinaud M.-F., Chabannes M., Arlat M., Chen S., He C., Noel L.D.,
RA Zhou J.-M.;
RT "The decoy substrate of a pathogen effector and a pseudokinase specify
RT pathogen-induced modified-self recognition and immunity in plants.";
RL Cell Host Microbe 18:285-295(2015).
RN [7]
RP INDUCTION BY ELEVATED TEMPERATURE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28499073; DOI=10.1111/nph.14585;
RA Wang Z., Cui D., Liu J., Zhao J., Liu C., Xin W., Li Y., Liu N., Ren D.,
RA Tang D., Hu Y.;
RT "Arabidopsis ZED1-related kinases mediate the temperature-sensitive
RT intersection of immune response and growth homeostasis.";
RL New Phytol. 215:711-724(2017).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=30948527; DOI=10.1126/science.aav5870;
RA Wang J., Hu M., Wang J., Qi J., Han Z., Wang G., Qi Y., Wang H.-W.,
RA Zhou J.-M., Chai J.;
RT "Reconstitution and structure of a plant NLR resistosome conferring
RT immunity.";
RL Science 364:0-0(2019).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, MUTAGENESIS OF
RP GLY-27; LEU-31; VAL-35; GLN-68; ASP-69; VAL-70; THR-231; PHE-232; GLY-233;
RP ILE-235 AND HIS-240, SUBUNIT, AND INTERACTION WITH RPP13L4/ZAR1 AND PBL2.
RC STRAIN=cv. Columbia;
RX PubMed=30948526; DOI=10.1126/science.aav5868;
RA Wang J., Wang J., Hu M., Wu S., Qi J., Wang G., Han Z., Qi Y., Gao N.,
RA Wang H.-W., Zhou J.-M., Chai J.;
RT "Ligand-triggered allosteric ADP release primes a plant NLR complex.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: Serine/threonine-protein kinase that confers a broad-spectrum
CC quantitative disease resistance (QDR) to the pathogenic biotrophic
CC bacteria Xanthomonas campestris (e.g. pv. campestris (Xcc), pv.
CC raphani, pv. armoriaceae and pv. incanae) by restricting bacterial
CC spread to the vascular system from the infection site; X.campestris
CC causes black rot disease in crops (PubMed:24068949, PubMed:26355215,
CC PubMed:30948526). Seems to not have any kinase activity
CC (PubMed:24068949). {ECO:0000269|PubMed:24068949,
CC ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:30948526}.
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Component of a stable high-order oligomeric complex made of
CC RKS1 and RPP13L4/ZAR1 which recruits Xanthomonas campestris effector
CC XopAC/AvrAC-mediated uridylylated PBL2 in the presence of ATP to form a
CC wheel-like pentameric resistosome; this complex triggers immunity
CC toward X.campestris in vascular tissues (PubMed:26355215,
CC PubMed:30948527, PubMed:30948526). Interacts with RPP13L4/ZAR1 and
CC uridylylated PBL2 (PubMed:26355215, PubMed:30948526).
CC {ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:30948526,
CC ECO:0000269|PubMed:30948527}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in germinating seeds and
CC at lower levels in adult leaves. {ECO:0000269|PubMed:24068949}.
CC -!- INDUCTION: Induced by elevated temperature (e.g. at 25 degrees
CC Celsius). {ECO:0000269|PubMed:28499073}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to the pathogenic
CC biotrophic bacteria Xanthomonas campestris pv. campestris (Xcc).
CC {ECO:0000269|PubMed:24068949, ECO:0000269|PubMed:26355215}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. ZRK subfamily. {ECO:0000305}.
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DR EMBL; KF363640; AGX29308.1; -; Genomic_DNA.
DR EMBL; KF363645; AGX29312.1; -; Genomic_DNA.
DR EMBL; KF363646; AGX29313.1; -; Genomic_DNA.
DR EMBL; KF363650; AGX29317.1; -; Genomic_DNA.
DR EMBL; KF363652; AGX29319.1; -; Genomic_DNA.
DR EMBL; KF363653; AGX29320.1; -; Genomic_DNA.
DR EMBL; KF363671; AGX29335.1; -; Genomic_DNA.
DR EMBL; KF363674; AGX29337.1; -; Genomic_DNA.
DR EMBL; KF363675; AGX29338.1; -; Genomic_DNA.
DR EMBL; KF363678; AGX29341.1; -; Genomic_DNA.
DR EMBL; KF363680; AGX29343.1; -; Genomic_DNA.
DR EMBL; KF363681; AGX29344.1; -; Genomic_DNA.
DR EMBL; KF363688; AGX29350.1; -; Genomic_DNA.
DR EMBL; KF363689; AGX29351.1; -; Genomic_DNA.
DR EMBL; KF363694; AGX29355.1; -; Genomic_DNA.
DR EMBL; KF363695; AGX29356.1; -; Genomic_DNA.
DR EMBL; KF363699; AGX29360.1; -; Genomic_DNA.
DR EMBL; KF363700; AGX29361.1; -; Genomic_DNA.
DR EMBL; KF363701; AGX29362.1; -; Genomic_DNA.
DR EMBL; KF363702; AGX29363.1; -; Genomic_DNA.
DR EMBL; KF363716; AGX29371.1; -; Genomic_DNA.
DR EMBL; KF363717; AGX29372.1; -; Genomic_DNA.
DR EMBL; KF363720; AGX29375.1; -; Genomic_DNA.
DR EMBL; KF363722; AGX29377.1; -; Genomic_DNA.
DR EMBL; KF363723; AGX29378.1; -; Genomic_DNA.
DR EMBL; KF363725; AGX29380.1; -; Genomic_DNA.
DR EMBL; KF363726; AGX29381.1; -; Genomic_DNA.
DR EMBL; KF363727; AGX29382.1; -; Genomic_DNA.
DR EMBL; KF363730; AGX29385.1; -; Genomic_DNA.
DR EMBL; KF363731; AGX29386.1; -; Genomic_DNA.
DR EMBL; KF363711; AGX29367.1; -; Genomic_DNA.
DR EMBL; AL049660; CAB41184.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79688.1; -; Genomic_DNA.
DR EMBL; AK175129; BAD42892.1; -; mRNA.
DR EMBL; AK175546; BAD43309.1; -; mRNA.
DR EMBL; AK175568; BAD43331.1; -; mRNA.
DR EMBL; AK221369; BAD94258.1; -; mRNA.
DR EMBL; AY085150; AAM61703.1; -; mRNA.
DR PIR; T06749; T06749.
DR RefSeq; NP_191330.1; NM_115631.3.
DR PDB; 6J5T; EM; 3.40 A; B/E/H/K/N=1-351.
DR PDB; 6J5U; EM; 3.90 A; B=1-351.
DR PDB; 6J5V; EM; 4.25 A; B=1-351.
DR PDB; 6J5W; EM; 3.70 A; B=1-351.
DR PDB; 6J6I; EM; 3.70 A; B=1-351.
DR PDBsum; 6J5T; -.
DR PDBsum; 6J5U; -.
DR PDBsum; 6J5V; -.
DR PDBsum; 6J5W; -.
DR PDBsum; 6J6I; -.
DR AlphaFoldDB; Q9SVY5; -.
DR SMR; Q9SVY5; -.
DR STRING; 3702.AT3G57710.1; -.
DR PaxDb; Q9SVY5; -.
DR PRIDE; Q9SVY5; -.
DR ProteomicsDB; 181185; -.
DR EnsemblPlants; AT3G57710.1; AT3G57710.1; AT3G57710.
DR GeneID; 824940; -.
DR Gramene; AT3G57710.1; AT3G57710.1; AT3G57710.
DR KEGG; ath:AT3G57710; -.
DR Araport; AT3G57710; -.
DR TAIR; locus:2076586; AT3G57710.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9SVY5; -.
DR OMA; FECCIPL; -.
DR OrthoDB; 778960at2759; -.
DR PhylomeDB; Q9SVY5; -.
DR PRO; PR:Q9SVY5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SVY5; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR045274; WAK-like.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Plant defense;
KW Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="Serine/threonine-protein kinase ZRK1"
FT /id="PRO_0000449489"
FT DOMAIN 60..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 211
FT /note="S -> F (in strain: cv. Kas-1, cv. Kon and cv. Sorbo;
FT confers sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc))"
FT /evidence="ECO:0000269|PubMed:24068949"
FT MUTAGEN 27
FT /note="G->A: Impaired interaction with RPP13L4/ZAR1 and
FT reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 31
FT /note="L->E: Impaired interaction with RPP13L4/ZAR1 and
FT reduced ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 35
FT /note="V->E: Impaired interaction with RPP13L4/ZAR1 and
FT reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 68
FT /note="Q->Y: Reduced interaction with uridylylated PBL2 and
FT reduced ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 69
FT /note="D->Y: Abolished interaction with uridylylated PBL2
FT and abolished ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 70
FT /note="V->Y: Reduced interaction with uridylylated PBL2 and
FT reduced ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 179
FT /note="L->F: Impaired interaction in the presence of the
FT Xanthomonas campestris effector XopAC/AvrAC, but normal
FT interaction with RPP13L4/ZAR1."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 231
FT /note="T->Y: Abolished interaction with uridylylated PBL2
FT and abolished ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 232
FT /note="F->A: Abolished interaction with uridylylated PBL2
FT and abolished ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 233
FT /note="G->A: Reduced interaction with uridylylated PBL2 and
FT reduced ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 235
FT /note="I->E: Abolished interaction with uridylylated PBL2
FT and abolished ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 240
FT /note="H->E: Abolished interaction with uridylylated PBL2
FT and abolished ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT CONFLICT 123
FT /note="L -> P (in Ref. 4; BAD94258)"
FT /evidence="ECO:0000305"
FT HELIX 19..38
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 308..322
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:6J5T"
SQ SEQUENCE 351 AA; 40086 MW; 8500BAACCFB2E88F CRC64;
MKKQYLKSGS GTRKEKDKAK RWFLDNGSIF LRELVADCNG KSIPIRSFSP EQILKATNNF
DSSCFVSQDV YYKWYRGEIE DRSYMIKRFS EDEITGKRHR VKEVYNDIVL SARMSNHSNF
LQLLGCCLEF PFPVLVFEFA EHGAMNQRGG VIVNGEESLL PWSVRLKIGK EIANAVTYLH
TAFPKIIIHR DVKPMHVFLD KNWTAKLSDL SFSISLPEGK SRIEAEWVLG TFGYIDPLYH
KTCFVTEYTD VYSFGICLLV IITGKPAIMT ISDGDLQGIL SLVRELCENG KLDEVIDPRL
MKDITSGQRL QVEACVVLAL RCCKERDEDR PKMIQVAKEL KQIEASLKNS S
