ID PBS1_ARATH Reviewed; 456 AA.
AC Q9FE20;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase PBS1 {ECO:0000303|PubMed:11359614};
DE EC=2.7.11.1 {ECO:0000269|PubMed:11359614};
DE AltName: Full=AvrPphB susceptible protein 1 {ECO:0000303|PubMed:11359614};
GN Name=PBS1 {ECO:0000303|PubMed:11359614};
GN OrderedLocusNames=At5g13160 {ECO:0000312|Araport:AT5G13160};
GN ORFNames=T19L5.120 {ECO:0000312|EMBL:CAC05444.1};
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 [MRNA], FUNCTION, ENZYME ACTIVITY, AUTOPHOSPHORYLATION,
RP MUTANT PBS1-2, AND MUTAGENESIS OF GLY-252.
RX PubMed=11359614; DOI=10.1046/j.1365-313x.2001.01014.x;
RA Swiderski M.R., Innes R.W.;
RT "The Arabidopsis PBS1 resistance gene encodes a member of a novel protein
RT kinase subfamily.";
RL Plant J. 26:101-112(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CLEAVAGE, INTERACTION WITH AVRPPHB, AND
RP MUTAGENESIS OF LYS-115; GLY-241; ASP-242 AND LYS-243.
RX PubMed=12947197; DOI=10.1126/science.1085671;
RA Shao F., Golstein C., Ade J., Stoutemyer M., Dixon J.E., Innes R.W.;
RT "Cleavage of Arabidopsis PBS1 by a bacterial type III effector.";
RL Science 301:1230-1233(2003).
RN [6]
RP FUNCTION, INTERACTION WITH RPS5, AND MUTAGENESIS OF LYS-115 AND GLY-252.
RX PubMed=17277084; DOI=10.1073/pnas.0608779104;
RA Ade J., DeYoung B.J., Golstein C., Innes R.W.;
RT "Indirect activation of a plant nucleotide binding site-leucine-rich repeat
RT protein by a bacterial protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2531-2536(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP INTERACTION WITH FLS2, DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION BY
RP FLAGELLIN.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
RN [9]
RP FUNCTION, INTERACTION WITH RPS5, AND MUTAGENESIS OF LYS-115 AND GLY-252.
RX PubMed=22372664; DOI=10.1111/j.1462-5822.2012.01779.x;
RA DeYoung B.J., Qi D., Kim S.H., Burke T.P., Innes R.W.;
RT "Activation of a plant nucleotide binding-leucine rich repeat disease
RT resistance protein by a modified self protein.";
RL Cell. Microbiol. 14:1071-1084(2012).
RN [10]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3; PHE-4 AND CYS-6, AND
RP MYRISTOYLATION AT GLY-2.
RX PubMed=22046960; DOI=10.1094/mpmi-11-10-0272;
RA Takemoto D., Rafiqi M., Hurley U., Lawrence G.J., Bernoux M., Hardham A.R.,
RA Ellis J.G., Dodds P.N., Jones D.A.;
RT "N-terminal motifs in some plant disease resistance proteins function in
RT membrane attachment and contribute to disease resistance.";
RL Mol. Plant Microbe Interact. 25:379-392(2012).
RN [11]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3; CYS-6; GLY-98; GLY-103;
RP SER-244 AND GLY-286, PALMITOYLATION AT CYS-3 AND CYS-6, AND MOTIF.
RX PubMed=24225654; DOI=10.1104/pp.113.227686;
RA Qi D., Dubiella U., Kim S.H., Sloss D.I., Dowen R.H., Dixon J.E.,
RA Innes R.W.;
RT "Recognition of the protein kinase AVRPPHB SUSCEPTIBLE1 by the disease
RT resistance protein RESISTANCE TO PSEUDOMONAS SYRINGAE5 is dependent on s-
RT acylation and an exposed loop in AVRPPHB SUSCEPTIBLE1.";
RL Plant Physiol. 164:340-351(2014).
CC -!- FUNCTION: Protein kinase required for plant defense mechanism mediated
CC by the disease resistance (R) protein RPS5. In case of infection by
CC Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism
CC via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB
CC are independently required to trigger the RPS5-mediated resistance.
CC Contributes to PAMP-triggered immunity (PTI) signaling and defense
CC responses downstream of FLS2. {ECO:0000269|PubMed:11359614,
CC ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084,
CC ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:22372664}.
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:0000269|PubMed:11359614};
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:0000269|PubMed:11359614};
CC -!- SUBUNIT: In infected plant cells, it interacts with the P.syringae
CC virulence protein avrPphB. In uninfected plants, autophosphorylated
CC form interacts with RPS5. Interacts with FLS2.
CC {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084,
CC ECO:0000269|PubMed:20413097}.
CC -!- INTERACTION:
CC Q9FE20; O64973: RPS5; NbExp=2; IntAct=EBI-2357898, EBI-15620767;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor
CC {ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:24225654}.
CC -!- INDUCTION: Induced by flagellin (flg22). {ECO:0000269|PubMed:20413097}.
CC -!- PTM: Cleaved by avrPphB in infected plant cells. Its cleavage serves as
CC a signal that triggers the RPS5-mediated defense system.
CC {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084}.
CC -!- PTM: Autophosphorylates (Probable). Autophosphorylation may be required
CC to trigger the RPS5-mediated plant defense system. {ECO:0000305}.
CC -!- PTM: Palmitoylation at Cys-3 and Cys-6 are required for plasma membrane
CC location that is essential for the RPS5-mediated plant defense
CC response. {ECO:0000269|PubMed:24225654}.
CC -!- DISRUPTION PHENOTYPE: Reduction in H(2)O(2) accumulation and callose
CC deposits. {ECO:0000269|PubMed:20413097}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AF314176; AAG38109.1; -; mRNA.
DR EMBL; AL391711; CAC05444.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91858.1; -; Genomic_DNA.
DR EMBL; AF372927; AAK50067.1; -; mRNA.
DR EMBL; AY078037; AAL77738.1; -; mRNA.
DR RefSeq; NP_196820.1; NM_121319.5.
DR AlphaFoldDB; Q9FE20; -.
DR SMR; Q9FE20; -.
DR BioGRID; 16433; 2.
DR DIP; DIP-53310N; -.
DR IntAct; Q9FE20; 3.
DR STRING; 3702.Q9FE20; -.
DR iPTMnet; Q9FE20; -.
DR SwissPalm; Q9FE20; -.
DR PaxDb; 3702-AT5G13160-1; -.
DR ProteomicsDB; 236798; -.
DR EnsemblPlants; AT5G13160.1; AT5G13160.1; AT5G13160.
DR GeneID; 831155; -.
DR Gramene; AT5G13160.1; AT5G13160.1; AT5G13160.
DR KEGG; ath:AT5G13160; -.
DR Araport; AT5G13160; -.
DR TAIR; AT5G13160; PBS1.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_0_1; -.
DR InParanoid; Q9FE20; -.
DR OMA; DENNQHI; -.
DR OrthoDB; 2999496at2759; -.
DR PhylomeDB; Q9FE20; -.
DR PRO; PR:Q9FE20; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FE20; baseline and differential.
DR Genevisible; Q9FE20; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR CDD; cd14066; STKc_IRAK; 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; PTHR47985; OS07G0668900 PROTEIN; 1.
DR PANTHER; PTHR47985:SF44; SERINE_THREONINE-PROTEIN KINASE PBS1; 1.
DR Pfam; PF00069; Pkinase; 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 ATP-binding; Cell membrane; Direct protein sequencing; Kinase; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:22046960"
FT CHAIN 2..456
FT /note="Serine/threonine-protein kinase PBS1"
FT /id="PRO_0000086482"
FT DOMAIN 86..363
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 292..296
FT /note="Recognition motif required for RPS5-mediated plant
FT resistance to P.syringae"
FT /evidence="ECO:0000269|PubMed:24225654"
FT COMPBIAS 22..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 243..244
FT /note="Cleavage; by avrPphB"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 160
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000303|PubMed:22046960"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:24225654"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:24225654"
FT MUTAGEN 2
FT /note="G->A: Slightly affects plasma membrane location.
FT Abolishes plasma membrane location; when associated with A-
FT 3 and A-6."
FT /evidence="ECO:0000269|PubMed:22046960,
FT ECO:0000269|PubMed:24225654"
FT MUTAGEN 3
FT /note="C->A: Affects plasma membrane location. Abolishes
FT plasma membrane location; when associated with A-2 and A-
FT 6."
FT /evidence="ECO:0000269|PubMed:22046960,
FT ECO:0000269|PubMed:24225654"
FT MUTAGEN 4
FT /note="F->A: Affects plasma membrane location."
FT /evidence="ECO:0000269|PubMed:22046960"
FT MUTAGEN 6
FT /note="C->A: Affects plasma membrane location. Abolishes
FT plasma membrane location; when associated with A-2 and A-
FT 3."
FT /evidence="ECO:0000269|PubMed:22046960,
FT ECO:0000269|PubMed:24225654"
FT MUTAGEN 98
FT /note="G->E: In pbs1-5; strongly impairs RPS5-mediated
FT plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:24225654"
FT MUTAGEN 103
FT /note="G->R: In pbs1-3; strongly impairs cleavage by
FT avrPphB and RPS5-mediated plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:24225654"
FT MUTAGEN 115
FT /note="K->N: Abolishes kinase activity and RPS5-mediated
FT plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:12947197,
FT ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:22372664"
FT MUTAGEN 241
FT /note="G->A: Abolishes cleavage by avrPphB and RPS5-
FT mediated plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:12947197"
FT MUTAGEN 242
FT /note="D->A: Strongly impairs cleavage by avrPphB and RPS5-
FT mediated plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:12947197"
FT MUTAGEN 243
FT /note="K->A: Affects cleavage by avrPphB and RPS5-mediated
FT plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:12947197"
FT MUTAGEN 244
FT /note="S->F: In pbs1-6; strongly impairs RPS5-mediated
FT plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:24225654"
FT MUTAGEN 252
FT /note="G->R: In pbs1-2; strongly impairs RPS5-mediated
FT plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:11359614,
FT ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:22372664"
FT MUTAGEN 286
FT /note="G->D: In pbs1-4; strongly impairs cleavage by
FT avrPphB and RPS5-mediated plant resistance to P.syringae."
FT /evidence="ECO:0000269|PubMed:24225654"
SQ SEQUENCE 456 AA; 50384 MW; C167E4E3F47ACBC3 CRC64;
MGCFSCFDSS DDEKLNPVDE SNHGQKKQSQ PTVSNNISGL PSGGEKLSSK TNGGSKRELL
LPRDGLGQIA AHTFAFRELA AATMNFHPDT FLGEGGFGRV YKGRLDSTGQ VVAVKQLDRN
GLQGNREFLV EVLMLSLLHH PNLVNLIGYC ADGDQRLLVY EFMPLGSLED HLHDLPPDKE
ALDWNMRMKI AAGAAKGLEF LHDKANPPVI YRDFKSSNIL LDEGFHPKLS DFGLAKLGPT
GDKSHVSTRV MGTYGYCAPE YAMTGQLTVK SDVYSFGVVF LELITGRKAI DSEMPHGEQN
LVAWARPLFN DRRKFIKLAD PRLKGRFPTR ALYQALAVAS MCIQEQAATR PLIADVVTAL
SYLANQAYDP SKDDSRRNRD ERGARLITRN DDGGGSGSKF DLEGSEKEDS PRETARILNR
DINRERAVAE AKMWGESLRE KRRQSEQGTS ESNSTG
//
