GH312_ARATH
ID GH312_ARATH Reviewed; 575 AA.
AC Q9LYU4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=4-substituted benzoates-glutamate ligase GH3.12;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 12;
DE Short=AtGH3-12;
DE AltName: Full=Protein GH3-LIKE DEFENSE GENE 1;
DE AltName: Full=Protein GRETCHEN HAGEN 3.12;
DE AltName: Full=Protein HOPW1-1-INTERACTING 3;
DE AltName: Full=Protein avrPPHB SUSCEPTIBLE 3;
GN Name=GH3.12; Synonyms=GDG1, PBS3, WIN3; OrderedLocusNames=At5g13320;
GN ORFNames=T22N19.5, T31B5.140;
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, INTERACTION WITH PSEUDOMONAS SYRINGAE
RP MACULICOLA HOPW1-1, AND INDUCTION BY PSEUDOMONAS SYRINGAE MACULICOLA.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18266921; DOI=10.1111/j.1365-313x.2008.03439.x;
RA Lee M.W., Jelenska J., Greenberg J.T.;
RT "Arabidopsis proteins important for modulating defense responses to
RT Pseudomonas syringae that secrete HopW1-1.";
RL Plant J. 54:452-465(2008).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10224270; DOI=10.1093/genetics/152.1.401;
RA Warren R.F., Merritt P.M., Holub E., Innes R.W.;
RT "Identification of three putative signal transduction genes involved in R
RT gene-specified disease resistance in Arabidopsis.";
RL Genetics 152:401-412(1999).
RN [5]
RP FUNCTION.
RX PubMed=11846877; DOI=10.1046/j.0960-7412.2001.01229.x;
RA van der Biezen E.A., Freddie C.T., Kahn K., Parker J.E., Jones J.D.;
RT "Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR
RT genes and confers downy mildew resistance through multiple signalling
RT components.";
RL Plant J. 29:439-451(2002).
RN [6]
RP FUNCTION.
RX PubMed=16353557; DOI=10.1094/mpmi-18-1226;
RA McDowell J.M., Williams S.G., Funderburg N.T., Eulgem T., Dangl J.L.;
RT "Genetic analysis of developmentally regulated resistance to downy mildew
RT (Hyaloperonospora parasitica) in Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 18:1226-1234(2005).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS SYRINGAE TOMATO,
RP AND INDUCTION BY PAD4 AND SALICYLIC ACID.
RX PubMed=17918621; DOI=10.1094/mpmi-20-10-1192;
RA Lee M.W., Lu H., Jung H.W., Greenberg J.T.;
RT "A key role for the Arabidopsis WIN3 protein in disease resistance
RT triggered by Pseudomonas syringae that secrete AvrRpt2.";
RL Mol. Plant Microbe Interact. 20:1192-1200(2007).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS SYRINGAE TOMATO,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17521413; DOI=10.1111/j.1365-313x.2007.03130.x;
RA Jagadeeswaran G., Raina S., Acharya B.R., Maqbool S.B., Mosher S.L.,
RA Appel H.M., Schultz J.C., Klessig D.F., Raina R.;
RT "Arabidopsis GH3-LIKE DEFENSE GENE 1 is required for accumulation of
RT salicylic acid, activation of defense responses and resistance to
RT Pseudomonas syringae.";
RL Plant J. 51:234-246(2007).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-502 AND ILE-519, AND
RP INDUCTION BY PSEUDOMONAS SYRINGAE TOMATO.
RC STRAIN=cv. Columbia, and cv. No-0;
RX PubMed=17468220; DOI=10.1104/pp.107.097691;
RA Nobuta K., Okrent R.A., Stoutemyer M., Rodibaugh N., Kempema L.,
RA Wildermuth M.C., Innes R.W.;
RT "The GH3 acyl adenylase family member PBS3 regulates salicylic acid-
RT dependent defense responses in Arabidopsis.";
RL Plant Physiol. 144:1144-1156(2007).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF GLU-502 AND ILE-519.
RC STRAIN=cv. Columbia;
RX PubMed=19189963; DOI=10.1074/jbc.m806662200;
RA Okrent R.A., Brooks M.D., Wildermuth M.C.;
RT "Arabidopsis GH3.12 (PBS3) conjugates amino acids to 4-substituted
RT benzoates and is inhibited by salicylate.";
RL J. Biol. Chem. 284:9742-9754(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH AMP AND SALICYLIC
RP ACID.
RX PubMed=22628555; DOI=10.1126/science.1221863;
RA Westfall C.S., Zubieta C., Herrmann J., Kapp U., Nanao M.H., Jez J.M.;
RT "Structural basis for prereceptor modulation of plant hormones by GH3
RT proteins.";
RL Science 336:1708-1711(2012).
CC -!- FUNCTION: Catalyzes the conjugation of specific amino acids (e.g. Glu
CC and possibly His, Lys, and Met) to their preferred acyl substrates
CC (e.g. 4-substituted benzoates), in a magnesium ion- and ATP-dependent
CC manner. Can use 4-substituted benzoates such as 4-aminobenzoate (pABA),
CC 4-fluorobenzoate and 4-hydroxybenzoate (4-HBA), and, to a lesser
CC extent, benzoate, vanillate and trans-cinnamate, but not 2-substituted
CC benzoates and salicylic acid (SA), as conjugating acyl substrates.
CC Involved in both basal and induced resistance in a SA-dependent manner.
CC Confers resistance to virulent and avirulent pathogens (at least
CC bacteria and oomycetes), and promotes SA glucosides accumulation.
CC Required for the establishment of hyper-sensitive response (HR) upon
CC incompatible interaction and subsequent systemic acquired resistance
CC (SAR). {ECO:0000269|PubMed:10224270, ECO:0000269|PubMed:11846877,
CC ECO:0000269|PubMed:16353557, ECO:0000269|PubMed:17468220,
CC ECO:0000269|PubMed:17521413, ECO:0000269|PubMed:17918621,
CC ECO:0000269|PubMed:18266921, ECO:0000269|PubMed:19189963}.
CC -!- ACTIVITY REGULATION: Specifically and reversibly inhibited by salicylic
CC acid (SA). {ECO:0000269|PubMed:19189963}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=153 uM for 4-aminobenzoate (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19189963};
CC KM=459 uM for 4-hydroxybenzoate (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19189963};
CC KM=867 uM for benzoate (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19189963};
CC KM=636 uM for ATP (with 4-aminobenzoate as cosubstrate at pH 8.5 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:19189963};
CC KM=791 uM for ATP (with 4-hydroxybenzoate as cosubstrate at pH 8.5
CC and 30 degrees Celsius) {ECO:0000269|PubMed:19189963};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:19189963};
CC -!- SUBUNIT: Interacts with the P.syringae pv. maculicola effector HopW1-1
CC (via C-terminus). {ECO:0000269|PubMed:18266921}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, mostly in cotyledons,
CC leaves, hypocotyls and sporadically in roots. Not detected in
CC unchallenged adult plants, except in flowers.
CC {ECO:0000269|PubMed:17521413}.
CC -!- DEVELOPMENTAL STAGE: Observed in young plants. In flowers, first
CC detected in flower buds at the beginning of the floral stage 13. In
CC petals, levels fade out during flower maturation do disappear at floral
CC opening. Present in sepals and to some extent in stamen and carpel.
CC {ECO:0000269|PubMed:17521413}.
CC -!- INDUCTION: By P.syringae pv. maculicola and pv. tomato. Induced by PAD4
CC locally at the infection site and in a salicylic acid-dependent manner
CC systemically. {ECO:0000269|PubMed:17468220,
CC ECO:0000269|PubMed:17521413, ECO:0000269|PubMed:17918621,
CC ECO:0000269|PubMed:18266921}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to virulent and avirulent
CC bacterial pathogens P.syringae pv. tomato and pv. maculicola ES4326
CC with or without DC3000(avrPphB, avrRpt2, avrB, avrRpm1, or avrRps4) as
CC well as to the oomycete pathogen Hyaloperonospora parasitica (downy
CC mildew) isolates Emoy2, Hind4, Hiks1, Wela3, Cand5, and Wand1. Impaired
CC hyper-sensitive response (HR) and systemic acquired resistance (SAR).
CC Compromised salicylic acid glucosides (SAG) accumulation. Resistance is
CC partially rescued by SA treatment. {ECO:0000269|PubMed:10224270,
CC ECO:0000269|PubMed:17468220, ECO:0000269|PubMed:17521413,
CC ECO:0000269|PubMed:17918621}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {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; EU214910; ABW84226.1; -; mRNA.
DR EMBL; AL163491; CAB86639.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91880.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68312.1; -; Genomic_DNA.
DR PIR; T48579; T48579.
DR RefSeq; NP_001330076.1; NM_001343269.1.
DR RefSeq; NP_196836.1; NM_121335.4.
DR PDB; 4EPM; X-ray; 2.10 A; A=1-575.
DR PDB; 4EQ4; X-ray; 2.07 A; A/B=1-575.
DR PDB; 4EQL; X-ray; 1.80 A; A/B=1-575.
DR PDB; 4EWV; X-ray; 2.90 A; A/B=1-575.
DR PDB; 4L39; X-ray; 2.81 A; A/B=1-575.
DR PDB; 6OMS; X-ray; 1.94 A; A/B=1-575.
DR PDBsum; 4EPM; -.
DR PDBsum; 4EQ4; -.
DR PDBsum; 4EQL; -.
DR PDBsum; 4EWV; -.
DR PDBsum; 4L39; -.
DR PDBsum; 6OMS; -.
DR AlphaFoldDB; Q9LYU4; -.
DR SMR; Q9LYU4; -.
DR STRING; 3702.AT5G13320.1; -.
DR PaxDb; Q9LYU4; -.
DR PRIDE; Q9LYU4; -.
DR ProteomicsDB; 220747; -.
DR EnsemblPlants; AT5G13320.1; AT5G13320.1; AT5G13320.
DR EnsemblPlants; AT5G13320.3; AT5G13320.3; AT5G13320.
DR GeneID; 831173; -.
DR Gramene; AT5G13320.1; AT5G13320.1; AT5G13320.
DR Gramene; AT5G13320.3; AT5G13320.3; AT5G13320.
DR KEGG; ath:AT5G13320; -.
DR Araport; AT5G13320; -.
DR TAIR; locus:6530584248; AT5G13320.
DR eggNOG; ENOG502QPMW; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q9LYU4; -.
DR OMA; CAPEDIT; -.
DR PhylomeDB; Q9LYU4; -.
DR BioCyc; ARA:AT5G13320-MON; -.
DR BioCyc; MetaCyc:AT5G13320-MON; -.
DR PRO; PR:Q9LYU4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYU4; baseline and differential.
DR Genevisible; Q9LYU4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0052625; F:4-aminobenzoate amino acid synthetase activity; IDA:TAIR.
DR GO; GO:0052628; F:4-hydroxybenzoate amino acid synthetase activity; IDA:TAIR.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR GO; GO:0052626; F:benzoate amino acid synthetase activity; IDA:TAIR.
DR GO; GO:0052627; F:vanillate amino acid synthetase activity; IDA:TAIR.
DR GO; GO:0018874; P:benzoate metabolic process; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0016046; P:detection of fungus; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IEP:TAIR.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Hypersensitive response; Ligase; Plant defense;
KW Reference proteome.
FT CHAIN 1..575
FT /note="4-substituted benzoates-glutamate ligase GH3.12"
FT /id="PRO_0000403642"
FT COILED 6..33
FT /evidence="ECO:0000255"
FT BINDING 95..96
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4,
FT ECO:0007744|PDB:4EQL"
FT BINDING 120..123
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EQ4, ECO:0007744|PDB:4EQL"
FT BINDING 301
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4,
FT ECO:0007744|PDB:4EQL"
FT BINDING 324
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4,
FT ECO:0007744|PDB:4EQL"
FT BINDING 328
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4,
FT ECO:0007744|PDB:4EQL"
FT BINDING 347
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4,
FT ECO:0007744|PDB:4EQL"
FT BINDING 398
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4,
FT ECO:0007744|PDB:4EQL"
FT BINDING 417
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EQ4"
FT MUTAGEN 502
FT /note="E->K: In pbs3-1; loss of conjugating activity, and
FT impaired resistance to virulent and avirulent pathogens;
FT when associated with T-519."
FT /evidence="ECO:0000269|PubMed:17468220,
FT ECO:0000269|PubMed:19189963"
FT MUTAGEN 519
FT /note="I->T: In pbs3-1; loss of conjugating activity, and
FT impaired resistance to virulent and avirulent pathogens;
FT when associated with K-502."
FT /evidence="ECO:0000269|PubMed:17468220,
FT ECO:0000269|PubMed:19189963"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 110..130
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 219..242
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:4EQ4"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 442..446
FT /evidence="ECO:0007829|PDB:4L39"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:4EPM"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 462..471
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 491..503
FT /evidence="ECO:0007829|PDB:4EQL"
FT HELIX 507..514
FT /evidence="ECO:0007829|PDB:4EQL"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4EQL"
FT TURN 529..533
FT /evidence="ECO:0007829|PDB:4EQ4"
FT TURN 536..540
FT /evidence="ECO:0007829|PDB:4EQ4"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:4EWV"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:4EQ4"
FT STRAND 567..573
FT /evidence="ECO:0007829|PDB:4EQ4"
SQ SEQUENCE 575 AA; 65128 MW; 3762CE16A43A1E92 CRC64;
MKPIFDINET FEKQLKDLTS NVKSIQDNLL EEIITPNTKT EYLQRFLIDR FDKELFKKNV
PIVSYEDIKP YLDRVVNGES SDVISARTIT GFLLSSGTSG GAQKMMPWNN KYLDNLTFIY
DLRMQVITKH VKGVEEGKGM MFLFTKQESM TPSGLPARVA TSSYFKSDYF KNRPSNWYYS
YTSPDEVILC PNNTESLYCH LLCGLVQRDE VVRTGSIFAS VMVRAIEVLK NSWEELCSNI
RSGHLSNWVT DLGCQNSVSL VLGGPRPELA DTIEEICNQN SWKGIVKRLW PNTKYIETVV
TGSMGQYVPM LNYYCNDLPL VSTTYGSSET TFGINLDPLC KPEDVSYTFM PNMSYFEFIP
MDGGDKNDVV DLEDVKLGCT YEPVVTNFAG LYRMRVGDIV LVTGFYNNAP QFKFVRRENV
VLSIDSDKTN EEDLFKAVSQ AKLVLESSGL DLKDFTSYAD TSTFPGHYVV YLEVDTKEGE
EKETAQFELD EEALSTCCLV MEESLDNVYK RCRFKDGSIG PLEIRVVRQG TFDSLMDFFI
SQGASTGQYK TPRCIKSGKA LQVLETCVVA KFFSI
