AMPD_ARATH
ID AMPD_ARATH Reviewed; 839 AA.
AC O80452; B9DFX9; Q56XX1; Q93ZR9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=AMP deaminase {ECO:0000303|PubMed:15918887};
DE Short=AtAMPD {ECO:0000303|PubMed:15918887};
DE EC=3.5.4.6 {ECO:0000305};
DE AltName: Full=Protein EMBRYONIC FACTOR 1 {ECO:0000303|PubMed:15918887};
GN Name=AMPD {ECO:0000303|PubMed:15918887};
GN Synonyms=FAC1 {ECO:0000303|PubMed:15918887};
GN OrderedLocusNames=At2g38280 {ECO:0000312|Araport:AT2G38280};
GN ORFNames=F16M14.21 {ECO:0000312|EMBL:AAC27176.2};
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], MUTAGENESIS OF ASP-598, FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15918887; DOI=10.1111/j.1365-313x.2005.02411.x;
RA Xu J., Zhang H.-Y., Xie C.-H., Xue H.-W., Dijkhuis P., Liu C.-M.;
RT "EMBRYONIC FACTOR 1 encodes an AMP deaminase and is essential for the
RT zygote to embryo transition in Arabidopsis.";
RL Plant J. 42:743-756(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-357.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-140 AND SER-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP INTERACTION WITH AHK4.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
RN [9]
RP CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 140-839 IN
RP COMPLEX WITH COFORMYCIN 5'-PHOSPHATE AND ZINC IONS.
RX PubMed=16511144; DOI=10.1107/s1744309105019792;
RA Han B.W., Bingman C.A., Mahnke D.K., Sabina R.L., Phillips G.N. Jr.;
RT "Crystallization and preliminary X-ray crystallographic analysis of
RT adenosine 5'-monophosphate deaminase (AMPD) from Arabidopsis thaliana in
RT complex with coformycin 5'-phosphate.";
RL Acta Crystallogr. F 61:740-742(2005).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP INTERACTION WITH EER5.
RX PubMed=19843313; DOI=10.1111/j.1365-313x.2009.04048.x;
RA Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
RA Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
RT "Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components
RT and anchoring nucleoporin.";
RL Plant J. 61:259-270(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 140-839 IN COMPLEX WITH COFORMYCIN
RP 5'-PHOSPHATE; PHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, SUBUNIT,
RP COFACTOR, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16543243; DOI=10.1074/jbc.m513009200;
RA Han B.W., Bingman C.A., Mahnke D.K., Bannen R.M., Bednarek S.Y.,
RA Sabina R.L., Phillips G.N. Jr.;
RT "Membrane association, mechanism of action, and structure of Arabidopsis
RT embryonic factor 1 (FAC1).";
RL J. Biol. Chem. 281:14939-14947(2006).
CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism.
CC Essential for the transition from zygote to embryo.
CC {ECO:0000269|PubMed:15918887}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6;
CC Evidence={ECO:0000269|PubMed:16543243};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16543243};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16543243};
CC -!- ACTIVITY REGULATION: Activated by ATP. Activated by sulfate ions (in
CC vitro). Inhibited by phosphate ions. {ECO:0000269|PubMed:16543243}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 mM for AMP (in the absence of ATP)
CC {ECO:0000269|PubMed:16543243};
CC KM=0.26 mM for AMP (in the presence of 1 mM ATP)
CC {ECO:0000269|PubMed:16543243};
CC Vmax=17 umol/min/mg enzyme (in the absence of ATP)
CC {ECO:0000269|PubMed:16543243};
CC Vmax=375 umol/min/mg enzyme (in the presence of 1 mM ATP)
CC {ECO:0000269|PubMed:16543243};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from AMP: step 1/1.
CC -!- SUBUNIT: Homodimer. Interacts with AHK4. Interacts with EER5
CC (PubMed:19843313). {ECO:0000269|PubMed:16511144,
CC ECO:0000269|PubMed:16543243, ECO:0000269|PubMed:18642946,
CC ECO:0000269|PubMed:19843313}.
CC -!- INTERACTION:
CC O80452; Q9C5U0: AHK4; NbExp=2; IntAct=EBI-1807679, EBI-1100775;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16543243}; Single-
CC pass membrane protein {ECO:0000269|PubMed:16543243}. Microsome membrane
CC {ECO:0000269|PubMed:16543243}. Note=Might be associated with the inner
CC mitochondrial membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, flowers,
CC pollen grains, pollen tubes and siliques, and at a lower level in
CC stems. {ECO:0000269|PubMed:15918887}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both male and female gametophytes, at
CC the zygote stage, in the endosperm, and during early embryo
CC development. Observed in cotyledonary embryos and in the basal part of
CC the embryo, but not in the suspensor or in mature embryos. Also
CC expressed during somatic embryogenesis. {ECO:0000269|PubMed:15918887}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94943.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC003028; AAC27176.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09516.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09517.1; -; Genomic_DNA.
DR EMBL; AY056301; AAL07150.1; -; mRNA.
DR EMBL; AY133852; AAM91786.1; -; mRNA.
DR EMBL; AK316943; BAH19646.1; -; mRNA.
DR EMBL; AK221552; BAD94943.1; ALT_SEQ; mRNA.
DR PIR; T01259; T01259.
DR RefSeq; NP_565886.1; NM_129384.3.
DR RefSeq; NP_850294.1; NM_179963.3.
DR PDB; 2A3L; X-ray; 3.34 A; A=139-839.
DR PDBsum; 2A3L; -.
DR AlphaFoldDB; O80452; -.
DR SMR; O80452; -.
DR BioGRID; 3750; 5.
DR IntAct; O80452; 2.
DR STRING; 3702.AT2G38280.2; -.
DR BindingDB; O80452; -.
DR ChEMBL; CHEMBL2366458; -.
DR iPTMnet; O80452; -.
DR PaxDb; O80452; -.
DR PRIDE; O80452; -.
DR ProteomicsDB; 244448; -.
DR EnsemblPlants; AT2G38280.1; AT2G38280.1; AT2G38280.
DR EnsemblPlants; AT2G38280.2; AT2G38280.2; AT2G38280.
DR GeneID; 818408; -.
DR Gramene; AT2G38280.1; AT2G38280.1; AT2G38280.
DR Gramene; AT2G38280.2; AT2G38280.2; AT2G38280.
DR KEGG; ath:AT2G38280; -.
DR Araport; AT2G38280; -.
DR TAIR; locus:2042902; AT2G38280.
DR eggNOG; KOG1096; Eukaryota.
DR HOGENOM; CLU_003782_3_0_1; -.
DR InParanoid; O80452; -.
DR OMA; ESPPYSY; -.
DR OrthoDB; 49756at2759; -.
DR PhylomeDB; O80452; -.
DR BioCyc; ARA:AT2G38280-MON; -.
DR BRENDA; 3.5.4.6; 399.
DR SABIO-RK; O80452; -.
DR UniPathway; UPA00591; UER00663.
DR EvolutionaryTrace; O80452; -.
DR PRO; PR:O80452; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80452; baseline and differential.
DR Genevisible; O80452; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0003876; F:AMP deaminase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd01319; AMPD; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Endoplasmic reticulum;
KW Hydrolase; Membrane; Metal-binding; Microsome; Nucleotide metabolism;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..839
FT /note="AMP deaminase"
FT /id="PRO_0000238455"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 40..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 681
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 289..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 393
FT /ligand="substrate"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 462..467
FT /ligand="substrate"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 662
FT /ligand="substrate"
FT BINDING 736
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 737..740
FT /ligand="substrate"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MUTAGEN 598
FT /note="D->N: In fac1-1; zygote-lethal phenotype."
FT /evidence="ECO:0000269|PubMed:15918887"
FT CONFLICT 324
FT /note="D -> G (in Ref. 5; BAH19646)"
FT /evidence="ECO:0000305"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 342..373
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 429..436
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 474..479
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 485..490
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 491..502
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 505..515
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 523..532
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 539..548
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 564..570
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 573..579
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 594..601
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 628..646
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 647..650
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 667..675
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 683..687
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 689..698
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 706..709
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 710..713
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 721..726
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 747..759
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 763..776
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 781..787
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 790..793
FT /evidence="ECO:0007829|PDB:2A3L"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 802..805
FT /evidence="ECO:0007829|PDB:2A3L"
FT HELIX 809..826
FT /evidence="ECO:0007829|PDB:2A3L"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:2A3L"
SQ SEQUENCE 839 AA; 95130 MW; 188F1F4A589A17DA CRC64;
MEPNIYQLAL AALFGASFVA VSGFFMHFKA LNLVLERGKE RKENPDGDEP QNPTLVRRRS
QVRRKVNDQY GRSPASLPDA TPFTDGGGGG GGDTGRSNGH VYVDEIPPGL PRLHTPSEGR
ASVHGASSIR KTGSFVRPIS PKSPVASASA FESVEESDDD DNLTNSEGLD ASYLQANGDN
EMPADANEEQ ISMAASSMIR SHSVSGDLHG VQPDPIAADI LRKEPEQETF VRLNVPLEVP
TSDEVEAYKC LQECLELRKR YVFQETVAPW EKEVISDPST PKPNTEPFAH YPQGKSDHCF
EMQDGVVHVF ANKDAKEDLF PVADATAFFT DLHHVLKVIA AGNIRTLCHR RLVLLEQKFN
LHLMLNADKE FLAQKSAPHR DFYNVRKVDT HVHHSACMNQ KHLLRFIKSK LRKEPDEVVI
FRDGTYLTLR EVFESLDLTG YDLNVDLLDV HADKSTFHRF DKFNLKYNPC GQSRLREIFL
KQDNLIQGRF LGEITKQVFS DLEASKYQMA EYRISIYGRK MSEWDQLASW IVNNDLYSEN
VVWLIQLPRL YNIYKDMGIV TSFQNILDNI FIPLFEATVD PDSHPQLHVF LKQVVGFDLV
DDESKPERRP TKHMPTPAQW TNAFNPAFSY YVYYCYANLY VLNKLRESKG MTTITLRPHS
GEAGDIDHLA ATFLTCHSIA HGINLRKSPV LQYLYYLAQI GLAMSPLSNN SLFLDYHRNP
FPVFFLRGLN VSLSTDDPLQ IHLTKEPLVE EYSIAASVWK LSACDLCEIA RNSVYQSGFS
HALKSHWIGK DYYKRGPDGN DIHKTNVPHI RVEFRDTIWK EEMQQVYLGK AVISDEVVP
