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   27-MAR-2024, entry version 154.
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; 3.
DR   STRING; 3702.O80452; -.
DR   BindingDB; O80452; -.
DR   ChEMBL; CHEMBL2366458; -.
DR   iPTMnet; O80452; -.
DR   PaxDb; 3702-AT2G38280-2; -.
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; AT2G38280; FAC1.
DR   eggNOG; KOG1096; Eukaryota.
DR   HOGENOM; CLU_003782_3_0_1; -.
DR   InParanoid; O80452; -.
DR   OMA; RKERGMC; -.
DR   OrthoDB; 20951at2759; -.
DR   PhylomeDB; O80452; -.
DR   BioCyc; ARA:AT2G38280-MONOMER; -.
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   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01319; AMPD; 1.
DR   Gene3D; 4.10.800.20; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
DR   Genevisible; O80452; AT.
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
//