ID   PUR9_CHICK              Reviewed;         593 AA.
AC   P31335;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Bifunctional purine biosynthesis protein ATIC;
DE   AltName: Full=AICAR transformylase/inosine monophosphate cyclohydrolase {ECO:0000303|PubMed:17324932};
DE            Short=ATIC {ECO:0000303|PubMed:17324932};
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE              EC=2.1.2.3 {ECO:0000269|PubMed:12501179};
DE     AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
DE              Short=AICAR formyltransferase;
DE     AltName: Full=AICAR transformylase;
DE   Includes:
DE     RecName: Full=Inosine 5'-monophosphate cyclohydrolase {ECO:0000305};
DE              Short=IMP cyclohydrolase {ECO:0000305};
DE              EC=3.5.4.10 {ECO:0000250|UniProtKB:P31939};
DE     AltName: Full=IMP synthase;
DE     AltName: Full=Inosinicase;
GN   Name=ATIC; Synonyms=PURH;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1937050; DOI=10.1016/0378-1119(91)90199-l;
RA   Ni L., Guan K., Zalkin H., Dixon J.E.;
RT   "De novo purine nucleotide biosynthesis: cloning, sequencing and expression
RT   of a chicken PurH cDNA encoding 5-aminoimidazole-4-carboxamide-
RT   ribonucleotide transformylase-IMP cyclohydrolase.";
RL   Gene 106:197-205(1991).
RN   [2] {ECO:0007744|PDB:1G8M}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GMP, AND SUBUNIT.
RX   PubMed=11323713; DOI=10.1038/87555;
RA   Greasley S.E., Horton P., Ramcharan J., Beardsley G.P., Benkovic S.J.,
RA   Wilson I.A.;
RT   "Crystal structure of a bifunctional transformylase and cyclohydrolase
RT   enzyme in purine biosynthesis.";
RL   Nat. Struct. Biol. 8:402-406(2001).
RN   [3] {ECO:0007744|PDB:1M9N}
RP   X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH AICAR AND XMP,
RP   FUNCTION, SUBUNIT, AND PATHWAY.
RX   PubMed=12501179; DOI=10.1021/bi020505x;
RA   Wolan D.W., Greasley S.E., Beardsley G.P., Wilson I.A.;
RT   "Structural insights into the avian AICAR transformylase mechanism.";
RL   Biochemistry 41:15505-15513(2002).
RN   [4] {ECO:0007744|PDB:1OZ0}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH BETA-DADF INHIBITOR.
RX   PubMed=12974624; DOI=10.1021/bi030106h;
RA   Wolan D.W., Greasley S.E., Wall M.J., Benkovic S.J., Wilson I.A.;
RT   "Structure of avian AICAR transformylase with a multisubstrate adduct
RT   inhibitor beta-DADF identifies the folate binding site.";
RL   Biochemistry 42:10904-10914(2003).
RN   [5] {ECO:0007744|PDB:1THZ}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 326203-A INHIBITOR,
RP   AND ACTIVITY REGULATION.
RX   PubMed=15355974; DOI=10.1074/jbc.m406801200;
RA   Xu L., Li C., Olson A.J., Wilson I.A.;
RT   "Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide
RT   transformylase in complex with a novel non-folate inhibitor identified by
RT   virtual ligand screening.";
RL   J. Biol. Chem. 279:50555-50565(2004).
RN   [6] {ECO:0007744|PDB:2B1G, ECO:0007744|PDB:2B1I, ECO:0007744|PDB:2IU0, ECO:0007744|PDB:2IU3}
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) IN COMPLEXES WITH TRANSITION STATE
RP   ANALOG INHIBITORS, AND ACTIVITY REGULATION.
RX   PubMed=17324932; DOI=10.1074/jbc.m607293200;
RA   Xu L., Chong Y., Hwang I., D'Onofrio A., Amore K., Beardsley G.P., Li C.,
RA   Olson A.J., Boger D.L., Wilson I.A.;
RT   "Structure-based design, synthesis, evaluation, and crystal structures of
RT   transition state analogue inhibitors of inosine monophosphate
RT   cyclohydrolase.";
RL   J. Biol. Chem. 282:13033-13046(2007).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the last two steps of
CC       purine biosynthesis (PubMed:12501179). Acts as a transformylase that
CC       incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-
CC       phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the
CC       intermediate formyl-AICAR (FAICAR) (PubMed:12501179). Can use both 10-
CC       formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor
CC       in this reaction. Also catalyzes the cyclization of FAICAR to IMP.
CC       Promotes insulin receptor/INSR autophosphorylation and is involved in
CC       INSR internalization (By similarity). {ECO:0000250|UniProtKB:P31939,
CC       ECO:0000269|PubMed:12501179}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3;
CC         Evidence={ECO:0000269|PubMed:12501179};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193;
CC         Evidence={ECO:0000305|PubMed:12501179};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-
CC         ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate;
CC         Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452,
CC         ChEBI:CHEBI:58467, ChEBI:CHEBI:58475;
CC         Evidence={ECO:0000250|UniProtKB:P31939};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145;
CC         Evidence={ECO:0000250|UniProtKB:P31939};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC         Evidence={ECO:0000250|UniProtKB:P31939};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447;
CC         Evidence={ECO:0000250|UniProtKB:P31939};
CC   -!- ACTIVITY REGULATION: AMP and XMP inhibit AICAR formyltransferase
CC       activity (By similarity). AICAR formyltransferase activity is
CC       competitively inhibited by 2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfo-
CC       phenyl)-1H-pyrazol-4-ylazo]-4-sulfo-benzoic acid (326203-A)
CC       (PubMed:15355974). FAICAR cyclization is competitively inhibited by
CC       1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one-2,2-dioxide and
CC       the corresponding nucleoside and nucleoside monophosphate
CC       (PubMed:17324932). {ECO:0000250|UniProtKB:P31939,
CC       ECO:0000269|PubMed:15355974, ECO:0000269|PubMed:17324932}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC       1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC       step 1/1. {ECO:0000269|PubMed:12501179}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC       from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC       1/1. {ECO:0000250|UniProtKB:P31939}.
CC   -!- SUBUNIT: Homodimer (PubMed:11323713, PubMed:12501179). Associates with
CC       internalized INSR complexes on Golgi/endosomal membranes. Interacts
CC       with INSR; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is
CC       proposed to be part of a signaling network regulating INSR
CC       autophosphorylation and endocytosis (By similarity).
CC       {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:11323713,
CC       ECO:0000269|PubMed:12501179}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P54113}.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region. {ECO:0000305|PubMed:17324932}.
CC   -!- MISCELLANEOUS: The de novo purine synthesis pathway includes 10
CC       sequential steps, beginning with phosphoribosyl pyrophosphate and
CC       ending with inositol monophosphate (IMP), the first purin compound of
CC       the pathway. {ECO:0000250|UniProtKB:P31939}.
CC   -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR   EMBL; S64492; AAB20309.1; -; mRNA.
DR   PIR; JQ1281; DTCHPH.
DR   RefSeq; NP_990509.1; NM_205178.1.
DR   PDB; 1G8M; X-ray; 1.75 A; A/B=1-593.
DR   PDB; 1M9N; X-ray; 1.93 A; A/B=1-593.
DR   PDB; 1OZ0; X-ray; 2.50 A; A/B=1-593.
DR   PDB; 1THZ; X-ray; 1.80 A; A/B=1-593.
DR   PDB; 2B1G; X-ray; 2.10 A; A/B/C/D=1-593.
DR   PDB; 2B1I; X-ray; 2.02 A; A/B=1-593.
DR   PDB; 2IU0; X-ray; 2.53 A; A/B=1-593.
DR   PDB; 2IU3; X-ray; 2.90 A; A/B=1-593.
DR   PDBsum; 1G8M; -.
DR   PDBsum; 1M9N; -.
DR   PDBsum; 1OZ0; -.
DR   PDBsum; 1THZ; -.
DR   PDBsum; 2B1G; -.
DR   PDBsum; 2B1I; -.
DR   PDBsum; 2IU0; -.
DR   PDBsum; 2IU3; -.
DR   AlphaFoldDB; P31335; -.
DR   SMR; P31335; -.
DR   STRING; 9031.ENSGALP00000061123; -.
DR   PaxDb; 9031-ENSGALP00000005643; -.
DR   GeneID; 396091; -.
DR   KEGG; gga:396091; -.
DR   CTD; 471; -.
DR   VEuPathDB; HostDB:geneid_396091; -.
DR   eggNOG; KOG2555; Eukaryota.
DR   InParanoid; P31335; -.
DR   PhylomeDB; P31335; -.
DR   BRENDA; 2.1.2.3; 1306.
DR   BRENDA; 3.5.4.10; 1306.
DR   Reactome; R-GGA-419140; De novo synthesis of IMP.
DR   SABIO-RK; P31335; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   EvolutionaryTrace; P31335; -.
DR   PRO; PR:P31335; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01421; IMPCH; 1.
DR   Gene3D; 1.10.287.440; -; 1.
DR   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00139; PurH; 1.
DR   InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR   InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR002695; PurH-like.
DR   NCBIfam; TIGR00355; purH; 1.
DR   PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR   PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Hydrolase; Multifunctional enzyme;
KW   Purine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..593
FT                   /note="Bifunctional purine biosynthesis protein ATIC"
FT                   /id="PRO_0000192155"
FT   DOMAIN          1..147
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   REGION          1..199
FT                   /note="IMP cyclohydrolase"
FT                   /evidence="ECO:0000305|PubMed:17324932"
FT   REGION          200..593
FT                   /note="AICAR formyltransferase"
FT                   /evidence="ECO:0000305|PubMed:17324932"
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor; for FAICAR cyclization
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   ACT_SITE        268
FT                   /note="Proton acceptor; for AICAR formyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         13..15
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000305|PubMed:11323713,
FT                   ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         35..38
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000305|PubMed:11323713,
FT                   ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         65..68
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000305|PubMed:11323713,
FT                   ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         102..103
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000305|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         126..127
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000305|PubMed:11323713,
FT                   ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         208..209
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         268
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         317
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         340
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         432
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         452
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         453
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000305|PubMed:12974624,
FT                   ECO:0007744|PDB:1OZ0"
FT   BINDING         542
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000269|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   BINDING         547
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000305|PubMed:12974624,
FT                   ECO:0007744|PDB:1OZ0"
FT   BINDING         566..567
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000305|PubMed:12974624,
FT                   ECO:0007744|PDB:1OZ0"
FT   BINDING         589
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000269|PubMed:12501179,
FT                   ECO:0007744|PDB:1M9N"
FT   SITE            267
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   MOD_RES         200
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   STRAND          7..13
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           36..44
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1M9N"
FT   HELIX           52..56
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           107..111
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:2IU0"
FT   HELIX           118..122
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           128..138
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   TURN            139..142
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           152..160
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           169..198
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   TURN            201..203
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          223..226
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          228..234
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           238..258
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          262..267
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          270..276
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           282..287
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   TURN            291..293
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           299..309
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   TURN            312..317
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          318..324
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           328..335
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          339..345
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           349..357
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           358..361
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          364..368
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          376..382
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          385..390
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           398..401
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           413..427
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          429..432
FT                   /evidence="ECO:0007829|PDB:1OZ0"
FT   STRAND          434..438
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          441..446
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           452..468
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           472..475
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           485..497
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           504..510
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          513..515
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           522..529
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          535..541
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           547..553
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   TURN            554..556
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          557..563
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   HELIX           569..579
FT                   /evidence="ECO:0007829|PDB:1G8M"
FT   STRAND          582..587
FT                   /evidence="ECO:0007829|PDB:1G8M"
SQ   SEQUENCE   593 AA;  64415 MW;  BD1A34F03D96A136 CRC64;
     MAARQQLALL SVSEKAGLVE FARSLNALGL GLIASGGTAT ALRDAGLPVR DVSDLTGFPE
     MLGGRVKTLH PAVHAGILAR NIPEDNADMN KQDFSLVRVV VCNLYPFVKT VSSPGVTVPE
     AVEKIDIGGV ALLRAAAKNH ARVTVVCDPA DYSSVAKEMA ASKDKDTSVE TRRHLALKAF
     THTAQYDAAI SDYFRKEYSK GVSQLPLRYG MNPHQSPAQL YTTRPKLPLT VVNGSPGFIN
     LCDALNAWQL VKELKQALGI PAAASFKHVS PAGAAVGIPL SEEEAQVCMV HDLHKTLTPL
     ASAYARSRGA DRMSSFGDFI ALSDICDVPT AKIISREVSD GVVAPGYEEE ALKILSKKKN
     GGYCVLQMDP NYEPDDNEIR TLYGLQLMQK RNNAVIDRSL FKNIVTKNKT LPESAVRDLI
     VASIAVKYTQ SNSVCYAKDG QVIGIGAGQQ SRIHCTRLAG DKANSWWLRH HPRVLSMKFK
     AGVKRAEVSN AIDQYVTGTI GEDEDLVKWQ AMFEEVPAQL TEAEKKQWIA KLTAVSLSSD
     AFFPFRDNVD RAKRIGVQFI VAPSGSAADE VVIEACNELG ITLIHTNLRL FHH
//