DNCV_VIBCH
ID DNCV_VIBCH Reviewed; 436 AA.
AC Q9KVG7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cyclic GMP-AMP synthase;
DE Short=c-GAMP synthase;
DE Short=c-GMP-AMP synthase;
DE EC=2.7.7.- {ECO:0000269|PubMed:22500802, ECO:0000269|PubMed:25131990};
DE AltName: Full=3'3'-cGAMP synthase;
DE AltName: Full=Cyclic AMP-GMP synthase {ECO:0000303|PubMed:22500802};
DE Short=c-AMP-GMP synthase {ECO:0000303|PubMed:22500802};
DE AltName: Full=Dinucleotide cyclase DncV {ECO:0000303|PubMed:22500802};
GN Name=dncV {ECO:0000303|PubMed:22500802}; OrderedLocusNames=VC_0179;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, GENE NAME, INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 131-ASP--ASP-133.
RC STRAIN=ATCC 55056 / El Tor Ogawa E7946, and El Tor C6706;
RX PubMed=22500802; DOI=10.1016/j.cell.2012.01.053;
RA Davies B.W., Bogard R.W., Young T.S., Mekalanos J.J.;
RT "Coordinated regulation of accessory genetic elements produces cyclic di-
RT nucleotides for V. cholerae virulence.";
RL Cell 149:358-370(2012).
RN [3]
RP FUNCTION, OVERPRODUCTION PHENOTYPE, AND MUTAGENESIS OF 131-ASP--ASP-133.
RX PubMed=29891656; DOI=10.1073/pnas.1801233115;
RA Severin G.B., Ramliden M.S., Hawver L.A., Wang K., Pell M.E.,
RA Kieninger A.K., Khataokar A., O'Hara B.J., Behrmann L.V., Neiditch M.B.,
RA Benning C., Waters C.M., Ng W.L.;
RT "Direct activation of a phospholipase by cyclic GMP-AMP in El Tor Vibrio
RT cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6048-E6055(2018).
RN [4]
RP NOMENCLATURE, AND SIMILARITY.
RX PubMed=30787435; DOI=10.1038/s41586-019-0953-5;
RA Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R.,
RA Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S.Y.,
RA Mekalanos J.J., Kranzusch P.J.;
RT "Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.";
RL Nature 567:194-199(2019).
RN [5]
RP ANTIVIRAL DEFENSE, AND OPERON STRUCTURE.
RC STRAIN=El Tor / Serotype O1;
RX PubMed=31533127; DOI=10.1038/s41586-019-1605-5;
RA Cohen D., Melamed S., Millman A., Shulman G., Oppenheimer-Shaanan Y.,
RA Kacen A., Doron S., Amitai G., Sorek R.;
RT "Cyclic GMP-AMP signalling protects bacteria against viral infection.";
RL Nature 574:691-695(2019).
RN [6]
RP ANTIVIRAL DEFENSE, AND OPERON STRUCTURE.
RC STRAIN=El Tor C6706;
RX PubMed=32544385; DOI=10.1016/j.cell.2020.05.019;
RA Lowey B., Whiteley A.T., Keszei A.F.A., Morehouse B.R., Antine S.P.,
RA Cabrera V.J., Kashin D., Schwede F., Mekalanos J.J., Shao S., Lee A.S.Y.,
RA Kranzusch P.J.;
RT "CBASS immunity uses CARF-related effectors to sense 3'-5' and 2'-5'-linked
RT cyclic oligonucleotide signals and protect bacteria from phage infection.";
RL Cell 182:38-49(2020).
RN [7]
RP CLASSIFICATION AND NOMENCLATURE.
RX PubMed=32839535; DOI=10.1038/s41564-020-0777-y;
RA Millman A., Melamed S., Amitai G., Sorek R.;
RT "Diversity and classification of cyclic-oligonucleotide-based anti-phage
RT signalling systems.";
RL Nat. Microbiol. 5:1608-1615(2020).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-413 IN COMPLEX WITH MAGNESIUM
RP AND CYCLIC DINUCLEOTIDE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLN-112 AND ILE-257.
RX PubMed=25131990; DOI=10.1016/j.cell.2014.07.028;
RA Kranzusch P.J., Lee A.S., Wilson S.C., Solovykh M.S., Vance R.E.,
RA Berger J.M., Doudna J.A.;
RT "Structure-guided reprogramming of human cGAS dinucleotide linkage
RT specificity.";
RL Cell 158:1011-1021(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 1-419 OF WILD-TYPE AND MUTANTS
RP ALA-131/ALA-133 AND ASN-193 IN COMPLEXES WITH ATP; GTP; MAGNESIUM;
RP 5-METHYLTETRAHYDROFOLATE AND 5-METHYLTETRAHYDROFOLATE DIGLUTAMATE, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF ARG-40; ARG-44; ARG-108; PHE-109; TYR-137
RP AND ASP-260.
RX PubMed=25201413; DOI=10.1016/j.molcel.2014.08.001;
RA Zhu D., Wang L., Shang G., Liu X., Zhu J., Lu D., Wang L., Kan B.,
RA Zhang J.R., Xiang Y.;
RT "Structural biochemistry of a Vibrio cholerae dinucleotide cyclase reveals
RT cyclase activity regulation by folates.";
RL Mol. Cell 55:931-937(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-215 AND 242-412 IN COMPLEX WITH
RP 3'-DEOXY-GTP; 3'-DEOXY-ATP; GTP AND MAGNESIUM.
RX PubMed=25865248; DOI=10.1016/j.str.2015.01.023;
RA Kato K., Ishii R., Hirano S., Ishitani R., Nureki O.;
RT "Structural basis for the catalytic mechanism of DncV, bacterial homolog of
RT cyclic GMP-AMP synthase.";
RL Structure 23:843-850(2015).
CC -!- FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling
CC system) provides immunity against bacteriophage. The CD-NTase protein
CC synthesizes cyclic nucleotides in response to infection; these serve as
CC specific second messenger signals. The signals activate a diverse range
CC of effectors, leading to bacterial cell death and thus abortive phage
CC infection. A type II-A(GA) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:31533127, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Catalyzes the synthesis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP)
CC from GTP and ATP, a second messenger in cell signal transduction. Is
CC also able to produce c-di-AMP and c-di-GMP from ATP and GTP,
CC respectively; however, 3'3'-cGAMP is the dominant molecule produced by
CC DncV in vivo, contrary to the 2'3'-cGAMP produced by eukaryotes. Is
CC required for efficient V.cholerae intestinal colonization, and down-
CC regulates the colonization-influencing process of chemotaxis. Is not
CC active with dATP, TTP, UTP, and CTP. Controls the activity of cGAMP-
CC activated phospholipase CapV, a patatin-like lipase that is a direct
CC 3',3'-cGAMP receptor encoded in the dncV operon (PubMed:29891656).
CC {ECO:0000269|PubMed:22500802, ECO:0000269|PubMed:25131990,
CC ECO:0000269|PubMed:29891656}.
CC -!- FUNCTION: Protects E.coli against phage T2 infection. When the CBASS
CC operon (capV-dcnV-cap2-cap3) is introduced in E.coli MG1655 there is a
CC more than 10(3) decrease in the efficiency of T2 plaque formation.
CC Protects 100-fold against phage T5, offers no protection against T7
CC (PubMed:32544385). When the 4 gene operon capV-dncV-cap2-cap3 is
CC introduced in E.coli MG1655 there is about 100-fold protection against
CC phages P1 and T2 (PubMed:31533127). {ECO:0000269|PubMed:31533127,
CC ECO:0000269|PubMed:32544385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:71501; Evidence={ECO:0000269|PubMed:22500802,
CC ECO:0000269|PubMed:25131990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648;
CC Evidence={ECO:0000269|PubMed:22500802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25131990};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:25131990};
CC -!- ACTIVITY REGULATION: Enzymatic activity of DncV is inhibited by folate-
CC like molecules, such as 5-methyltetrahydrofolate di-glutamate and 5-
CC methyltetrahydrofolate, suggesting the existence of a signaling pathway
CC that links folate-like metabolism cofactors to the regulation of cyclic
CC dinucleotide second messenger synthesis (PubMed:25201413). Lacks a
CC regulatory loop and is constitutively activated (PubMed:25131990).
CC {ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:25201413}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25131990}.
CC -!- INDUCTION: Expression is repressed by the transcriptional regulator
CC VspR (PubMed:22500802). Part of the CBASS operon consisting of capV-
CC dncV-cap2-cap3 (Probable). {ECO:0000269|PubMed:22500802,
CC ECO:0000305|PubMed:31533127, ECO:0000305|PubMed:32544385}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a significant defect
CC in intestinal colonization. {ECO:0000269|PubMed:22500802}.
CC -!- MISCELLANEOUS: Overproduction of the cGAMP synthase DncV leads to an
CC increase in intracellular cGAMP, and induces the formation of cells
CC more translucent than normal with a defect in cell membrane integrity,
CC planktonic growth arrest and a small colony phenotype in El Tor
CC V.cholerae. {ECO:0000269|PubMed:29891656}.
CC -!- SIMILARITY: Belongs to the CD-NTase family. A01 subfamily.
CC {ECO:0000305|PubMed:30787435}.
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DR EMBL; AE003852; AAF93355.1; -; Genomic_DNA.
DR PIR; F82354; F82354.
DR RefSeq; NP_229836.1; NC_002505.1.
DR RefSeq; WP_001901330.1; NZ_LT906614.1.
DR PDB; 4TXY; X-ray; 3.00 A; A/B=3-413.
DR PDB; 4TXZ; X-ray; 2.80 A; A/B=3-413.
DR PDB; 4TY0; X-ray; 1.80 A; A/B=3-413.
DR PDB; 4U03; X-ray; 2.04 A; A/B=1-419.
DR PDB; 4U0L; X-ray; 2.10 A; A/B=1-419.
DR PDB; 4U0M; X-ray; 2.30 A; A/B=1-419.
DR PDB; 4U0N; X-ray; 2.10 A; A/B=1-419.
DR PDB; 4XJ1; X-ray; 1.77 A; A=1-215, A=242-412.
DR PDB; 4XJ3; X-ray; 1.65 A; A=1-215, A=242-412.
DR PDB; 4XJ4; X-ray; 1.60 A; A=1-215, A=242-412.
DR PDB; 4XJ5; X-ray; 1.55 A; A=1-215, A=242-412.
DR PDB; 5GO3; X-ray; 2.20 A; A/B=1-436.
DR PDBsum; 4TXY; -.
DR PDBsum; 4TXZ; -.
DR PDBsum; 4TY0; -.
DR PDBsum; 4U03; -.
DR PDBsum; 4U0L; -.
DR PDBsum; 4U0M; -.
DR PDBsum; 4U0N; -.
DR PDBsum; 4XJ1; -.
DR PDBsum; 4XJ3; -.
DR PDBsum; 4XJ4; -.
DR PDBsum; 4XJ5; -.
DR PDBsum; 5GO3; -.
DR AlphaFoldDB; Q9KVG7; -.
DR SMR; Q9KVG7; -.
DR STRING; 243277.VC_0179; -.
DR DNASU; 2614190; -.
DR EnsemblBacteria; AAF93355; AAF93355; VC_0179.
DR GeneID; 57738919; -.
DR KEGG; vch:VC_0179; -.
DR PATRIC; fig|243277.26.peg.163; -.
DR eggNOG; ENOG502Z9WZ; Bacteria.
DR HOGENOM; CLU_051668_0_0_6; -.
DR OMA; KPTCIRI; -.
DR BioCyc; VCHO:VC0179-MON; -.
DR BRENDA; 2.7.7.B24; 15003.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0140701; F:3',3'-cyclic GMP-AMP synthase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052621; F:diguanylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0050922; P:negative regulation of chemotaxis; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..436
FT /note="Cyclic GMP-AMP synthase"
FT /id="PRO_0000423945"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0M,
FT ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ4,
FT ECO:0007744|PDB:4XJ5"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4TXY, ECO:0007744|PDB:4TXZ,
FT ECO:0007744|PDB:4TY0, ECO:0007744|PDB:4U03,
FT ECO:0007744|PDB:4U0N, ECO:0007744|PDB:4XJ5"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4TXY, ECO:0007744|PDB:4TXZ,
FT ECO:0007744|PDB:4TY0, ECO:0007744|PDB:4U03,
FT ECO:0007744|PDB:4U0N, ECO:0007744|PDB:4XJ5"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0007744|PDB:4U0M"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4TXY, ECO:0007744|PDB:4TXZ,
FT ECO:0007744|PDB:4TY0, ECO:0007744|PDB:4U03,
FT ECO:0007744|PDB:4U0N, ECO:0007744|PDB:4XJ5"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0007744|PDB:4U03,
FT ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ4,
FT ECO:0007744|PDB:4XJ5"
FT BINDING 287
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0M,
FT ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ4,
FT ECO:0007744|PDB:4XJ5"
FT BINDING 301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0M,
FT ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ4,
FT ECO:0007744|PDB:4XJ5"
FT BINDING 348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25131990,
FT ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0M,
FT ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ5"
FT MUTAGEN 40
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25201413"
FT MUTAGEN 44
FT /note="R->E: Impairs protein folding."
FT /evidence="ECO:0000269|PubMed:25201413"
FT MUTAGEN 108
FT /note="R->W: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25201413"
FT MUTAGEN 109
FT /note="F->P: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25201413"
FT MUTAGEN 112
FT /note="Q->T: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25131990"
FT MUTAGEN 131..133
FT /note="DID->AIA: Loss of catalytic activity. Lack of effect
FT on chemotaxis. Overexpression of this mutant does not lead
FT to substantial growth arrest, in contrast to wild-type."
FT /evidence="ECO:0000269|PubMed:22500802,
FT ECO:0000269|PubMed:29891656"
FT MUTAGEN 137
FT /note="Y->R: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25201413"
FT MUTAGEN 257
FT /note="I->R: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:25131990"
FT MUTAGEN 260
FT /note="D->A: Impairs protein folding."
FT /evidence="ECO:0000269|PubMed:25201413"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:4XJ5"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 26..59
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4XJ5"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4XJ4"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:4TY0"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 322..338
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 361..381
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:4XJ5"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:4XJ5"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:4XJ5"
SQ SEQUENCE 436 AA; 49363 MW; FB462969F3628BE6 CRC64;
MRMTWNFHQY YTNRNDGLMG KLVLTDEEKN NLKALRKIIR LRTRDVFEEA KGIAKAVKKS
ALTFEIIQEK VSTTQIKHLS DSEQREVAKL IYEMDDDARD EFLGLTPRFW TQGSFQYDTL
NRPFQPGQEM DIDDGTYMPM PIFESEPKIG HSLLILLVDA SLKSLVAENH GWKFEAKQTC
GRIKIEAEKT HIDVPMYAIP KDEFQKKQIA LEANRSFVKG AIFESYVADS ITDDSETYEL
DSENVNLALR EGDRKWINSD PKIVEDWFND SCIRIGKHLR KVCRFMKAWR DAQWDVGGPS
SISLMAATVN ILDSVAHDAS DLGETMKIIA KHLPSEFARG VESPDSTDEK PLFPPSYKHG
PREMDIMSKL ERLPEILSSA ESADSKSEAL KKINMAFGNR VTNSELIVLA KALPAFAQEP
SSASKPEKIS STMVSG
