ID   DNAG_ECOLI              Reviewed;         581 AA.
AC   P0ABS5; P02922; P02923; Q2M9D9; Q47613;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:340457};
GN   Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; Synonyms=dnaP, parB;
GN   OrderedLocusNames=b3066, JW3038;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6186393; DOI=10.1016/0092-8674(83)90453-1;
RA   Burton Z.F., Gross C.A., Watanabe K.K., Burgess R.R.;
RT   "The operon that encodes the sigma subunit of RNA polymerase also encodes
RT   ribosomal protein S21 and DNA primase in E. coli K12.";
RL   Cell 32:335-349(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6750604; DOI=10.1073/pnas.79.15.4550;
RA   Smiley B.L., Lupski J.R., Svec P.S., McMacken R., Godson G.N.;
RT   "Sequences of the Escherichia coli dnaG primase gene and regulation of its
RT   expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:4550-4554(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC   STRAIN=K12;
RX   PubMed=6222240; DOI=10.1007/bf00326054;
RA   Lupski J.R., Smiley B.L., Godson G.N.;
RT   "Regulation of the rpsU-dnaG-rpoD macromolecular synthesis operon and the
RT   initiation of DNA replication in Escherichia coli K-12.";
RL   Mol. Gen. Genet. 189:48-57(1983).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=340457; DOI=10.1016/s0021-9258(17)38167-x;
RA   Rowen L., Kornberg A.;
RT   "Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA
RT   chains.";
RL   J. Biol. Chem. 253:758-764(1978).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND ZINC-BINDING.
RX   PubMed=1511009; DOI=10.1016/0167-4781(92)90047-4;
RA   Stamford N.P.J., Lilley P.E., Dixon N.E.;
RT   "Enriched sources of Escherichia coli replication proteins. The dnaG
RT   primase is a zinc metalloprotein.";
RL   Biochim. Biophys. Acta 1132:17-25(1992).
RN   [8]
RP   COFACTOR, AND ZINC-BINDING.
RX   PubMed=8679581; DOI=10.1021/bi952948p;
RA   Griep M.A., Lokey E.R.;
RT   "The role of zinc and the reactivity of cysteines in Escherichia coli
RT   primase.";
RL   Biochemistry 35:8260-8267(1996).
RN   [9]
RP   INTERACTION WITH DNAB, AND MUTAGENESIS OF GLN-576.
RX   PubMed=8917517; DOI=10.1073/pnas.93.23.12902;
RA   Lu Y.B., Ratnakar P.V., Mohanty B.K., Bastia D.;
RT   "Direct physical interaction between DnaG primase and DnaB helicase of
RT   Escherichia coli is necessary for optimal synthesis of primer RNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12902-12907(1996).
RN   [10]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [11]
RP   SUBUNIT, AND INTERACTION WITH DNAB.
RX   PubMed=14557266; DOI=10.1074/jbc.m308956200;
RA   Mitkova A.V., Khopde S.M., Biswas S.B.;
RT   "Mechanism and stoichiometry of interaction of DnaG primase with DnaB
RT   helicase of Escherichia coli in RNA primer synthesis.";
RL   J. Biol. Chem. 278:52253-52261(2003).
RN   [12]
RP   ACTIVITY REGULATION.
RX   PubMed=16285921; DOI=10.1016/j.molcel.2005.09.004;
RA   Corn J.E., Pease P.J., Hura G.L., Berger J.M.;
RT   "Crosstalk between primase subunits can act to regulate primer synthesis in
RT   trans.";
RL   Mol. Cell 20:391-401(2005).
RN   [13] {ECO:0007744|PDB:1EQN}
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 109-429.
RX   PubMed=10873470; DOI=10.1006/jmbi.2000.3844;
RA   Podobnik M., McInerney P., O'Donnell M., Kuriyan J.;
RT   "A TOPRIM domain in the crystal structure of the catalytic core of
RT   Escherichia coli primase confirms a structural link to DNA
RT   topoisomerases.";
RL   J. Mol. Biol. 300:353-362(2000).
RN   [14] {ECO:0007744|PDB:1DD9, ECO:0007744|PDB:1DDE}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 111-433, AND DOMAIN.
RX   PubMed=10741967; DOI=10.1126/science.287.5462.2482;
RA   Keck J.L., Roche D.D., Lynch A.S., Berger J.M.;
RT   "Structure of the RNA polymerase domain of E. coli primase.";
RL   Science 287:2482-2486(2000).
RN   [15] {ECO:0007744|PDB:1T3W}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 434-581, INTERACTION WITH DNAB,
RP   AND DOMAIN.
RX   PubMed=15649896; DOI=10.1074/jbc.m412645200;
RA   Oakley A.J., Loscha K.V., Schaeffer P.M., Liepinsh E., Pintacuda G.,
RA   Wilce M.C., Otting G., Dixon N.E.;
RT   "Crystal and solution structures of the helicase-binding domain of
RT   Escherichia coli primase.";
RL   J. Biol. Chem. 280:11495-11504(2005).
RN   [16] {ECO:0007744|PDB:2HAJ}
RP   STRUCTURE BY NMR OF 434-581, SUBUNIT, AND DOMAIN.
RX   PubMed=17010164; DOI=10.1111/j.1742-4658.2006.05495.x;
RA   Su X.C., Schaeffer P.M., Loscha K.V., Gan P.H., Dixon N.E., Otting G.;
RT   "Monomeric solution structure of the helicase-binding domain of Escherichia
RT   coli DnaG primase.";
RL   FEBS J. 273:4997-5009(2006).
RN   [17] {ECO:0007744|PDB:3B39}
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 111-429, DNA-BINDING, AND
RP   MUTAGENESIS OF TRP-165; ARG-199 AND ARG-201.
RX   PubMed=18193061; DOI=10.1038/nsmb.1373;
RA   Corn J.E., Pelton J.G., Berger J.M.;
RT   "Identification of a DNA primase template tracking site redefines the
RT   geometry of primer synthesis.";
RL   Nat. Struct. Mol. Biol. 15:163-169(2008).
RN   [18] {ECO:0007744|PDB:6CBR, ECO:0007744|PDB:6CBS, ECO:0007744|PDB:6CBT}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 434-581.
RA   Oakley A.J., Lo A.T.Y.;
RT   "DnaG primase C-terminal domain complex with SSB C-terminal peptide.";
RL   Submitted (FEB-2018) to the PDB data bank.
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:1511009,
CC       ECO:0000269|PubMed:340457}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC         EC=2.7.7.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00974,
CC         ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:340457};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00974, ECO:0000269|PubMed:1511009,
CC         ECO:0000269|PubMed:8679581};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974,
CC       ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:8679581};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00974};
CC       Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC   -!- ACTIVITY REGULATION: Activity can be regulated by an intermolecular
CC       trans association between the zinc-binding domain and the catalytic
CC       core domain of two different primase molecules.
CC       {ECO:0000269|PubMed:16285921}.
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. The primase-helicase complex is
CC       composed of up to three DnaG bound to one DnaB hexamer.
CC       {ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:14557266,
CC       ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:15649896,
CC       ECO:0000269|PubMed:17010164, ECO:0000269|PubMed:340457,
CC       ECO:0000269|PubMed:8917517}.
CC   -!- INTERACTION:
CC       P0ABS5; P0ACB0: dnaB; NbExp=3; IntAct=EBI-549259, EBI-548978;
CC       P0ABS5; P0A7L0: rplA; NbExp=2; IntAct=EBI-549259, EBI-543771;
CC       P0ABS5; P0AGE0: ssb; NbExp=2; IntAct=EBI-549259, EBI-1118620;
CC   -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC       domain that contains the primase activity, and a C-terminal DnaB-
CC       binding domain. {ECO:0000255|HAMAP-Rule:MF_00974,
CC       ECO:0000269|PubMed:10741967, ECO:0000269|PubMed:15649896,
CC       ECO:0000269|PubMed:17010164}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00974}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA23531.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; J01687; AAA24600.1; -; Genomic_DNA.
DR   EMBL; V00274; CAA23531.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U28379; AAA89146.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76102.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77117.1; -; Genomic_DNA.
DR   EMBL; V00346; CAA23636.1; -; Genomic_DNA.
DR   PIR; A03423; RYEC2.
DR   RefSeq; NP_417538.1; NC_000913.3.
DR   RefSeq; WP_000918827.1; NZ_STEB01000001.1.
DR   PDB; 1DD9; X-ray; 1.60 A; A=111-433.
DR   PDB; 1DDE; X-ray; 1.70 A; A=111-433.
DR   PDB; 1EQN; X-ray; 2.90 A; A/B/C/D/E=111-429.
DR   PDB; 1T3W; X-ray; 2.80 A; A/B=434-581.
DR   PDB; 2HAJ; NMR; -; A=434-581.
DR   PDB; 3B39; X-ray; 2.35 A; A/B=111-429.
DR   PDB; 6CBR; X-ray; 1.50 A; A/B=434-581.
DR   PDB; 6CBS; X-ray; 1.85 A; A/B=434-581.
DR   PDB; 6CBT; X-ray; 2.10 A; A/B=434-581.
DR   PDB; 7T22; EM; 4.20 A; G/H/I=434-581.
DR   PDB; 7T23; EM; 4.20 A; G/H=434-581.
DR   PDBsum; 1DD9; -.
DR   PDBsum; 1DDE; -.
DR   PDBsum; 1EQN; -.
DR   PDBsum; 1T3W; -.
DR   PDBsum; 2HAJ; -.
DR   PDBsum; 3B39; -.
DR   PDBsum; 6CBR; -.
DR   PDBsum; 6CBS; -.
DR   PDBsum; 6CBT; -.
DR   PDBsum; 7T22; -.
DR   PDBsum; 7T23; -.
DR   AlphaFoldDB; P0ABS5; -.
DR   BMRB; P0ABS5; -.
DR   EMDB; EMD-25609; -.
DR   EMDB; EMD-25610; -.
DR   SMR; P0ABS5; -.
DR   BioGRID; 4262146; 230.
DR   BioGRID; 851886; 1.
DR   ComplexPortal; CPX-1933; DnaB-DnaG primase-helicase complex.
DR   ComplexPortal; CPX-5909; Replication restart primosome complex, priAC variant.
DR   ComplexPortal; CPX-5910; Replication restart primosome complex, priAB variant.
DR   ComplexPortal; CPX-5911; Replication restart primosome complex, priC-rep variant.
DR   DIP; DIP-47954N; -.
DR   IntAct; P0ABS5; 17.
DR   STRING; 511145.b3066; -.
DR   jPOST; P0ABS5; -.
DR   PaxDb; 511145-b3066; -.
DR   EnsemblBacteria; AAC76102; AAC76102; b3066.
DR   GeneID; 75205347; -.
DR   GeneID; 947570; -.
DR   KEGG; ecj:JW3038; -.
DR   KEGG; eco:b3066; -.
DR   PATRIC; fig|1411691.4.peg.3664; -.
DR   EchoBASE; EB0235; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_5_4_6; -.
DR   InParanoid; P0ABS5; -.
DR   OMA; LMWPIRD; -.
DR   OrthoDB; 9803773at2; -.
DR   PhylomeDB; P0ABS5; -.
DR   BioCyc; EcoCyc:EG10239-MONOMER; -.
DR   BioCyc; MetaCyc:EG10239-MONOMER; -.
DR   BRENDA; 2.7.7.101; 2026.
DR   EvolutionaryTrace; P0ABS5; -.
DR   PRO; PR:P0ABS5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:1990156; C:DnaB-DnaG complex; IPI:ComplexPortal.
DR   GO; GO:1990077; C:primosome complex; NAS:ComplexPortal.
DR   GO; GO:0030894; C:replisome; NAS:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IDA:EcoliWiki.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:ComplexPortal.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; NAS:ComplexPortal.
DR   GO; GO:0031297; P:replication fork processing; NAS:ComplexPortal.
DR   CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR   DisProt; DP02134; -.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR019475; DNA_primase_DnaB-bd.
DR   InterPro; IPR006295; DNA_primase_DnaG.
DR   InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
DR   InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR   InterPro; IPR030846; DnaG_bac.
DR   InterPro; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00766; DnaG_DnaB_bind; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF117023; DNA primase DnaG, C-terminal domain; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Primosome;
KW   Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..581
FT                   /note="DNA primase"
FT                   /id="PRO_0000180490"
FT   DOMAIN          259..341
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   ZN_FING         40..64
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   MUTAGEN         165
FT                   /note="W->A: Abolishes DNA-binding and primer synthesis."
FT                   /evidence="ECO:0000269|PubMed:18193061"
FT   MUTAGEN         199
FT                   /note="R->A: Abolishes primer synthesis but can still bind
FT                   DNA. Abolishes DNA-binding; when associated with A-201."
FT                   /evidence="ECO:0000269|PubMed:18193061"
FT   MUTAGEN         201
FT                   /note="R->A: Abolishes primer synthesis but can still bind
FT                   DNA. Abolishes DNA-binding; when associated with A-199."
FT                   /evidence="ECO:0000269|PubMed:18193061"
FT   MUTAGEN         576
FT                   /note="Q->A: Decreases interaction with DnaB and primase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8917517"
FT   CONFLICT        24
FT                   /note="D -> N (in Ref. 5; CAA23636)"
FT                   /evidence="ECO:0000305"
FT   HELIX           116..131
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           137..145
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           150..156
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           167..172
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           176..184
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          202..209
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:1EQN"
FT   STRAND          215..225
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   TURN            241..243
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           248..253
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          261..266
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           267..275
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          281..283
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          285..288
FT                   /evidence="ECO:0007829|PDB:1DDE"
FT   HELIX           291..300
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          302..311
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           312..325
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           326..328
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   STRAND          334..340
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           346..362
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           368..376
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           377..379
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           385..399
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           405..419
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           424..427
FT                   /evidence="ECO:0007829|PDB:1DD9"
FT   HELIX           450..460
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   HELIX           462..467
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   TURN            472..474
FT                   /evidence="ECO:0007829|PDB:2HAJ"
FT   HELIX           476..478
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   HELIX           482..494
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   HELIX           500..507
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   HELIX           510..512
FT                   /evidence="ECO:0007829|PDB:1T3W"
FT   HELIX           513..520
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   HELIX           523..525
FT                   /evidence="ECO:0007829|PDB:6CBS"
FT   HELIX           528..561
FT                   /evidence="ECO:0007829|PDB:6CBR"
FT   HELIX           565..580
FT                   /evidence="ECO:0007829|PDB:6CBR"
SQ   SEQUENCE   581 AA;  65565 MW;  294CF020E7B45D94 CRC64;
     MAGRIPRVFI NDLLARTDIV DLIDARVKLK KQGKNFHACC PFHNEKTPSF TVNGEKQFYH
     CFGCGAHGNA IDFLMNYDKL EFVETVEELA AMHNLEVPFE AGSGPSQIER HQRQTLYQLM
     DGLNTFYQQS LQQPVATSAR QYLEKRGLSH EVIARFAIGF APPGWDNVLK RFGGNPENRQ
     SLIDAGMLVT NDQGRSYDRF RERVMFPIRD KRGRVIGFGG RVLGNDTPKY LNSPETDIFH
     KGRQLYGLYE AQQDNAEPNR LLVVEGYMDV VALAQYGINY AVASLGTSTT ADHIQLLFRA
     TNNVICCYDG DRAGRDAAWR ALETALPYMT DGRQLRFMFL PDGEDPDTLV RKEGKEAFEA
     RMEQAMPLSA FLFNSLMPQV DLSTPDGRAR LSTLALPLIS QVPGETLRIY LRQELGNKLG
     ILDDSQLERL MPKAAESGVS RPVPQLKRTT MRILIGLLVQ NPELATLVPP LENLDENKLP
     GLGLFRELVN TCLSQPGLTT GQLLEHYRGT NNAATLEKLS MWDDIADKNI AEQTFTDSLN
     HMFDSLLELR QEELIARERT HGLSNEERLE LWTLNQELAK K
//