DNAG_ECOLI
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 03-AUG-2022, entry version 135.
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; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974,
CC ECO:0000269|PubMed:1511009, 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;
CC Evidence={ECO:0000255|HAMAP-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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 AlphaFoldDB; P0ABS5; -.
DR BMRB; P0ABS5; -.
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; P0ABS5; -.
DR PRIDE; P0ABS5; -.
DR EnsemblBacteria; AAC76102; AAC76102; b3066.
DR EnsemblBacteria; BAE77117; BAE77117; BAE77117.
DR GeneID; 66673035; -.
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 PhylomeDB; P0ABS5; -.
DR BioCyc; EcoCyc:EG10239-MON; -.
DR BioCyc; MetaCyc:EG10239-MON; -.
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; IC:ComplexPortal.
DR GO; GO:0030894; C:replisome; IC: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; IC:ComplexPortal.
DR GO; GO:0031297; P:replication fork processing; IC:ComplexPortal.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR DisProt; DP02134; -.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR013264; DNA_primase_core_N.
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; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08278; DnaG_DnaB_bind; 1.
DR Pfam; PF08275; Toprim_N; 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 TIGRFAMs; TIGR01391; dnaG; 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
