PRIA_ECOLI
ID PRIA_ECOLI Reviewed; 732 AA.
AC P17888; Q2M8N1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Primosomal protein N' {ECO:0000255|HAMAP-Rule:MF_00983};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent helicase PriA {ECO:0000255|HAMAP-Rule:MF_00983};
DE AltName: Full=Replication factor Y;
GN Name=priA {ECO:0000255|HAMAP-Rule:MF_00983};
GN OrderedLocusNames=b3935, JW3906;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21.
RX PubMed=2162050; DOI=10.1073/pnas.87.12.4620;
RA Lee E.H., Masai H., Allen G.C. Jr., Kornberg A.;
RT "The priA gene encoding the primosomal replicative n' protein of
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4620-4624(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-16.
RX PubMed=2162049; DOI=10.1073/pnas.87.12.4615;
RA Nurse P., Digate R., Zavitz K., Marians K.;
RT "Molecular cloning and DNA sequence analysis of Escherichia coli priA, the
RT gene encoding the primosomal protein replication factor Y.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4615-4619(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=2825188; DOI=10.1073/pnas.84.23.8345;
RA Lee M.S., Marians K.J.;
RT "Escherichia coli replication factor Y, a component of the primosome, can
RT act as a DNA helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8345-8349(1987).
RN [7]
RP SIMILARITY TO DEAD-BOX HELICASES.
RX PubMed=1662369; DOI=10.1093/nar/19.24.6953;
RA Ouzounis C.A., Blencowe B.J.;
RT "Bacterial DNA replication initiation factor priA is related to proteins
RT belonging to the 'DEAD-box' family.";
RL Nucleic Acids Res. 19:6953-6953(1991).
RN [8]
RP FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=8366072; DOI=10.1016/s0021-9258(19)36500-7;
RA Allen G.C. Jr., Kornberg A.;
RT "Assembly of the primosome of DNA replication in Escherichia coli.";
RL J. Biol. Chem. 268:19204-19209(1993).
RN [9]
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 [10]
RP FUNCTION IN BACTERIOPHAGE MU DNA REPLICATION, DNA-BINDING, AND MUTAGENESIS
RP OF LYS-230.
RX PubMed=10356325; DOI=10.1006/jmbi.1999.2783;
RA Jones J.M., Nakai H.;
RT "Duplex opening by primosome protein PriA for replisome assembly on a
RT recombination intermediate.";
RL J. Mol. Biol. 289:503-516(1999).
RN [11]
RP FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=10956036; DOI=10.1021/bi001113y;
RA Jezewska M.J., Bujalowski W.;
RT "Interactions of Escherichia coli replicative helicase PriA protein with
RT single-stranded DNA.";
RL Biochemistry 39:10454-10467(2000).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11929519; DOI=10.1046/j.1365-2958.2002.02747.x;
RA Rangarajan S., Woodgate R., Goodman M.F.;
RT "Replication restart in UV-irradiated Escherichia coli involving pols II,
RT III, V, PriA, RecA and RecFOR proteins.";
RL Mol. Microbiol. 43:617-628(2002).
RN [13]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS OF
RP THR-226; LYS-230; ASP-320 AND ARG-584.
RX PubMed=12622722; DOI=10.1046/j.1365-2443.2003.00630.x;
RA Tanaka T., Taniyama C., Arai K., Masai H.;
RT "ATPase/helicase motif mutants of Escherichia coli PriA protein essential
RT for recombination-dependent DNA replication.";
RL Genes Cells 8:251-261(2003).
RN [14]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12917421; DOI=10.1074/jbc.c300285200;
RA Mizukoshi T., Tanaka T., Arai K., Kohda D., Masai H.;
RT "A critical role of the 3' terminus of nascent DNA chains in recognition of
RT stalled replication forks.";
RL J. Biol. Chem. 278:42234-42239(2003).
RN [15]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SSB.
RX PubMed=15576682; DOI=10.1093/nar/gkh980;
RA Cadman C.J., McGlynn P.;
RT "PriA helicase and SSB interact physically and functionally.";
RL Nucleic Acids Res. 32:6378-6387(2004).
RN [16]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=17483094; DOI=10.1074/jbc.m701848200;
RA Tanaka T., Mizukoshi T., Sasaki K., Kohda D., Masai H.;
RT "Escherichia coli PriA protein, two modes of DNA binding and activation of
RT ATP hydrolysis.";
RL J. Biol. Chem. 282:19917-19927(2007).
RN [17]
RP SUBUNIT, AND INTERACTION WITH PRIB.
RX PubMed=17588514; DOI=10.1016/j.molcel.2007.05.012;
RA Lopper M., Boonsombat R., Sandler S.J., Keck J.L.;
RT "A hand-off mechanism for primosome assembly in replication restart.";
RL Mol. Cell 26:781-793(2007).
RN [18]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [19]
RP FUNCTION.
RX PubMed=23264623; DOI=10.1074/jbc.m112.435966;
RA Manhart C.M., McHenry C.S.;
RT "The PriA replication restart protein blocks replicase access prior to
RT helicase assembly and directs template specificity through its ATPase
RT activity.";
RL J. Biol. Chem. 288:3989-3999(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-105 IN COMPLEXES WITH DAMP AND
RP DCMP.
RA Sasaki K., Ose T., Okamoto N., Tanaka T., Maenaka K., Masai H., Kohda D.;
RT "Structural basis for the specific recognition of the 3' terminal
RT nucleotide of DNA by the PriA protein from E.coli.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 1-105.
RA Sasaki K., Ose T., Okamoto N., Tanaka T., Maenaka K., Shirai T., Masai H.,
RA Kohda D.;
RT "Insights into base nonselective recognition of 3'-terminus of DNA in
RT stalled replication forks by the PriA protein.";
RL Submitted (AUG-2006) to the PDB data bank.
CC -!- FUNCTION: Involved in the restart of stalled replication forks.
CC Recognizes and binds the arrested nascent DNA chain at stalled
CC replication forks. It can open the DNA duplex, via its helicase
CC activity, and promote assembly of the primosome and loading of the
CC major replicative helicase DnaB onto DNA. Is also involved in
CC initiation of normal DNA replication in various plasmids and phages.
CC Binds to branched DNA structures that resemble D-loops or to the
CC primosome assembly site (PAS). Binds to DNA in two distinct modes,
CC either dependent on or independent of the 3' terminus recognition.
CC {ECO:0000255|HAMAP-Rule:MF_00983, ECO:0000269|PubMed:10356325,
CC ECO:0000269|PubMed:10956036, ECO:0000269|PubMed:11929519,
CC ECO:0000269|PubMed:12622722, ECO:0000269|PubMed:12917421,
CC ECO:0000269|PubMed:15576682, ECO:0000269|PubMed:17483094,
CC ECO:0000269|PubMed:23264623, ECO:0000269|PubMed:2825188,
CC ECO:0000269|PubMed:8366072}.
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by binding to DNA.
CC Helicase activity is stimulated by SSB. {ECO:0000269|PubMed:12622722,
CC ECO:0000269|PubMed:15576682, ECO:0000269|PubMed:17483094}.
CC -!- SUBUNIT: Component of the primosome, which is composed of PriA, PriB,
CC PriC, DnaB, DnaC, DnaG and DnaT. Binds ssDNA as a monomer. Interacts
CC with SSB and PriB. {ECO:0000255|HAMAP-Rule:MF_00983,
CC ECO:0000269|PubMed:10956036, ECO:0000269|PubMed:15576682,
CC ECO:0000269|PubMed:17588514, ECO:0000269|PubMed:8366072}.
CC -!- INTERACTION:
CC P17888; P07013: priB; NbExp=3; IntAct=EBI-552050, EBI-1125223;
CC P17888; P0AGE0: ssb; NbExp=3; IntAct=EBI-552050, EBI-1118620;
CC -!- INDUCTION: Induced by hydroxyurea. {ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain and a C-terminal
CC helicase domain. The helicase domain plays an important role in high
CC affinity and stable binding of PriA to forked DNAs.
CC {ECO:0000269|PubMed:12622722, ECO:0000269|PubMed:17483094}.
CC -!- DISRUPTION PHENOTYPE: Mutants show delayed replication restart after
CC exposition to UV. {ECO:0000269|PubMed:11929519}.
CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00983}.
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DR EMBL; M33293; AAA24416.1; -; Genomic_DNA.
DR EMBL; D00616; BAA00491.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03067.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76917.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77375.1; -; Genomic_DNA.
DR PIR; S40878; A35505.
DR RefSeq; NP_418370.1; NC_000913.3.
DR RefSeq; WP_001301269.1; NZ_LN832404.1.
DR PDB; 2D7E; X-ray; 2.50 A; A/B/C/D=1-105.
DR PDB; 2D7G; X-ray; 3.30 A; A/B/C/D=1-105.
DR PDB; 2D7H; X-ray; 3.00 A; A/B/C/D=1-105.
DR PDB; 2DWL; X-ray; 3.20 A; A/B/C/D=1-105.
DR PDB; 2DWM; X-ray; 3.15 A; A/B/C/D=1-105.
DR PDB; 2DWN; X-ray; 3.35 A; A/B/C/D=1-105.
DR PDB; 6DCR; X-ray; 1.98 A; A/B=1-114, A/B=175-732.
DR PDBsum; 2D7E; -.
DR PDBsum; 2D7G; -.
DR PDBsum; 2D7H; -.
DR PDBsum; 2DWL; -.
DR PDBsum; 2DWM; -.
DR PDBsum; 2DWN; -.
DR PDBsum; 6DCR; -.
DR AlphaFoldDB; P17888; -.
DR SMR; P17888; -.
DR BioGRID; 4262651; 65.
DR ComplexPortal; CPX-1951; Replication restart pre-primosome complex, priAB variant.
DR ComplexPortal; CPX-1952; Replication restart pre-primosome complex, priAC variant.
DR ComplexPortal; CPX-5909; Replication restart primosome complex, priAC variant.
DR ComplexPortal; CPX-5910; Replication restart primosome complex, priAB variant.
DR DIP; DIP-10562N; -.
DR IntAct; P17888; 17.
DR STRING; 511145.b3935; -.
DR PaxDb; P17888; -.
DR PRIDE; P17888; -.
DR EnsemblBacteria; AAC76917; AAC76917; b3935.
DR EnsemblBacteria; BAE77375; BAE77375; BAE77375.
DR GeneID; 948426; -.
DR KEGG; ecj:JW3906; -.
DR KEGG; eco:b3935; -.
DR PATRIC; fig|1411691.4.peg.2770; -.
DR EchoBASE; EB0756; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_6; -.
DR InParanoid; P17888; -.
DR OMA; RCHYCGY; -.
DR PhylomeDB; P17888; -.
DR BioCyc; EcoCyc:EG10763-MON; -.
DR BioCyc; MetaCyc:EG10763-MON; -.
DR BRENDA; 3.6.4.12; 2026.
DR EvolutionaryTrace; P17888; -.
DR PRO; PR:P17888; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990158; C:DnaB-DnaC-DnaT-PriA-PriB complex; IC:ComplexPortal.
DR GO; GO:1990159; C:DnaB-DnaC-DnaT-PriA-PriC complex; IC:ComplexPortal.
DR GO; GO:1990077; C:primosome complex; IC:ComplexPortal.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IMP:EcoliWiki.
DR GO; GO:0006260; P:DNA replication; IMP:EcoCyc.
DR GO; GO:0006270; P:DNA replication initiation; IMP:EcoCyc.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:EcoCyc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:EcoliWiki.
DR GO; GO:0006302; P:double-strand break repair; IMP:EcoliWiki.
DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoCyc.
DR GO; GO:0031297; P:replication fork processing; IC:ComplexPortal.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoliWiki.
DR GO; GO:0010332; P:response to gamma radiation; IMP:EcoliWiki.
DR Gene3D; 3.40.1440.60; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00983; PriA; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR InterPro; IPR041236; PriA_C.
DR InterPro; IPR040498; PriA_CRR.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00595; priA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Primosome; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..732
FT /note="Primosomal protein N'"
FT /id="PRO_0000102123"
FT DOMAIN 211..377
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 447..638
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 436..448
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 463..479
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 320..323
FT /note="DEAH box"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MUTAGEN 226
FT /note="T->V: Strong decrease in ATPase and helicase
FT activities. Does not affect DNA binding."
FT /evidence="ECO:0000269|PubMed:12622722"
FT MUTAGEN 230
FT /note="K->D: Lack of ATPase activity and strong decrease in
FT helicase activity. Does not affect DNA binding."
FT /evidence="ECO:0000269|PubMed:10356325,
FT ECO:0000269|PubMed:12622722"
FT MUTAGEN 230
FT /note="K->R: Lack of helicase activity. Decreases Mu DNA
FT replication."
FT /evidence="ECO:0000269|PubMed:10356325,
FT ECO:0000269|PubMed:12622722"
FT MUTAGEN 320
FT /note="D->A: Strong decrease in ATPase and helicase
FT activities. Decreases DNA binding."
FT /evidence="ECO:0000269|PubMed:12622722"
FT MUTAGEN 584
FT /note="R->A: Does not affect DNA binding, but impairs
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:12622722"
FT CONFLICT 156
FT /note="A -> R (in Ref. 1; AAA24416)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="A -> R (in Ref. 1; AAA24416)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="A -> V (in Ref. 2; BAA00491)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2DWN"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:6DCR"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 494..501
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 532..538
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 570..584
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 593..599
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 614..627
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 633..647
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 648..661
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 671..683
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 686..696
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 698..709
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 710..714
FT /evidence="ECO:0007829|PDB:6DCR"
FT HELIX 716..719
FT /evidence="ECO:0007829|PDB:6DCR"
FT STRAND 720..728
FT /evidence="ECO:0007829|PDB:6DCR"
SQ SEQUENCE 732 AA; 81655 MW; AB6C90F43042A363 CRC64;
MPVAHVALPV PLPRTFDYLL PEGMTVKAGC RVRVPFGKQQ ERIGIVVSVS DASELPLNEL
KAVVEVLDSE PVFTHSVWRL LLWAADYYHH PIGDVLFHAL PILLRQGRPA ANAPMWYWFA
TEQGQAVDLN SLKRSPKQQQ ALAALRQGKI WRDQVATLEF NDAALQALRK KGLCDLASET
PEFSDWRTNY AVSGERLRLN TEQATAVGAI HSAADTFSAW LLAGVTGSGK TEVYLSVLEN
VLAQGKQALV MVPEIGLTPQ TIARFRERFN APVEVLHSGL NDSERLSAWL KAKNGEAAIV
IGTRSALFTP FKNLGVIVID EEHDSSYKQQ EGWRYHARDL AVYRAHSEQI PIILGSATPA
LETLCNVQQK KYRLLRLTRR AGNARPAIQH VLDLKGQKVQ AGLAPALITR MRQHLQADNQ
VILFLNRRGF APALLCHDCG WIAECPRCDH YYTLHQAQHH LRCHHCDSQR PVPRQCPSCG
STHLVPVGLG TEQLEQTLAP LFPGVPISRI DRDTTSRKGA LEQQLAEVHR GGARILIGTQ
MLAKGHHFPD VTLVALLDVD GALFSADFRS AERFAQLYTQ VAGRAGRAGK QGEVVLQTHH
PEHPLLQTLL YKGYDAFAEQ ALAERRMMQL PPWTSHVIVR AEDHNNQHAP LFLQQLRNLI
LSSPLADEKL WVLGPVPALA PKRGGRWRWQ ILLQHPSRVR LQHIINGTLA LINTIPDSRK
VKWVLDVDPI EG
