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DNA polymerase IV (Pol IV) (EC 2.7.7.7) (Translesion synthesis polymerase IV) (TSL polymerase IV)

 DPO4_ECOLI              Reviewed;         351 AA.
Q47155; Q47683; Q8RJ78; Q8RJ81; Q8RJ86; Q8RJ87; Q8RNI5; Q8RNI6;
Q8RNI7; Q8RNI8; Q8RNI9; Q8RNJ0; Q8RNJ1; Q8RNJ2; Q8RNJ3; Q8RNJ4;
Q8RNJ5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
07-NOV-2018, entry version 148.
RecName: Full=DNA polymerase IV;
Short=Pol IV;
EC=2.7.7.7;
AltName: Full=Translesion synthesis polymerase IV {ECO:0000303|PubMed:14729336};
Short=TSL polymerase IV;
Name=dinB; Synonyms=dinP; OrderedLocusNames=b0231, JW0221;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7596361; DOI=10.1016/0165-7992(95)90024-1;
Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.;
"dinP, a new gene in Escherichia coli, whose product shows
similarities to UmuC and its homologues.";
Mutat. Res. 347:1-7(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
4.0 - 6.0 min (189,987 - 281,416bp) region.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-342.
STRAIN=ECOR 10A, ECOR 13A, ECOR 17A, ECOR 1A, ECOR 20A, ECOR 23A,
ECOR 24A, ECOR 26B1, ECOR 27B1, ECOR 34B1, ECOR 35D, ECOR 37UG,
ECOR 45B1, ECOR 46D, ECOR 49D, ECOR 4A, ECOR 50D, ECOR 51B2,
ECOR 52B2, ECOR 57B2, ECOR 58B1, ECOR 59B2, ECOR 60B2, ECOR 62B2,
ECOR 68B1, and ECOR 70B1;
Bjedov I., Matic I., Denamur E.;
"Phylogeny of SOS inducible DNA polymerases of Escherichia coli.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[7]
CHARACTERIZATION.
PubMed=6771759; DOI=10.1073/pnas.77.5.2819;
Kenyon C.J., Walker G.C.;
"DNA-damaging agents stimulate gene expression at specific loci in
Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 77:2819-2823(1980).
[8]
FUNCTION.
STRAIN=K12;
PubMed=9391106; DOI=10.1073/pnas.94.25.13792;
Kim S.-R., Maenhaut-Michel G., Yamada M., Yamamoto Y., Matsui K.,
Sofuni T., Nohmi T., Ohmori H.;
"Multiple pathways for SOS-induced mutagenesis in Escherichia coli: an
overexpression of dinB/dinP results in strongly enhancing mutagenesis
in the absence of any exogenous treatment to damage DNA.";
Proc. Natl. Acad. Sci. U.S.A. 94:13792-13797(1997).
[9]
FUNCTION, AND MUTAGENESIS OF ASP-8; ARG-49; ASP-103 AND GLU-104.
STRAIN=K12;
PubMed=10488344; DOI=10.1016/S1097-2765(00)80376-7;
Wagner J., Gruz P., Kim S.-R., Yamada M., Matsui K., Fuchs R.P.P.,
Nohmi T.;
"The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV,
involved in mutagenesis.";
Mol. Cell 4:281-286(1999).
[10]
FUNCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=11080171; DOI=10.1093/emboj/19.22.6259;
Napolitano R., Janel-Bintz R., Wagner J., Fuchs R.P.P.;
"All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V)
are involved in induced mutagenesis.";
EMBO J. 19:6259-6265(2000).
[11]
FUNCTION, AND STIMULATION BY BETA SLIDING-CLAMP COMPLEX.
PubMed=10801133; DOI=10.1038/35010020;
Tang M., Pham P., Shen X., Taylor J.S., O'Donnell M., Woodgate R.,
Goodman M.F.;
"Roles of E. coli DNA polymerases IV and V in lesion-targeted and
untargeted SOS mutagenesis.";
Nature 404:1014-1018(2000).
[12]
FUNCTION.
PubMed=11463382; DOI=10.1016/S1097-2765(01)00204-0;
McKenzie G.J., Lee P.L., Lombardo M.-J., Hastings P.J.,
Rosenberg S.M.;
"SOS mutator DNA polymerase IV functions in adaptive mutation and not
adaptive amplification.";
Mol. Cell 7:571-579(2001).
[13]
FUNCTION.
PubMed=11751576; DOI=10.1093/embo-reports/kvf007;
Lenne-Samuel N., Wagner J., Etienne H., Fuchs R.P.P.;
"The processivity factor beta controls DNA polymerase IV traffic
during spontaneous mutagenesis and translesion synthesis in vivo.";
EMBO Rep. 3:45-49(2002).
[14]
FUNCTION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=12060704; DOI=10.1073/pnas.092269199;
Yeiser B., Pepper E.D., Goodman M.F., Finkel S.E.;
"SOS-induced DNA polymerases enhance long-term survival and
evolutionary fitness.";
Proc. Natl. Acad. Sci. U.S.A. 99:8737-8741(2002).
[15]
INDUCTION, AND OPERON STRUCTURE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=12813093; DOI=10.1128/JB.185.13.3972-3977.2003;
McKenzie G.J., Magner D.B., Lee P.L., Rosenberg S.M.;
"The dinB operon and spontaneous mutation in Escherichia coli.";
J. Bacteriol. 185:3972-3977(2003).
[16]
SUBUNIT.
PubMed=16168375; DOI=10.1016/j.molcel.2005.08.011;
Indiani C., McInerney P., Georgescu R., Goodman M.F., O'Donnell M.;
"A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases
simultaneously.";
Mol. Cell 19:805-815(2005).
[17]
REVIEW.
PubMed=11595180; DOI=10.1016/S0092-8674(01)00509-8;
Friedberg E.C., Fischhaber P.L., Kisker C.;
"Error-prone DNA polymerases: novel structures and the benefits of
infidelity.";
Cell 107:9-12(2001).
[18]
REVIEW.
PubMed=11587937; DOI=10.1016/S1369-5274(00)00255-1;
McKenzie G.J., Rosenberg S.M.;
"Adaptive mutations, mutator DNA polymerases and genetic change
strategies of pathogens.";
Curr. Opin. Microbiol. 4:586-594(2001).
[19]
INDUCTION BY HYDROXYUREA.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[20]
REVIEW.
PubMed=12045089; DOI=10.1146/annurev.biochem.71.083101.124707;
Goodman M.F.;
"Error-prone repair DNA polymerases in prokaryotes and eukaryotes.";
Annu. Rev. Biochem. 71:17-50(2002).
[21] {ECO:0000244|PDB:1UNN}
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-351 IN COMPLEX WITH DNAN.
PubMed=14592985; DOI=10.1093/emboj/cdg568;
Bunting K.A., Roe S.M., Pearl L.H.;
"Structural basis for recruitment of translesion DNA polymerase Pol
IV/DinB to the beta-clamp.";
EMBO J. 22:5883-5892(2003).
[22] {ECO:0000244|PDB:1OK7}
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 336-351 IN COMPLEX WITH
DNAN.
PubMed=14729336; DOI=10.1016/J.JMB.2003.11.049;
Burnouf D.Y., Olieric V., Wagner J., Fujii S., Reinbolt J.,
Fuchs R.P., Dumas P.;
"Structural and biochemical analysis of sliding clamp/ligand
interactions suggest a competition between replicative and translesion
DNA polymerases.";
J. Mol. Biol. 335:1187-1197(2004).
-!- FUNCTION: Poorly processive, error-prone DNA polymerase involved
in translesion repair and untargeted mutagenesis (PubMed:10488344,
PubMed:10801133). Copies undamaged DNA at stalled replication
forks, which arise in vivo from mismatched or misaligned primer
ends. These misaligned primers can be extended by Pol IV. Exhibits
no 3'-5' exonuclease (proofreading) activity (PubMed:10488344).
Overexpression of Pol IV results in increased frameshift
mutagenesis. It is required for stationary-phase adaptive
mutation, which provides the bacterium with flexibility in dealing
with environmental stress, enhancing long-term survival and
evolutionary fitness. Not seen to be involved in translesion
snythesis even when stimulated by the beta slding-clamp and clamp-
loading complex, which do however increase non-targeted DNA
polymerase efficiency 3,000-fold, may be due to targeting to
stalled replication forks on nondamaged DNA (PubMed:10801133,
PubMed:16168375). Involved in translesional synthesis, in
conjunction with the beta clamp from PolIII (PubMed:14592985,
PubMed:14729336). {ECO:0000269|PubMed:10488344,
ECO:0000269|PubMed:10801133, ECO:0000269|PubMed:11080171,
ECO:0000269|PubMed:11463382, ECO:0000269|PubMed:11751576,
ECO:0000269|PubMed:12060704, ECO:0000269|PubMed:14592985,
ECO:0000269|PubMed:16168375, ECO:0000269|PubMed:9391106,
ECO:0000305|PubMed:14729336}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer. Interacts with beta sliding clamp, which confers
increased processivity (PubMed:14592985,
PubMed:14729336,PubMed:16168375). {ECO:0000269|PubMed:14592985,
ECO:0000269|PubMed:14729336, ECO:0000269|PubMed:16168375,
ECO:0000305}.
-!- INTERACTION:
P0A988:dnaN; NbExp=2; IntAct=EBI-1037359, EBI-542385;
P0AFF6:nusA; NbExp=3; IntAct=EBI-1037359, EBI-551571;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- INDUCTION: By SOS response. A member of the dinB-yafNOP operon
(PubMed:12813093). Induced by hydroxyurea (PubMed:20005847).
{ECO:0000269|PubMed:12813093, ECO:0000269|PubMed:20005847}.
-!- DOMAIN: The catalytic core consists of fingers, palm and thumb
subdomains, but the fingers and thumb subdomains are much smaller
than in high-fidelity polymerases; residues from five sequence
motifs of the Y-family cluster around an active site cleft that
can accommodate DNA and nucleotide substrates with relaxed
geometric constraints, with consequently higher rates of
misincorporation and low processivity. It lacks the O helices
present in high-fidelity DNA polymerases in the fingers domain (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
{ECO:0000305}.
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EMBL; D38582; BAA07593.1; -; Genomic_DNA.
EMBL; U70214; AAB08651.1; -; Genomic_DNA.
EMBL; U00096; AAC73335.1; -; Genomic_DNA.
EMBL; AP009048; BAA77901.1; -; Genomic_DNA.
EMBL; AF483080; AAL91943.1; -; Genomic_DNA.
EMBL; AF483081; AAL91944.1; -; Genomic_DNA.
EMBL; AF483082; AAL91945.1; -; Genomic_DNA.
EMBL; AF483083; AAL91946.1; -; Genomic_DNA.
EMBL; AF483084; AAL91947.1; -; Genomic_DNA.
EMBL; AF483085; AAL91948.1; -; Genomic_DNA.
EMBL; AF483086; AAL91949.1; -; Genomic_DNA.
EMBL; AF483087; AAL91950.1; -; Genomic_DNA.
EMBL; AF483088; AAL91951.1; -; Genomic_DNA.
EMBL; AF483089; AAL91952.1; -; Genomic_DNA.
EMBL; AF483090; AAL91953.1; -; Genomic_DNA.
EMBL; AF483091; AAL91954.1; -; Genomic_DNA.
EMBL; AF483092; AAL91955.1; -; Genomic_DNA.
EMBL; AF483093; AAL91956.1; -; Genomic_DNA.
EMBL; AF483094; AAL91957.1; -; Genomic_DNA.
EMBL; AF483095; AAL91958.1; -; Genomic_DNA.
EMBL; AF483096; AAL91959.1; -; Genomic_DNA.
EMBL; AF483097; AAL91960.1; -; Genomic_DNA.
EMBL; AF483098; AAL91961.1; -; Genomic_DNA.
EMBL; AF483099; AAL91962.1; -; Genomic_DNA.
EMBL; AF483100; AAL91963.1; -; Genomic_DNA.
EMBL; AF483101; AAL91964.1; -; Genomic_DNA.
EMBL; AF483102; AAL91965.1; -; Genomic_DNA.
EMBL; AF483103; AAL91966.1; -; Genomic_DNA.
EMBL; AF483104; AAL91967.1; -; Genomic_DNA.
EMBL; AF483105; AAL91968.1; -; Genomic_DNA.
PIR; H64747; H64747.
RefSeq; NP_414766.1; NC_000913.3.
RefSeq; WP_001226164.1; NZ_LN832404.1.
PDB; 1OK7; X-ray; 1.65 A; C=336-351.
PDB; 1UNN; X-ray; 1.90 A; C/D=243-351.
PDB; 4IR1; X-ray; 2.38 A; A/F=2-351.
PDB; 4IR9; X-ray; 2.33 A; A/F=2-351.
PDB; 4IRC; X-ray; 2.67 A; A/F=2-341.
PDB; 4IRD; X-ray; 2.48 A; A/F=2-341.
PDB; 4IRK; X-ray; 2.32 A; A/B=2-341.
PDB; 4Q43; X-ray; 2.45 A; A/F=2-351.
PDB; 4Q44; X-ray; 2.71 A; A/F=2-341.
PDB; 4Q45; X-ray; 2.18 A; A/F=2-341.
PDB; 4R8U; X-ray; 2.30 A; A=2-340, B=2-338.
PDB; 5C5J; X-ray; 2.10 A; A/F=2-351.
PDB; 5YUR; X-ray; 2.04 A; A/F=2-351.
PDB; 5YUT; X-ray; 2.15 A; A/F=2-351.
PDB; 5YV1; X-ray; 2.09 A; A/F=2-351.
PDB; 5YV2; X-ray; 1.90 A; A/F=2-351.
PDB; 5YV4; X-ray; 1.97 A; A/F=2-351.
PDB; 5YYD; X-ray; 2.05 A; A/F=2-351.
PDB; 5YYE; X-ray; 2.33 A; A/F=2-351.
PDBsum; 1OK7; -.
PDBsum; 1UNN; -.
PDBsum; 4IR1; -.
PDBsum; 4IR9; -.
PDBsum; 4IRC; -.
PDBsum; 4IRD; -.
PDBsum; 4IRK; -.
PDBsum; 4Q43; -.
PDBsum; 4Q44; -.
PDBsum; 4Q45; -.
PDBsum; 4R8U; -.
PDBsum; 5C5J; -.
PDBsum; 5YUR; -.
PDBsum; 5YUT; -.
PDBsum; 5YV1; -.
PDBsum; 5YV2; -.
PDBsum; 5YV4; -.
PDBsum; 5YYD; -.
PDBsum; 5YYE; -.
ProteinModelPortal; Q47155; -.
SMR; Q47155; -.
BioGrid; 4261678; 55.
IntAct; Q47155; 3.
MINT; Q47155; -.
STRING; 316385.ECDH10B_0213; -.
PaxDb; Q47155; -.
PRIDE; Q47155; -.
EnsemblBacteria; AAC73335; AAC73335; b0231.
EnsemblBacteria; BAA77901; BAA77901; BAA77901.
GeneID; 944922; -.
KEGG; ecj:JW0221; -.
KEGG; eco:b0231; -.
PATRIC; fig|1411691.4.peg.2052; -.
EchoBASE; EB2935; -.
EcoGene; EG13141; dinB.
eggNOG; ENOG4105CQ3; Bacteria.
eggNOG; COG0389; LUCA.
InParanoid; Q47155; -.
KO; K02346; -.
PhylomeDB; Q47155; -.
BioCyc; EcoCyc:G6115-MONOMER; -.
BioCyc; MetaCyc:G6115-MONOMER; -.
EvolutionaryTrace; Q47155; -.
PRO; PR:Q47155; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:EcoliWiki.
GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
GO; GO:0070987; P:error-free translesion synthesis; IBA:GO_Central.
GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
GO; GO:0009432; P:SOS response; IDA:EcoCyc.
GO; GO:0019985; P:translesion synthesis; IDA:EcoCyc.
CDD; cd03586; PolY_Pol_IV_kappa; 1.
Gene3D; 3.30.1490.100; -; 1.
HAMAP; MF_01113; DNApol_IV; 1.
InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
InterPro; IPR022880; DNApol_IV.
InterPro; IPR024728; PolY_HhH_motif.
InterPro; IPR001126; UmuC.
Pfam; PF00817; IMS; 1.
Pfam; PF11799; IMS_C; 1.
Pfam; PF11798; IMS_HHH; 1.
SUPFAM; SSF100879; SSF100879; 1.
PROSITE; PS50173; UMUC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair;
DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium;
Metal-binding; Mutator protein; Nucleotidyltransferase;
Reference proteome; Transferase.
CHAIN 1 351 DNA polymerase IV.
/FTId=PRO_0000173912.
DOMAIN 4 185 UmuC.
ACT_SITE 104 104 {ECO:0000250}.
METAL 8 8 Magnesium. {ECO:0000250}.
METAL 103 103 Magnesium. {ECO:0000250}.
SITE 13 13 Substrate discrimination. {ECO:0000250}.
VARIANT 36 38 ERR -> ARG (in strain: ECOR 45B1).
VARIANT 124 124 Q -> K (in strain: ECOR 35D).
VARIANT 132 132 N -> S (in strain: ECOR 34B1 and ECOR
37UG).
VARIANT 135 135 Q -> H (in strain: ECOR 70B1).
VARIANT 170 170 P -> S (in strain: ECOR 37UG).
VARIANT 171 171 A -> T (in strain: ECOR 45B1, ECOR 46D,
ECOR 49D and ECOR 50D).
VARIANT 176 176 L -> F (in strain: ECOR 37UG).
VARIANT 201 201 G -> S (in strain: ECOR 59B2).
VARIANT 210 210 M -> I (in strain: ECOR 37UG, ECOR 45B1,
ECOR 51B2, ECOR 52B2, ECOR 58B1 and ECOR
70B1).
VARIANT 210 210 M -> T (in strain: ECOR 35D, ECOR 46D,
ECOR 49D, ECOR 50D, ECOR 57B2, ECOR 59B2,
ECOR 60B2 and ECOR 62B2).
VARIANT 225 225 R -> C (in strain: ECOR 59B2 and ECOR
60B2).
VARIANT 310 310 A -> S (in strain: ECOR 57B2, ECOR 59B2,
ECOR 60B2 and ECOR 62B2).
VARIANT 321 321 D -> N (in strain: ECOR 35D).
MUTAGEN 8 8 D->A,H: Loss of function.
{ECO:0000269|PubMed:10488344}.
MUTAGEN 49 49 R->A,F: Loss of function.
{ECO:0000269|PubMed:10488344}.
MUTAGEN 103 103 D->A,N: Loss of function.
{ECO:0000269|PubMed:10488344}.
MUTAGEN 104 104 E->A: Loss of function.
{ECO:0000269|PubMed:10488344}.
STRAND 4 9 {ECO:0000244|PDB:5YV4}.
HELIX 12 20 {ECO:0000244|PDB:5YV4}.
HELIX 22 24 {ECO:0000244|PDB:5YV4}.
STRAND 25 27 {ECO:0000244|PDB:5YUR}.
STRAND 29 32 {ECO:0000244|PDB:5YV4}.
TURN 35 38 {ECO:0000244|PDB:5YV4}.
STRAND 40 44 {ECO:0000244|PDB:5YV4}.
HELIX 46 49 {ECO:0000244|PDB:5YV4}.
TURN 50 52 {ECO:0000244|PDB:5YV4}.
HELIX 59 65 {ECO:0000244|PDB:5YV4}.
STRAND 70 72 {ECO:0000244|PDB:5YV4}.
HELIX 76 91 {ECO:0000244|PDB:5YV4}.
STRAND 97 101 {ECO:0000244|PDB:5YV4}.
STRAND 104 108 {ECO:0000244|PDB:5YV4}.
HELIX 114 117 {ECO:0000244|PDB:5YV4}.
HELIX 119 134 {ECO:0000244|PDB:5YV4}.
STRAND 138 145 {ECO:0000244|PDB:5YV4}.
HELIX 146 155 {ECO:0000244|PDB:5YV4}.
STRAND 161 163 {ECO:0000244|PDB:5YV4}.
HELIX 166 168 {ECO:0000244|PDB:5YV4}.
HELIX 169 174 {ECO:0000244|PDB:5YV4}.
HELIX 178 180 {ECO:0000244|PDB:5YV4}.
HELIX 186 193 {ECO:0000244|PDB:5YV4}.
TURN 194 196 {ECO:0000244|PDB:5YV4}.
HELIX 200 204 {ECO:0000244|PDB:5YV4}.
HELIX 208 215 {ECO:0000244|PDB:5YV4}.
HELIX 217 225 {ECO:0000244|PDB:5YV4}.
TURN 226 228 {ECO:0000244|PDB:5YV4}.
STRAND 243 253 {ECO:0000244|PDB:1UNN}.
HELIX 256 277 {ECO:0000244|PDB:1UNN}.
STRAND 284 292 {ECO:0000244|PDB:1UNN}.
STRAND 297 303 {ECO:0000244|PDB:1UNN}.
HELIX 309 323 {ECO:0000244|PDB:1UNN}.
STRAND 329 337 {ECO:0000244|PDB:1UNN}.
SEQUENCE 351 AA; 39516 MW; 74DF44DCA18D405F CRC64;
MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK FGVRSAMPTG
MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL SLDEAYLDVT DSVHCHGSAT
LIAQEIRQTI FNELQLTASA GVAPVKFLAK IASDMNKPNG QFVITPAEVP AFLQTLPLAK
IPGVGKVSAA KLEAMGLRTC GDVQKCDLVM LLKRFGKFGR ILWERSQGID ERDVNSERLR
KSVGVERTMA EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
EHVWPRLNKA DLIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG L


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