RDRP_BPQBE
ID RDRP_BPQBE Reviewed; 589 AA.
AC P14647; D0U1F4; D0U1F8; D0U1G6; G4WZR0; G4WZR4; Q8LTE0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=RNA-directed RNA polymerase subunit beta;
DE EC=2.7.7.48 {ECO:0000269|PubMed:22245970};
DE AltName: Full=RNA replicase beta chain;
DE AltName: Full=RNA-directed RNA polymerase subunit II {ECO:0000303|PubMed:816798};
OS Escherichia virus Qbeta (Bacteriophage Q-beta).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Allolevivirus.
OX NCBI_TaxID=39803;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2538637; DOI=10.1016/0022-2836(89)90319-7;
RA Mills D.R., Priano C., Dimauro P., Binderow B.D.;
RT "Q-beta replicase: mapping the functional domains of an RNA-dependent RNA
RT polymerase.";
RL J. Mol. Biol. 205:751-764(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Mekler P.;
RL Thesis (1981), University of Zurich, Switzerland.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14667253; DOI=10.1186/1471-2148-3-24;
RA Bacher J.M., Bull J.J., Ellington A.D.;
RT "Evolution of phage with chemically ambiguous proteomes.";
RL BMC Evol. Biol. 3:24-24(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=QB_1 {ECO:0000312|EMBL:ACY07225.1},
RC QB_2 {ECO:0000312|EMBL:ACY07229.1}, and
RC QB_ancestral {ECO:0000312|EMBL:ACY07237.1};
RX PubMed=19956760; DOI=10.1371/journal.pgen.1000742;
RA Domingo-Calap P., Cuevas J.M., Sanjuan R.;
RT "The fitness effects of random mutations in single-stranded DNA and RNA
RT bacteriophages.";
RL PLoS Genet. 5:E1000742-E1000742(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Qbeta_1_FR, and Qbeta_2_FR {ECO:0000312|EMBL:AEQ25547.1};
RX PubMed=21967437; DOI=10.1111/j.1558-5646.2011.01339.x;
RA Domingo-Calap P., Sanjuan R.;
RT "Experimental evolution of RNA versus DNA viruses.";
RL Evolution 65:2987-2994(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Anc;
RX PubMed=25056887; DOI=10.1128/jvi.01127-14;
RA Kashiwagi A., Sugawara R., Sano-Tsushima F., Kumagai T., Yomo T.;
RT "Contribution of silent mutations to thermal adaptation of RNA
RT bacteriophage Qbeta.";
RL J. Virol. 88:11459-11468(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-23.
RX PubMed=1247542; DOI=10.1016/0005-2787(76)90067-8;
RA Weber H.;
RT "The binding site for coat protein on bacteriophage Q-beta RNA.";
RL Biochim. Biophys. Acta 418:175-183(1976).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=58611;
RA Kondo M.;
RT "Structure and function of RNA replicase of bacteriophage Qbeta.";
RL Arch. Int. Physiol. Biochim. 83:909-948(1975).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=816798; DOI=10.1016/s0021-9258(17)33551-2;
RA Carmichael G.G., Landers T.A., Weber K.;
RT "Immunochemical analysis of the functions of the subunits of phage Qbeta
RT ribonucleic acid replicase.";
RL J. Biol. Chem. 251:2744-2748(1976).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=6358207; DOI=10.1016/s0021-9258(17)43965-2;
RA Guerrier-Takada C., Subramanian A.R., Cole P.E.;
RT "The activity of discrete fragments of ribosomal protein S1 in Q beta
RT replicase function.";
RL J. Biol. Chem. 258:13649-13652(1983).
RN [11]
RP CONSTRUCT TO PRODUCE VIRAL CATALYTIC CORE.
RX PubMed=16781472; DOI=10.1263/jbb.101.421;
RA Kita H., Cho J., Matsuura T., Nakaishi T., Taniguchi I., Ichikawa T.,
RA Shima Y., Urabe I., Yomo T.;
RT "Functional Qbeta replicase genetically fusing essential subunits EF-Ts and
RT EF-Tu with beta-subunit.";
RL J. Biosci. Bioeng. 101:421-426(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF VIRAL CATALYTIC CORE, FUNCTION,
RP AND SUBUNIT.
RX PubMed=20534494; DOI=10.1073/pnas.1003015107;
RA Kidmose R.T., Vasiliev N.N., Chetverin A.B., Andersen G.R., Knudsen C.R.;
RT "Structure of the Qbeta replicase, an RNA-dependent RNA polymerase
RT consisting of viral and host proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10884-10889(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF VIRAL CATALYTIC CORE IN COMPLEX
RP WITH CALCIUM, FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF LYS-78;
RP ARG-153; ARG-164; LYS-214; ARG-220; ASP-274; SER-279; TYR-357; ASP-359;
RP ASP-360; GLU-395; TYR-411 AND ARG-413.
RX PubMed=20798060; DOI=10.1073/pnas.1006559107;
RA Takeshita D., Tomita K.;
RT "Assembly of Q{beta} viral RNA polymerase with host translational
RT elongation factors EF-Tu and -Ts.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15733-15738(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF VIRAL CATALYTIC CORE IN COMPLEX
RP WITH CALCIUM, FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-168; ARG-241;
RP PHE-329; TYR-357; TYR-511 AND ASN-549, AND CATALYTIC ACTIVITY.
RX PubMed=22245970; DOI=10.1038/nsmb.2204;
RA Takeshita D., Tomita K.;
RT "Molecular basis for RNA polymerization by Qbeta replicase.";
RL Nat. Struct. Mol. Biol. 19:229-237(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF VIRAL CATALYTIC CORE IN COMPLEX
RP WITH CALCIUM, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=22884418; DOI=10.1016/j.str.2012.07.004;
RA Takeshita D., Yamashita S., Tomita K.;
RT "Mechanism for template-independent terminal adenylation activity of Qbeta
RT replicase.";
RL Structure 20:1661-1669(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-589 OF THE REPLICASE COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=25122749; DOI=10.1093/nar/gku745;
RA Takeshita D., Yamashita S., Tomita K.;
RT "Molecular insights into replication initiation by Qbeta replicase using
RT ribosomal protein S1.";
RL Nucleic Acids Res. 42:10809-10822(2014).
RN [17] {ECO:0007744|PDB:4R71}
RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF THE REPLICASE COMPLEX, FUNCTION,
RP RNA-BINDING, SUBUNIT, AND MUTAGENESIS OF ARG-132; ARG-133; LYS-134;
RP LYS-137; GLU-345; ASP-348 AND ASP-350.
RX PubMed=26578560; DOI=10.1093/nar/gkv1212;
RA Gytz H., Mohr D., Seweryn P., Yoshimura Y., Kutlubaeva Z., Dolman F.,
RA Chelchessa B., Chetverin A.B., Mulder F.A., Brodersen D.E., Knudsen C.R.;
RT "Structural basis for RNA-genome recognition during bacteriophage Qbeta
RT replication.";
RL Nucleic Acids Res. 43:10893-10906(2015).
CC -!- FUNCTION: This is the catalytic subunit of the viral RNA-dependent RNA
CC polymerase complex. This complex is involved in viral RNA replication
CC that produces (+)-stranded genomes via a complementary, (-)-stranded
CC intermediate. Binds RNA cooperatively with the host ribosomal protein
CC S1. {ECO:0000269|PubMed:20534494, ECO:0000269|PubMed:20798060,
CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418,
CC ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:26578560,
CC ECO:0000269|PubMed:58611, ECO:0000269|PubMed:6358207,
CC ECO:0000269|PubMed:816798}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539,
CC ECO:0000269|PubMed:22245970};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
CC ECO:0000269|PubMed:22884418};
CC Note=Binds 2 Mg(2+) per subunit, Ca(2+) is used in crystallization to
CC prevent RNA polymerase activity. {ECO:0000269|PubMed:20798060,
CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418};
CC -!- SUBUNIT: Homodimer; the replicase complex can dimerize. Part of the
CC viral RNA-dependent RNA polymerase complex, the other subunits are the
CC host ribosomal protein S1, EF-Tu and EF-Ts. S1 is needed for the
CC initiation of genomic RNA (+)-strand replication.
CC {ECO:0000269|PubMed:1247542, ECO:0000269|PubMed:20534494,
CC ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
CC ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749,
CC ECO:0000269|PubMed:58611, ECO:0000269|PubMed:6358207,
CC ECO:0000269|PubMed:816798}.
CC -!- INTERACTION:
CC P14647; P0A6P1: tsf; Xeno; NbExp=2; IntAct=EBI-9010000, EBI-301164;
CC P14647; P0CE47: tufA; Xeno; NbExp=2; IntAct=EBI-9010000, EBI-301077;
CC -!- MISCELLANEOUS: In order to produce high amounts of RNA polymerase
CC catalytic core, a fusion protein consisting of tsf-tufB-replicase with
CC a cleavable linker between tufB and the viral replicase subunit is
CC frequently used. {ECO:0000269|PubMed:16781472,
CC ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
CC ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749}.
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DR EMBL; X14764; CAA32872.1; -; mRNA.
DR EMBL; AY099114; AAM33128.1; -; Genomic_RNA.
DR EMBL; GQ153928; ACY07225.1; -; Genomic_RNA.
DR EMBL; GQ153929; ACY07229.1; -; Genomic_RNA.
DR EMBL; AB971354; BAP18765.1; -; Genomic_RNA.
DR EMBL; JF719735; AEQ25543.1; -; Genomic_RNA.
DR EMBL; JF719736; AEQ25547.1; -; Genomic_RNA.
DR EMBL; GQ153931; ACY07237.1; -; Genomic_RNA.
DR EMBL; M24876; AAA50307.1; -; Genomic_RNA.
DR PIR; S03340; RRBPBQ.
DR PDB; 3AGP; X-ray; 2.80 A; A=1-589.
DR PDB; 3AGQ; X-ray; 3.22 A; A=1-589.
DR PDB; 3AVT; X-ray; 2.61 A; A=1-589.
DR PDB; 3AVU; X-ray; 2.91 A; A=1-589.
DR PDB; 3AVV; X-ray; 3.12 A; A=1-589.
DR PDB; 3AVW; X-ray; 2.60 A; A=1-589.
DR PDB; 3AVX; X-ray; 2.41 A; A=1-589.
DR PDB; 3AVY; X-ray; 2.62 A; A=1-589.
DR PDB; 3MMP; X-ray; 2.50 A; F/G=1-589.
DR PDB; 3VNU; X-ray; 3.20 A; A=1-589.
DR PDB; 3VNV; X-ray; 2.60 A; A=1-589.
DR PDB; 4FWT; X-ray; 3.20 A; A=1-589.
DR PDB; 4Q7J; X-ray; 2.90 A; C/G=2-589.
DR PDB; 4R71; X-ray; 3.21 A; B/D=1-589.
DR PDBsum; 3AGP; -.
DR PDBsum; 3AGQ; -.
DR PDBsum; 3AVT; -.
DR PDBsum; 3AVU; -.
DR PDBsum; 3AVV; -.
DR PDBsum; 3AVW; -.
DR PDBsum; 3AVX; -.
DR PDBsum; 3AVY; -.
DR PDBsum; 3MMP; -.
DR PDBsum; 3VNU; -.
DR PDBsum; 3VNV; -.
DR PDBsum; 4FWT; -.
DR PDBsum; 4Q7J; -.
DR PDBsum; 4R71; -.
DR SMR; P14647; -.
DR DIP; DIP-59375N; -.
DR IntAct; P14647; 2.
DR BRENDA; 2.7.7.48; 727.
DR Proteomes; UP000185268; Genome.
DR Proteomes; UP000305125; Genome.
DR Proteomes; UP000306921; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR007096; RNA-dir_Rpol_phage_catalytic.
DR InterPro; IPR005093; RNArep_beta.
DR Pfam; PF03431; RNA_replicase_B; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50522; RDRP_PHAGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..589
FT /note="RNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000164855"
FT DOMAIN 259..391
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418"
FT VARIANT 71
FT /note="L -> F (in strain:QB_1)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 130
FT /note="M -> I (in strain: QB_ancestral, QB_1, QB_2,
FT Qbeta_1_FR and Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:19956760,
FT ECO:0000269|PubMed:21967437"
FT VARIANT 198
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:2538637, ECO:0000269|Ref.2"
FT VARIANT 251
FT /note="L -> R (in strain:QB_1 and Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:19956760,
FT ECO:0000269|PubMed:21967437"
FT VARIANT 418
FT /note="S -> G (in strain:QB_1 and Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 500
FT /note="D -> G (in strain:QB_2 and Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:19956760,
FT ECO:0000269|PubMed:21967437"
FT MUTAGEN 78
FT /note="K->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 132
FT /note="R->M: Complete loss of infectivity; when associated
FT with M-133."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 133
FT /note="R->M: Complete loss of infectivity; when associated
FT with M-132."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 134
FT /note="K->A: Complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 137
FT /note="K->M: Complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 153
FT /note="R->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 164
FT /note="R->A: 80% loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 168
FT /note="H->A: 80% loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:22245970"
FT MUTAGEN 214
FT /note="K->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 220
FT /note="R->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 241
FT /note="R->A: Decreased initiation of RNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:22245970"
FT MUTAGEN 274
FT /note="D->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 279
FT /note="S->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 329
FT /note="F->A: Decreased initiation of RNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:22245970"
FT MUTAGEN 345
FT /note="E->A: Almost complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 348
FT /note="D->A: 80% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 350
FT /note="D->A: 95% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:26578560"
FT MUTAGEN 357
FT /note="Y->A: Decreased initiation of RNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:20798060,
FT ECO:0000269|PubMed:22245970"
FT MUTAGEN 359
FT /note="D->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 360
FT /note="D->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 395
FT /note="E->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 411
FT /note="Y->A: 60% loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 413
FT /note="R->A: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 511
FT /note="Y->A: 50% loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:22245970"
FT MUTAGEN 549
FT /note="N->A: 25% loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:22245970"
FT MUTAGEN 549
FT /note="N->G: 50% loss of RNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:22245970"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:4R71"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3VNU"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:3AVX"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3AVV"
FT HELIX 90..110
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 123..139
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4Q7J"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3AVX"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3AVV"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3VNV"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:3AGQ"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3AVW"
FT HELIX 328..346
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 368..377
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:3AGP"
FT HELIX 441..451
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:3AVV"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:3AVX"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 488..500
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 505..520
FT /evidence="ECO:0007829|PDB:3AVX"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:3MMP"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:3AVX"
FT STRAND 554..566
FT /evidence="ECO:0007829|PDB:3AVX"
SQ SEQUENCE 589 AA; 65531 MW; 8C02DB50F7202DEF CRC64;
MSKTASSRNS LSAQLRRAAN TRIEVEGNLA LSIANDLLLA YGQSPFNSEA ECISFSPRFD
GTPDDFRINY LKAEIMSKYD DFSLGIDTEA VAWEKFLAAE AECALTNARL YRPDYSEDFN
FSLGESCIHM ARRKIAKLIG DVPSVEGMLR HCRFSGGATT TNNRSYGHPS FKFALPQACT
PRALKYVLAL RASTHFDIRI SDISPFNKAV TVPKNSKTDR CIAIEPGWNM FFQLGIGGIL
RDRLRCWGID LNDQTINQRR AHEGSVTNNL ATVDLSAASD SISLALCELL LPPGWFEVLM
DLRSPKGRLP DGSVVTYEKI SSMGNGYTFE LESLIFASLA RSVCEILDLD SSEVTVYGDD
IILPSCAVPA LREVFKYVGF TTNTKKTFSE GPFRESCGKH YYSGVDVTPF YIRHRIVSPA
DLILVLNNLY RWATIDGVWD PRAHSVYLKY RKLLPKQLQR NTIPDGYGDG ALVGSVLINP
FAKNRGWIRY VPVITDHTRD RERAELGSYL YDLFSRCLSE SNDGLPLRGP SGCDSADLFA
IDQLICRSNP TKISRSTGKF DIQYIACSSR VLAPYGVFQG TKVASLHEA
