TN5P_ECOLX
ID TN5P_ECOLX Reviewed; 476 AA.
AC Q46731; Q08JA5; Q47661; Q57460;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Transposase for transposon Tn5;
DE EC=3.1.-.-;
DE AltName: Full=Tnp;
GN Name=tnpA; Synonyms=tnp;
OS Escherichia coli.
OG Plasmid pO86A1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RX PubMed=6260374; DOI=10.1016/0092-8674(81)90284-1;
RA Rothstein S.J., Reznikoff W.S.;
RT "The functional differences in the inverted repeats of Tn5 are caused by a
RT single base pair nonhomology.";
RL Cell 23:191-199(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=6271452; DOI=10.1101/sqb.1981.045.01.019;
RA Auerswald E.A., Ludwig G., Schaller H.;
RT "Structural analysis of Tn5.";
RL Cold Spring Harb. Symp. Quant. Biol. 45:107-113(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7867940; DOI=10.1016/0378-1119(94)00854-l;
RA Ahmed A., Podemski L.;
RT "The revised nucleotide sequence of Tn5.";
RL Gene 154:129-130(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=DIJ1; PLASMID=pO86A1;
RA Yamamoto T.;
RT "pO86A1 is a Tn5-insert derivative of adherence plasmid pO86A in strain
RT DIJ1.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND ALTERNATIVE PROMOTER USAGE.
RX PubMed=2438419; DOI=10.1016/0022-2836(86)90028-8;
RA Krebs M.P., Reznikoff W.S.;
RT "Transcriptional and translational initiation sites of IS50. Control of
RT transposase and inhibitor expression.";
RL J. Mol. Biol. 192:781-791(1986).
RN [6]
RP FUNCTION.
RX PubMed=6291786; DOI=10.1016/0092-8674(82)90292-6;
RA Johnson R.C., Yin J.C.P., Reznikoff W.S.;
RT "Control of Tn5 transposition in Escherichia coli is mediated by protein
RT from the right repeat.";
RL Cell 30:873-882(1982).
RN [7]
RP FUNCTION.
RX PubMed=6303899; DOI=10.1093/genetics/103.4.605;
RA Lowe J.B., Berg D.E.;
RT "A product of the Tn5 transposase gene inhibits transposition.";
RL Genetics 103:605-615(1983).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF MET-56; GLU-110 AND GLU-345.
RX PubMed=1310499; DOI=10.1128/jb.174.4.1229-1239.1992;
RA Wiegand T.W., Reznikoff W.S.;
RT "Characterization of two hypertransposing Tn5 mutants.";
RL J. Bacteriol. 174:1229-1239(1992).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8226636; DOI=10.1128/jb.175.21.6932-6938.1993;
RA de la Cruz N.B., Weinreich M.D., Wiegand T.W., Krebs M.P., Reznikoff W.S.;
RT "Characterization of the Tn5 transposase and inhibitor proteins: a model
RT for the inhibition of transposition.";
RL J. Bacteriol. 175:6932-6938(1993).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8871560; DOI=10.1093/nar/24.19.3790;
RA York D., Reznikoff W.S.;
RT "Purification and biochemical analyses of a monomeric form of Tn5
RT transposase.";
RL Nucleic Acids Res. 24:3790-3796(1996).
RN [11]
RP MUTAGENESIS OF TYR-41; THR-47 AND GLU-54.
RX PubMed=9268665; DOI=10.1006/jmbi.1997.1188;
RA Zhou M., Reznikoff W.S.;
RT "Tn5 transposase mutants that alter DNA binding specificity.";
RL J. Mol. Biol. 271:362-373(1997).
RN [12]
RP MUTAGENESIS OF ARG-30; LYS-40 AND ARG-62.
RX PubMed=11283001; DOI=10.1074/jbc.m010748200;
RA Twining S.S., Goryshin I.Y., Bhasin A., Reznikoff W.S.;
RT "Functional characterization of arginine 30, lysine 40, and arginine 62 in
RT Tn5 transposase.";
RL J. Biol. Chem. 276:23135-23143(2001).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF ASP-97; ASP-188; TYR-319; ARG-322; GLU-326;
RP LYS-330 AND LYS-333.
RX PubMed=11877443; DOI=10.1074/jbc.m200742200;
RA Naumann T.A., Reznikoff W.S.;
RT "Tn5 transposase active site mutants.";
RL J. Biol. Chem. 277:17623-17629(2002).
RN [14]
RP MUTAGENESIS OF ARG-342; GLU-344; ASN-348; SER-438; LYS-439 AND SER-445.
RX PubMed=17693501; DOI=10.1128/jb.00524-07;
RA Vaezeslami S., Sterling R., Reznikoff W.S.;
RT "Site-directed mutagenesis studies of Tn5 transposase residues involved in
RT synaptic complex formation.";
RL J. Bacteriol. 189:7436-7441(2007).
RN [15]
RP REVIEW.
RX PubMed=18680433; DOI=10.1146/annurev.genet.42.110807.091656;
RA Reznikoff W.S.;
RT "Transposon tn5.";
RL Annu. Rev. Genet. 42:269-286(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 56-476.
RX PubMed=10207011; DOI=10.1074/jbc.274.17.11904;
RA Davies D.R., Mahnke Braam L., Reznikoff W.S., Rayment I.;
RT "The three-dimensional structure of a Tn5 transposase-related protein
RT determined to 2.9-A resolution.";
RL J. Biol. Chem. 274:11904-11913(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT LYS-54/ALA-56/PRO-372 IN
RP COMPLEX WITH DNA AND MANGANESE IONS, COFACTOR, AND SUBUNIT.
RX PubMed=10884228; DOI=10.1126/science.289.5476.77;
RA Davies D.R., Goryshin I.Y., Reznikoff W.S., Rayment I.;
RT "Three-dimensional structure of the Tn5 synaptic complex transposition
RT intermediate.";
RL Science 289:77-85(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT
RP LYS-54/ALA-56/LYS-345/PRO-372 IN COMPLEX WITH DNA AND MANGANESE IONS, AND
RP FUNCTION.
RX PubMed=12367522; DOI=10.1016/s0022-2836(02)00877-x;
RA Steiniger-White M., Bhasin A., Lovell S., Rayment I., Reznikoff W.S.;
RT "Evidence for 'unseen' transposase-DNA contacts.";
RL J. Mol. Biol. 322:971-982(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT
RP LYS-54/ALA-56/LYS-119/ALA-120/LYS-345/PRO-372 IN COMPLEX WITH MANGANESE
RP IONS AND DNA, COFACTOR, AND SUBUNIT.
RX PubMed=11896402; DOI=10.1038/nsb778;
RA Lovell S., Goryshin I.Y., Reznikoff W.R., Rayment I.;
RT "Two-metal active site binding of a Tn5 transposase synaptic complex.";
RL Nat. Struct. Biol. 9:278-281(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT
RP LYS-54/ALA-56/LYS-119/ALA-120/LYS-345/PRO-372 IN COMPLEX WITH DNA AND
RP MANGANESE IONS, SUBUNIT, AND COFACTOR.
RX PubMed=15102449; DOI=10.1016/j.sbi.2004.01.008;
RA Steiniger-White M., Rayment I., Reznikoff W.S.;
RT "Structure/function insights into Tn5 transposition.";
RL Curr. Opin. Struct. Biol. 14:50-57(2004).
CC -!- FUNCTION: Mediates transposition of transposon Tn5 by a 'cut and paste'
CC mechanism. First, the monomeric transposase binds the 19 bp inverted
CC DNA repeats flanking the transposon. Then, dimerization of the DNA-
CC bound transposase creates a synaptic DNA complex. After nicking of the
CC first DNA strand, excision of the transposon proceeds through a series
CC of intermediates. The transposase then mediates the insertion of the
CC transposon at a new site by strand transfer. The activity of the wild-
CC type transposase is very low, and is further inhibited by dimerization
CC with the transposase inhibitor (inh). {ECO:0000269|PubMed:11877443,
CC ECO:0000269|PubMed:12367522, ECO:0000269|PubMed:1310499,
CC ECO:0000269|PubMed:6260374, ECO:0000269|PubMed:6291786,
CC ECO:0000269|PubMed:6303899, ECO:0000269|PubMed:8226636,
CC ECO:0000269|PubMed:8871560}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10884228, ECO:0000269|PubMed:11896402,
CC ECO:0000269|PubMed:15102449};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:10884228,
CC ECO:0000269|PubMed:11896402, ECO:0000269|PubMed:15102449};
CC -!- SUBUNIT: Monomer. Homodimer of tnp (isoform 1), and heterodimer of tnp
CC (isoform 1) and inh (isoform 2). {ECO:0000269|PubMed:10884228,
CC ECO:0000269|PubMed:11896402, ECO:0000269|PubMed:12367522,
CC ECO:0000269|PubMed:15102449, ECO:0000269|PubMed:8226636,
CC ECO:0000269|PubMed:8871560}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=Transposase, Tnp;
CC IsoId=Q46731-1; Sequence=Displayed;
CC Name=2; Synonyms=Transposition inhibitor, Inh;
CC IsoId=Q46731-2; Sequence=VSP_035522;
CC -!- MISCELLANEOUS: Tn5 is a bacterial transposon that contains three genes
CC conferring resistance to the antibiotics kanamycin/neomycin, bleomycin
CC and streptomycin, flanked by two IS50 elements. IS50R codes for the
CC functional transposase (isoform 1) and for the transposition inhibitor
CC (isoform 2). IS50L differs by one nucleotide, giving rise to an ochre
CC stop codon and producing C-terminally truncated proteins that lack
CC transposase activity.
CC -!- MISCELLANEOUS: [Isoform 2]: Expressed at 4 times higher levels than
CC isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transposase 11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF34032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00004; AAA73393.1; -; Genomic_DNA.
DR EMBL; U00004; AAA73394.1; -; Genomic_DNA.
DR EMBL; V00617; CAA23891.1; -; Genomic_DNA.
DR EMBL; U15573; AAB60064.1; -; Genomic_DNA.
DR EMBL; AB255435; BAF34032.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000633033.1; NZ_RRGJ01000093.1.
DR RefSeq; YP_788129.1; NC_008460.1.
DR PDB; 1B7E; X-ray; 2.90 A; A=56-476.
DR PDB; 1MM8; X-ray; 2.80 A; A=1-476.
DR PDB; 1MUH; X-ray; 2.30 A; A=1-476.
DR PDB; 1MUS; X-ray; 1.90 A; A=1-476.
DR PDB; 3ECP; X-ray; 2.50 A; A=1-476.
DR PDB; 4DM0; X-ray; 2.50 A; A=1-476.
DR PDBsum; 1B7E; -.
DR PDBsum; 1MM8; -.
DR PDBsum; 1MUH; -.
DR PDBsum; 1MUS; -.
DR PDBsum; 3ECP; -.
DR PDBsum; 4DM0; -.
DR AlphaFoldDB; Q46731; -.
DR SMR; Q46731; -.
DR DIP; DIP-17010N; -.
DR BRENDA; 2.7.7.B22; 2026.
DR EvolutionaryTrace; Q46731; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004803; F:transposase activity; IEA:InterPro.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro.
DR Gene3D; 1.10.246.40; -; 1.
DR Gene3D; 1.10.740.10; -; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR038215; TN5-like_N_sf.
DR InterPro; IPR002559; Transposase_11.
DR InterPro; IPR014737; Transposase_Tn5-like_C.
DR InterPro; IPR014735; Transposase_Tn5-like_N.
DR Pfam; PF01609; DDE_Tnp_1; 1.
DR Pfam; PF14706; Tnp_DNA_bind; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Direct protein sequencing;
KW DNA recombination; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Plasmid; Transposable element; Transposition.
FT CHAIN 1..476
FT /note="Transposase for transposon Tn5"
FT /id="PRO_0000351545"
FT REGION 1..70
FT /note="Interaction with DNA"
FT REGION 237..255
FT /note="Interaction with DNA"
FT REGION 319..348
FT /note="Interaction with DNA"
FT REGION 369..476
FT /note="Important for dimerization"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT SITE 210
FT /note="Interaction with DNA"
FT SITE 298
FT /note="Interaction with DNA"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035522"
FT MUTAGEN 30
FT /note="R->Q: Loss of transposase activity."
FT /evidence="ECO:0000269|PubMed:11283001"
FT MUTAGEN 40
FT /note="K->Q: Strongly reduced transposase activity."
FT /evidence="ECO:0000269|PubMed:11283001"
FT MUTAGEN 41
FT /note="Y->H: Enhances interaction with DNA and increases
FT transposition frequency."
FT /evidence="ECO:0000269|PubMed:9268665"
FT MUTAGEN 47
FT /note="T->P: Enhances interaction with DNA and increases
FT transposition frequency."
FT /evidence="ECO:0000269|PubMed:9268665"
FT MUTAGEN 54
FT /note="E->K,V: Enhances interaction with DNA and increases
FT transposition frequency."
FT /evidence="ECO:0000269|PubMed:9268665"
FT MUTAGEN 56
FT /note="M->A: Abolishes expression of the transposase
FT inhibitor Inh (isoform 2)."
FT /evidence="ECO:0000269|PubMed:1310499"
FT MUTAGEN 62
FT /note="R->Q: Loss of transposase activity."
FT /evidence="ECO:0000269|PubMed:11283001"
FT MUTAGEN 97
FT /note="D->A: Loss of transposase activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 110
FT /note="E->K: Enhances transposase activity."
FT /evidence="ECO:0000269|PubMed:1310499"
FT MUTAGEN 188
FT /note="D->A: Loss of transposase activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 319
FT /note="Y->A: Loss of strand transfer activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 322
FT /note="R->A,K: Loss of strand transfer activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 322
FT /note="R->Q: Strongly reduced strand transfer activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 326
FT /note="E->A: Loss of transposase activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 330
FT /note="K->A: Reduced transposase activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 330
FT /note="K->R: No effect."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 333
FT /note="K->A,R: Strongly reduced DNA cleavage. Loss of
FT strand transfer activity."
FT /evidence="ECO:0000269|PubMed:11877443"
FT MUTAGEN 342
FT /note="R->A: Abolishes formation of the synaptic complex
FT and transposition."
FT /evidence="ECO:0000269|PubMed:17693501"
FT MUTAGEN 344
FT /note="E->A: Enhances transposase activity."
FT /evidence="ECO:0000269|PubMed:17693501"
FT MUTAGEN 345
FT /note="E->K: Enhances transposase activity."
FT /evidence="ECO:0000269|PubMed:1310499"
FT MUTAGEN 348
FT /note="N->A: Reduces formation of synaptic complex and
FT transposition."
FT /evidence="ECO:0000269|PubMed:17693501"
FT MUTAGEN 372
FT /note="L->P: Enhances transposase activity."
FT MUTAGEN 438
FT /note="S->A: Abolishes formation of the synaptic complex
FT and transposition."
FT /evidence="ECO:0000269|PubMed:17693501"
FT MUTAGEN 439
FT /note="K->A: Abolishes formation of synaptic complex and
FT transposition."
FT /evidence="ECO:0000269|PubMed:17693501"
FT MUTAGEN 445
FT /note="S->A: Reduces formation of synaptic complex and
FT transposition."
FT /evidence="ECO:0000269|PubMed:17693501"
FT MUTAGEN 462
FT /note="G->D: Abolishes formation of the synaptic complex
FT and transposition."
FT MUTAGEN 466
FT /note="A->D: Abolishes formation of the synaptic complex
FT and transposition."
FT CONFLICT 64
FT /note="I -> Y (in Ref. 1; AAA73393/AAA73394 and 2;
FT CAA23891)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> R (in Ref. 1; AAA73393/AAA73394 and 2;
FT CAA23891)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Y -> I (in Ref. 1; AAA73393/AAA73394 and 2;
FT CAA23891)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="S -> G (in Ref. 1; AAA73393/AAA73394 and 2;
FT CAA23891)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3ECP"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3ECP"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:1MUS"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1MUS"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:1MUS"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1MUS"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 259..272
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 277..288
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:1MUS"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 346..370
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:1B7E"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1MUS"
FT HELIX 399..409
FT /evidence="ECO:0007829|PDB:1MUS"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1B7E"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1MM8"
FT HELIX 422..432
FT /evidence="ECO:0007829|PDB:1MUS"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1B7E"
FT HELIX 446..471
FT /evidence="ECO:0007829|PDB:1MUS"
SQ SEQUENCE 476 AA; 53306 MW; B52F2F143646AF10 CRC64;
MITSALHRAA DWAKSVFSSA ALGDPRRTAR LVNVAAQLAK YSGKSITISS EGSEAMQEGA
YRFIRNPNVS AEAIRKAGAM QTVKLAQEFP ELLAIEDTTS LSYRHQVAEE LGKLGSIQDK
SRGWWVHSVL LLEATTFRTV GLLHQEWWMR PDDPADADEK ESGKWLAAAA TSRLRMGSMM
SNVIAVCDRE ADIHAYLQDK LAHNERFVVR SKHPRKDVES GLYLYDHLKN QPELGGYQIS
IPQKGVVDKR GKRKNRPARK ASLSLRSGRI TLKQGNITLN AVLAEEINPP KGETPLKWLL
LTSEPVESLA QALRVIDIYT HRWRIEEFHK AWKTGAGAER QRMEEPDNLE RMVSILSFVA
VRLLQLRESF TLPQALRAQG LLKEAEHVES QSAETVLTPD ECQLLGYLDK GKRKRKEKAG
SLQWAYMAIA RLGGFMDSKR TGIASWGALW EGWEALQSKL DGFLAAKDLM AQGIKI
