TRAI1_ECOLI
ID TRAI1_ECOLI Reviewed; 1756 AA.
AC P14565; Q51811;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Multifunctional conjugation protein TraI;
DE Includes:
DE RecName: Full=DNA relaxase TraI;
DE EC=5.6.2.1;
DE AltName: Full=DNA nickase TraI;
DE AltName: Full=Transesterase TraI;
DE Includes:
DE RecName: Full=DNA helicase I;
DE EC=3.6.4.12;
GN Name=traI; OrderedLocusNames=ECOK12F104;
OS Escherichia coli (strain K12).
OG Plasmid F.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC PLASMID=F;
RX PubMed=2163400; DOI=10.1128/jb.172.7.4127-4131.1990;
RA Bradshaw H.D. Jr., Traxler B.A., Minkley E.G. Jr., Nester E.W.,
RA Gordon M.P.;
RT "Nucleotide sequence of the traI (helicase I) gene from the sex factor F.";
RL J. Bacteriol. 172:4127-4131(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=F;
RX PubMed=7915817; DOI=10.1128/mr.58.2.162-210.1994;
RA Frost L.S., Ippen-Ihler K., Skurray R.A.;
RT "Analysis of the sequence and gene products of the transfer region of the F
RT sex factor.";
RL Microbiol. Rev. 58:162-210(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / CR63; PLASMID=F;
RA Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT "Complete nucleotide sequence of the F plasmid: its implications for
RT organization and diversification of plasmid genomes.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
RC STRAIN=K12; PLASMID=F;
RX PubMed=2680768; DOI=10.1016/0378-1119(89)90179-0;
RA Jalajakumari M.B., Manning P.A.;
RT "Nucleotide sequence of the traD region in the Escherichia coli F sex
RT factor.";
RL Gene 81:195-202(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC PLASMID=F;
RX PubMed=2164585; DOI=10.1016/0022-2836(90)90145-c;
RA Yoshioka Y., Fujita Y., Ohtsubo E.;
RT "Nucleotide sequence of the promoter-distal region of the tra operon of
RT plasmid R100, including traI (DNA helicase I) and traD genes.";
RL J. Mol. Biol. 214:39-53(1990).
RN [6]
RP PROTEIN SEQUENCE OF 1-5, FUNCTION IN SS-DNA DIGESTION, SUBUNIT,
RP CHARACTERIZATION OF RELAXASE CATALYTIC RESIDUES, AND MUTAGENESIS OF TYR-16;
RP TYR-17; TYR-23 AND TYR-24.
RC PLASMID=F;
RX PubMed=12637015; DOI=10.1016/s1570-9639(02)00553-8;
RA Street L.M., Harley M.J., Stern J.C., Larkin C., Williams S.L.,
RA Miller D.L., Dohm J.A., Rodgers M.E., Schildbach J.F.;
RT "Subdomain organization and catalytic residues of the F factor TraI
RT relaxase domain.";
RL Biochim. Biophys. Acta 1646:86-99(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-1756.
RC PLASMID=F;
RX PubMed=8736534; DOI=10.1046/j.1365-2958.1996.5361059.x;
RA Penfold S.S., Simon J., Frost L.S.;
RT "Regulation of the expression of the traM gene of the F sex factor of
RT Escherichia coli.";
RL Mol. Microbiol. 20:549-558(1996).
RN [8]
RP FUNCTION AS DNA HELICASE I.
RC PLASMID=F;
RX PubMed=6308637; DOI=10.1073/pnas.80.15.4659;
RA Abdel-Monem M., Taucher-Scholz G., Klinkert M.Q.;
RT "Identification of Escherichia coli DNA helicase I as the traI gene product
RT of the F sex factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4659-4663(1983).
RN [9]
RP FUNCTION IN COVALENT BINDING TO SS-DNA.
RC PLASMID=F;
RX PubMed=8386720; DOI=10.1128/jb.175.9.2599-2606.1993;
RA Matson S.W., Nelson W.C., Morton B.S.;
RT "Characterization of the reaction product of the oriT nicking reaction
RT catalyzed by Escherichia coli DNA helicase I.";
RL J. Bacteriol. 175:2599-2606(1993).
RN [10]
RP FUNCTION IN F PLASMID NICKING.
RC PLASMID=F;
RX PubMed=7499339; DOI=10.1074/jbc.270.47.28381;
RA Nelson W.C., Howard M.T., Sherman J.A., Matson S.W.;
RT "The traY gene product and integration host factor stimulate Escherichia
RT coli DNA helicase I-catalyzed nicking at the F plasmid oriT.";
RL J. Biol. Chem. 270:28374-28380(1995).
RN [11]
RP CHARACTERIZATION OF RELAXOSOME ASSEMBLY ORDER.
RC PLASMID=F;
RX PubMed=7499340; DOI=10.1074/jbc.270.47.28374;
RA Howard M.T., Nelson W.C., Matson S.W.;
RT "Stepwise assembly of a relaxosome at the F plasmid origin of transfer.";
RL J. Biol. Chem. 270:28381-28386(1995).
RN [12]
RP FUNCTION IN SS-DNA-BINDING, CHARACTERIZATION OF DNA SEQUENCE SPECIFICITY,
RP AND MUTAGENESIS OF TYR-16.
RC PLASMID=F;
RX PubMed=11560509; DOI=10.1021/bi010877q;
RA Stern J.C., Schildbach J.F.;
RT "DNA recognition by F factor TraI36: highly sequence-specific binding of
RT single-stranded DNA.";
RL Biochemistry 40:11586-11595(2001).
RN [13]
RP DOMAINS, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-998.
RC PLASMID=F;
RX PubMed=11054423; DOI=10.1074/jbc.m008728200;
RA Matson S.W., Sampson J.K., Byrd D.R.;
RT "F plasmid conjugative DNA transfer: the TraI helicase activity is
RT essential for DNA strand transfer.";
RL J. Biol. Chem. 276:2372-2379(2001).
RN [14]
RP CHARACTERIZATION OF THE C-TERMINUS, DOMAINS, AND MUTAGENESIS OF LYS-998.
RC PLASMID=F;
RX PubMed=15629940; DOI=10.1128/jb.187.2.697-706.2005;
RA Matson S.W., Ragonese H.;
RT "The F-plasmid TraI protein contains three functional domains required for
RT conjugative DNA strand transfer.";
RL J. Bacteriol. 187:697-706(2005).
RN [15]
RP CHARACTERIZATION OF HELICASE ACTIVITY, AND SUBUNIT.
RC PLASMID=F;
RX PubMed=16984922; DOI=10.1074/jbc.m604412200;
RA Sikora B., Eoff R.L., Matson S.W., Raney K.D.;
RT "DNA unwinding by Escherichia coli DNA helicase I (TraI) provides evidence
RT for a processive monomeric molecular motor.";
RL J. Biol. Chem. 281:36110-36116(2006).
RN [16]
RP INTERACTION WITH TRAM; TRAY AND IHF, AND SUBUNIT.
RC PLASMID=F;
RX PubMed=17238924; DOI=10.1111/j.1365-2958.2006.05576.x;
RA Ragonese H., Haisch D., Villareal E., Choi J.H., Matson S.W.;
RT "The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage
RT at oriT through an interaction with TraI.";
RL Mol. Microbiol. 63:1173-1184(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-330 IN COMPLEX WITH MAGNESIUM.
RC PLASMID=F;
RX PubMed=14604527; DOI=10.1016/j.str.2003.10.001;
RA Datta S., Larkin C., Schildbach J.F.;
RT "Structural insights into single-stranded DNA binding and cleavage by F
RT factor TraI.";
RL Structure 11:1369-1379(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 1-330 BOUND TO SS-DNA AND
RP MAGNESIUM, CHARACTERIZATION OF RELAXASE CATALYTIC RESIDUE, AND MUTAGENESIS
RP OF MET-1; SER-3; TYR-16; LYS-88; ARG-237 AND ILE-241.
RC PLASMID=F;
RX PubMed=16216584; DOI=10.1016/j.str.2005.06.013;
RA Larkin C., Datta S., Harley M.J., Anderson B.J., Ebie A., Hargreaves V.,
RA Schildbach J.F.;
RT "Inter- and intramolecular determinants of the specificity of single-
RT stranded DNA binding and cleavage by the F factor relaxase.";
RL Structure 13:1533-1544(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-300 IN COMPLEX WITH SS-DNA WITH
RP AND WITHOUT INHIBITOR, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-159.
RC PLASMID=F;
RX PubMed=17630285; DOI=10.1073/pnas.0702760104;
RA Lujan S.A., Guogas L.M., Ragonese H., Matson S.W., Redinbo M.R.;
RT "Disrupting antibiotic resistance propagation by inhibiting the conjugative
RT DNA relaxase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12282-12287(2007).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1476-1628, DNA-BINDING BY
RP C-TERMINUS, MUTAGENESIS OF 1517-ALA--GLY-1525; 1574-LEU-GLN-1575; VAL-1603
RP AND 1721-GLU--ASP-1756, AND DISRUPTION PHENOTYPE.
RC PLASMID=F;
RX PubMed=19136009; DOI=10.1016/j.jmb.2008.12.057;
RA Guogas L.M., Kennedy S.A., Lee J.H., Redinbo M.R.;
RT "A novel fold in the TraI relaxase-helicase c-terminal domain is essential
RT for conjugative DNA transfer.";
RL J. Mol. Biol. 386:554-568(2009).
CC -!- FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer
CC of ssDNA plasmid from a donor to a recipient cell. It is the central
CC mechanism by which antibiotic resistance and virulence factors are
CC propagated in bacterial populations. Part of the relaxosome, which
CC facilitates a site- and strand-specific cut in the origin of transfer
CC by TraI, at the nic site. Relaxosome formation requires binding of IHF
CC and TraY to the oriT region, which then facilitates binding of TraI
CC relaxase. TraI forms a covalent 5'-phosphotyrosine intermediate linkage
CC to the ssDNA. The transesterified T-strand moves from the donor cell to
CC the recipient cell in a 5'to 3' direction, with the DNA helicase
CC activity of TraI unwinding the DNA. DNA transfer occurs via the
CC conjugative pore (transferosome) an intercellular junction mediated by
CC a type IV secretion system, with TraD providing the means to link the
CC relaxosome to the conjugative pore. The relaxase completes DNA transfer
CC by reversing the covalent phosphotyrosine linkage and releasing the T-
CC strand.
CC -!- FUNCTION: TraI has also been identified as DNA helicase I. DNA.
CC helicase I is a potent, highly processive DNA-dependent ATPase, able to
CC unwind about 1.1 kb dsDNA per second in a 5' to 3' manner.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Nicking activity (relaxase) is inhibited by
CC bisphosphonates such as the non-competitive inhibitor imidobisphosphate
CC (PNP), etidronic acid (ETIDRO) and clodronic acid (CLODRO). The latter
CC 2 are competitive inhibitors, and are already used clinically to treat
CC bone loss (marketed as Didronel and Bonefos). All 3 compounds also
CC inhibit conjugation and kill F plasmid-containing cells. They are
CC specific to dual tyrosine relaxases such as those found in F and
CC related R conjugative plasmids. {ECO:0000269|PubMed:17630285}.
CC -!- SUBUNIT: Monomer. Part of the relaxosome, a complex composed of
CC plasmid-encodes TraI, TraM, TraY and host-encoded IHF bound to the F
CC plasmid origin of transfer (oriT). Directly contacts coupling protein
CC TraD. Seems to directly contact TraM via its C-terminus.
CC {ECO:0000269|PubMed:12637015, ECO:0000269|PubMed:14604527,
CC ECO:0000269|PubMed:16984922, ECO:0000269|PubMed:17238924,
CC ECO:0000269|PubMed:17630285}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=traI;
CC IsoId=P14565-1; Sequence=Displayed;
CC Name=traI*;
CC IsoId=P14565-2; Sequence=VSP_018971;
CC -!- DOMAIN: Has 4 domains; the relaxase domain (residues 1-330), an unknown
CC domain (residues 330-990), the helicase domain (residues 990-1450) and
CC the C-terminal domain (1450-1756) which is required for conjugative DNA
CC transfer, possibly via interaction with TraM.
CC {ECO:0000269|PubMed:11054423, ECO:0000269|PubMed:15629940}.
CC -!- DISRUPTION PHENOTYPE: Loss of conjugative DNA transfer.
CC {ECO:0000269|PubMed:11054423, ECO:0000269|PubMed:19136009}.
CC -!- SIMILARITY: To TraI of plasmid IncFII R100. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83930.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M54796; AAA98085.1; -; Genomic_DNA.
DR EMBL; M54796; AAA98086.1; -; Genomic_DNA.
DR EMBL; U01159; AAC44186.1; -; Genomic_DNA.
DR EMBL; AP001918; BAA97974.1; -; Genomic_DNA.
DR EMBL; M29254; AAA83930.1; ALT_INIT; Genomic_DNA.
DR EMBL; X57430; CAA40677.1; -; Genomic_DNA.
DR EMBL; U01159; AAC44187.1; -; Genomic_DNA.
DR RefSeq; NP_061483.1; NC_002483.1. [P14565-1]
DR RefSeq; WP_000987005.1; NZ_CP014273.1.
DR PDB; 1P4D; X-ray; 2.60 A; A/B/C=1-330.
DR PDB; 2A0I; X-ray; 2.72 A; A=1-330.
DR PDB; 2L8B; NMR; -; A=381-569.
DR PDB; 2Q7T; X-ray; 2.42 A; A/B=1-300.
DR PDB; 2Q7U; X-ray; 3.00 A; A/B=1-300.
DR PDB; 3FLD; X-ray; 2.40 A; A/B=1476-1628.
DR PDB; 5N8O; EM; 3.90 A; A=1-1756.
DR PDBsum; 1P4D; -.
DR PDBsum; 2A0I; -.
DR PDBsum; 2L8B; -.
DR PDBsum; 2Q7T; -.
DR PDBsum; 2Q7U; -.
DR PDBsum; 3FLD; -.
DR PDBsum; 5N8O; -.
DR AlphaFoldDB; P14565; -.
DR SMR; P14565; -.
DR PRIDE; P14565; -.
DR PATRIC; fig|83333.107.peg.607; -.
DR EvolutionaryTrace; P14565; -.
DR PRO; PR:P14565; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014059; Conjug_relaxase_N.
DR InterPro; IPR014129; Conjug_relaxase_TraI.
DR InterPro; IPR009767; DNA_helicase_TraI.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040668; TraI_2B.
DR InterPro; IPR040987; TraI_N.
DR InterPro; IPR014862; TrwC.
DR Pfam; PF18272; ssDNA_TraI_N; 1.
DR Pfam; PF07057; TraI; 1.
DR Pfam; PF18340; TraI_2B; 1.
DR Pfam; PF08751; TrwC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR02686; relax_trwC; 1.
DR TIGRFAMs; TIGR02760; TraI_TIGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; ATP-binding; Coiled coil;
KW Conjugation; Cytoplasm; Direct protein sequencing; DNA-binding; Helicase;
KW Hydrolase; Isomerase; Magnesium; Metal-binding; Mobility protein;
KW Multifunctional enzyme; Nucleotide-binding; Plasmid.
FT CHAIN 1..1756
FT /note="Multifunctional conjugation protein TraI"
FT /id="PRO_0000024504"
FT REGION 1..330
FT /note="DNA relaxase"
FT REGION 950..1500
FT /note="DNA helicase I"
FT REGION 1534..1756
FT /note="Required for DNA transfer, may interact with TraM"
FT COILED 1717..1753
FT /evidence="ECO:0000255"
FT ACT_SITE 16
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate; for
FT relaxase activity"
FT /evidence="ECO:0000305"
FT ACT_SITE 17
FT /note="Relaxase"
FT /evidence="ECO:0000255"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14604527"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14604527"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14604527"
FT BINDING 992..999
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..954
FT /note="Missing (in isoform traI*)"
FT /evidence="ECO:0000305"
FT /id="VSP_018971"
FT MUTAGEN 1
FT /note="Missing: Loss of ssDNA binding."
FT /evidence="ECO:0000269|PubMed:16216584"
FT MUTAGEN 3
FT /note="S->A: 1000-fold reduced affinity for ssDNA."
FT /evidence="ECO:0000269|PubMed:16216584"
FT MUTAGEN 16
FT /note="Y->F: Loss of DNA nicking ability; still binds
FT ssDNA."
FT /evidence="ECO:0000269|PubMed:11560509,
FT ECO:0000269|PubMed:12637015, ECO:0000269|PubMed:16216584"
FT MUTAGEN 17
FT /note="Y->F: Loss of DNA nicking ability; still binds
FT ssDNA."
FT /evidence="ECO:0000269|PubMed:12637015"
FT MUTAGEN 23
FT /note="Y->F: Reduced DNA nicking ability."
FT /evidence="ECO:0000269|PubMed:12637015"
FT MUTAGEN 24
FT /note="Y->F: Reduced DNA nicking ability."
FT /evidence="ECO:0000269|PubMed:12637015"
FT MUTAGEN 88
FT /note="K->A: 10000-fold reduced affinity for ssDNA."
FT /evidence="ECO:0000269|PubMed:16216584"
FT MUTAGEN 159
FT /note="H->E: Loss of oriT cleavage."
FT /evidence="ECO:0000269|PubMed:17630285"
FT MUTAGEN 237
FT /note="R->A: 300-fold reduced affinity for ssDNA."
FT /evidence="ECO:0000269|PubMed:16216584"
FT MUTAGEN 241
FT /note="I->A: 1500-fold reduced affinity for ssDNA."
FT /evidence="ECO:0000269|PubMed:16216584"
FT MUTAGEN 998
FT /note="K->M: No helicase activity, nicks DNA, loss of DNA
FT transfer activity."
FT /evidence="ECO:0000269|PubMed:11054423,
FT ECO:0000269|PubMed:15629940"
FT MUTAGEN 1517..1525
FT /note="Missing: 10,000-fold reduction in conjugative DNA
FT transfer."
FT /evidence="ECO:0000269|PubMed:19136009"
FT MUTAGEN 1518..1525
FT /note="PGRKYPQP->GGRKYGQG: 100,000-fold reduction in
FT conjugative DNA transfer."
FT MUTAGEN 1574..1575
FT /note="LQ->AA: 200-fold reduction in conjugative DNA
FT transfer; when associated with A-1603."
FT /evidence="ECO:0000269|PubMed:19136009"
FT MUTAGEN 1603
FT /note="V->A: 200-fold reduction in conjugative DNA
FT transfer; when associated with 1574-A-A-1575."
FT /evidence="ECO:0000269|PubMed:19136009"
FT MUTAGEN 1721..1756
FT /note="Missing: More than 100-fold reduction in conjugative
FT DNA transfer."
FT /evidence="ECO:0000269|PubMed:19136009"
FT CONFLICT 69..74
FT /note="MQDGSN -> CRMAVT (in Ref. 4; AAA83930)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2Q7T"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2A0I"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2A0I"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2Q7T"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2Q7T"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2A0I"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:2A0I"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:2Q7T"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:2Q7T"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 417..429
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 443..458
FT /evidence="ECO:0007829|PDB:2L8B"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:2L8B"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:2L8B"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:2L8B"
FT TURN 489..495
FT /evidence="ECO:0007829|PDB:2L8B"
FT STRAND 504..512
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 513..527
FT /evidence="ECO:0007829|PDB:2L8B"
FT STRAND 532..538
FT /evidence="ECO:0007829|PDB:2L8B"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 544..552
FT /evidence="ECO:0007829|PDB:2L8B"
FT HELIX 1477..1487
FT /evidence="ECO:0007829|PDB:3FLD"
FT HELIX 1491..1493
FT /evidence="ECO:0007829|PDB:3FLD"
FT HELIX 1495..1504
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1514..1516
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1526..1532
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1538..1545
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1547..1549
FT /evidence="ECO:0007829|PDB:3FLD"
FT TURN 1550..1552
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1553..1555
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1562..1565
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1571..1576
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1578..1587
FT /evidence="ECO:0007829|PDB:3FLD"
FT HELIX 1588..1597
FT /evidence="ECO:0007829|PDB:3FLD"
FT STRAND 1601..1608
FT /evidence="ECO:0007829|PDB:3FLD"
FT HELIX 1616..1618
FT /evidence="ECO:0007829|PDB:3FLD"
SQ SEQUENCE 1756 AA; 192016 MW; AA07D61DB2BFD9FA CRC64;
MMSIAQVRSA GSAGNYYTDK DNYYVLGSMG ERWAGRGAEQ LGLQGSVDKD VFTRLLEGRL
PDGADLSRMQ DGSNRHRPGY DLTFSAPKSV SMMAMLGGDK RLIDAHNQAV DFAVRQVEAL
ASTRVMTDGQ SETVLTGNLV MALFNHDTSR DQEPQLHTHA VVANVTQHNG EWKTLSSDKV
GKTGFIENVY ANQIAFGRLY REKLKEQVEA LGYETEVVGK HGMWEMPGVP VEAFSGRSQT
IREAVGEDAS LKSRDVAALD TRKSKQHVDP EIKMAEWMQT LKETGFDIRA YRDAADQRAD
LRTLTPGPAS QDGPDVQQAV TQAIAGLSER KVQFTYTDVL ARTVGILPPE NGVIERARAG
IDEAISREQL IPLDREKGLF TSGIHVLDEL SVRALSRDIM KQNRVTVHPE KSVPRTAGYS
DAVSVLAQDR PSLAIVSGQG GAAGQRERVA ELVMMAREQG REVQIIAADR RSQMNMKQDE
RLSGELITGR RQLLEGMAFT PGSTVIVDQG EKLSLKETLT LLDGAARHNV QVLITDSGQR
TGTGSALMAM KDAGVNTYRW QGGEQRPATI ISEPDRNVRY ARLAGDFAAS VKAGEESVAQ
VSGVREQAIL TQAIRSELKT QGVLGLPEVT MTALSPVWLD SRSRYLRDMY RPGMVMEQWN
PETRSHDRYV IDRVTAQSHS LTLRDAQGET QVVRISSLDS SWSLFRPEKM PVADGERLRV
TGKIPGLRVS GGDRLQVASV SEDAMTVVVP GRAEPATLPV SDSPFTALKL ENGWVETPGH
SVSDSATVFA SVTQMAMDNA TLNGLARSGR DVRLYSSLDE TRTAEKLARH PSFTVVSEQI
KTRAGETSLE TAISHQKSAL HTPAQQAIHL ALPVVESKKL AFSMVDLLTE AKSFAAEGTG
FTELGGEINA QIKRGDLLYV DVAKGYGTGL LVSRASYEAE KSILRHILEG KEAVMPLMER
VPGELMEKLT SGQRAATRMI LETSDRFTVV QGYAGVGKTT QFRAVMSAVN MLPESERPRV
VGLGPTHRAV GEMRSAGVDA QTLASFLHDT QLQQRSGETP DFSNTLFLLD ESSMVGNTDM
ARAYALIAAG GGRAVASGDT DQLQAIAPGQ PFRLQQTRSA ADVAIMKEIV RQTPELREAV
YSLINRDVER ALSGLESVKP SQVPRQEGAW APEHSVTEFS HSQEAKLAEA QQKAMLKGEA
FPDVPMTLYE AIVRDYTGRT PEAREQTLIV THLNEDRRVL NSMIHDVREK AGELGKEQVM
VPVLNTANIR DGELRRLSTW ETHRDALVLV DNVYHRIAGI SKDDGLITLQ DAEGNTRLIS
PREAVAEGVT LYTPDTIRVG TGDRMRFTKS DRERGYVANS VWTVTAVSGD SVTLSDGQQT
REIRPGQEQA EQHIDLAYAI TAHGAQGASE TFAIALEGTE GNRKLMAGFE SAYVALSRMK
QHVQVYTDNR QGWTDAINNA VQKGTAHDVF EPKPDREVMN AERLFSTARE LRDVAAGRAV
LRQAGLAGGD SPARFIAPGR KYPQPYVALP AFDRNGKSAG IWLNPLTTDD GNGLRGFSGE
GRVKGSGDAQ FVALQGSRNG ESLLADNMQD GVRIARDNPD SGVVVRIAGE GRPWNPGAIT
GGRVWGDIPD NSVQPGAGNG EPVTAEVLAQ RQAEEAIRRE TERRADEIVR KMAENKPDLP
DGKTEQAVRE IAGQERDRAA ITEREAALPE GVLREPQRVR EAVREIAREN LLQERLQQME
RDMVRDLQKE KTLGGD
