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Multifunctional conjugation protein TraI [Includes: DNA relaxase TraI (EC 5.99.1.2) (DNA nickase TraI) (Transesterase TraI); DNA helicase I (EC 3.6.4.12)]

 TRAI1_ECOLI             Reviewed;        1756 AA.
P14565; Q51811;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
05-DEC-2018, entry version 133.
RecName: Full=Multifunctional conjugation protein TraI;
Includes:
RecName: Full=DNA relaxase TraI;
EC=5.99.1.2;
AltName: Full=DNA nickase TraI;
AltName: Full=Transesterase TraI;
Includes:
RecName: Full=DNA helicase I;
EC=3.6.4.12;
Name=traI; OrderedLocusNames=ECOK12F104;
Escherichia coli (strain K12).
Plasmid F.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PLASMID=F;
PubMed=2163400; DOI=10.1128/jb.172.7.4127-4131.1990;
Bradshaw H.D. Jr., Traxler B.A., Minkley E.G. Jr., Nester E.W.,
Gordon M.P.;
"Nucleotide sequence of the traI (helicase I) gene from the sex factor
F.";
J. Bacteriol. 172:4127-4131(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=F;
PubMed=7915817;
Frost L.S., Ippen-Ihler K., Skurray R.A.;
"Analysis of the sequence and gene products of the transfer region of
the F sex factor.";
Microbiol. Rev. 58:162-210(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / CR63; PLASMID=F;
Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
"Complete nucleotide sequence of the F plasmid: its implications for
organization and diversification of plasmid genomes.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
STRAIN=K12; PLASMID=F;
PubMed=2680768; DOI=10.1016/0378-1119(89)90179-0;
Jalajakumari M.B., Manning P.A.;
"Nucleotide sequence of the traD region in the Escherichia coli F sex
factor.";
Gene 81:195-202(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
PLASMID=F;
PubMed=2164585; DOI=10.1016/0022-2836(90)90145-C;
Yoshioka Y., Fujita Y., Ohtsubo E.;
"Nucleotide sequence of the promoter-distal region of the tra operon
of plasmid R100, including traI (DNA helicase I) and traD genes.";
J. Mol. Biol. 214:39-53(1990).
[6]
PROTEIN SEQUENCE OF 1-5, FUNCTION IN SS-DNA DIGESTION, SUBUNIT,
CHARACTERIZATION OF RELAXASE CATALYTIC RESIDUES, AND MUTAGENESIS OF
TYR-16; TYR-17; TYR-23 AND TYR-24.
PLASMID=F;
PubMed=12637015; DOI=10.1016/S1570-9639(02)00553-8;
Street L.M., Harley M.J., Stern J.C., Larkin C., Williams S.L.,
Miller D.L., Dohm J.A., Rodgers M.E., Schildbach J.F.;
"Subdomain organization and catalytic residues of the F factor TraI
relaxase domain.";
Biochim. Biophys. Acta 1646:86-99(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-1756.
PLASMID=F;
PubMed=8736534; DOI=10.1046/j.1365-2958.1996.5361059.x;
Penfold S.S., Simon J., Frost L.S.;
"Regulation of the expression of the traM gene of the F sex factor of
Escherichia coli.";
Mol. Microbiol. 20:549-558(1996).
[8]
FUNCTION AS DNA HELICASE I.
PLASMID=F;
PubMed=6308637; DOI=10.1073/pnas.80.15.4659;
Abdel-Monem M., Taucher-Scholz G., Klinkert M.Q.;
"Identification of Escherichia coli DNA helicase I as the traI gene
product of the F sex factor.";
Proc. Natl. Acad. Sci. U.S.A. 80:4659-4663(1983).
[9]
FUNCTION IN COVALENT BINDING TO SS-DNA.
PLASMID=F;
PubMed=8386720; DOI=10.1128/jb.175.9.2599-2606.1993;
Matson S.W., Nelson W.C., Morton B.S.;
"Characterization of the reaction product of the oriT nicking reaction
catalyzed by Escherichia coli DNA helicase I.";
J. Bacteriol. 175:2599-2606(1993).
[10]
FUNCTION IN F PLASMID NICKING.
PLASMID=F;
PubMed=7499339; DOI=10.1074/jbc.270.47.28381;
Nelson W.C., Howard M.T., Sherman J.A., Matson S.W.;
"The traY gene product and integration host factor stimulate
Escherichia coli DNA helicase I-catalyzed nicking at the F plasmid
oriT.";
J. Biol. Chem. 270:28374-28380(1995).
[11]
CHARACTERIZATION OF RELAXOSOME ASSEMBLY ORDER.
PLASMID=F;
PubMed=7499340; DOI=10.1074/jbc.270.47.28374;
Howard M.T., Nelson W.C., Matson S.W.;
"Stepwise assembly of a relaxosome at the F plasmid origin of
transfer.";
J. Biol. Chem. 270:28381-28386(1995).
[12]
FUNCTION IN SS-DNA-BINDING, CHARACTERIZATION OF DNA SEQUENCE
SPECIFICITY, AND MUTAGENESIS OF TYR-16.
PLASMID=F;
PubMed=11560509; DOI=10.1021/bi010877q;
Stern J.C., Schildbach J.F.;
"DNA recognition by F factor TraI36: highly sequence-specific binding
of single-stranded DNA.";
Biochemistry 40:11586-11595(2001).
[13]
DOMAINS, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-998.
PLASMID=F;
PubMed=11054423; DOI=10.1074/jbc.M008728200;
Matson S.W., Sampson J.K., Byrd D.R.;
"F plasmid conjugative DNA transfer: the TraI helicase activity is
essential for DNA strand transfer.";
J. Biol. Chem. 276:2372-2379(2001).
[14]
CHARACTERIZATION OF THE C-TERMINUS, DOMAINS, AND MUTAGENESIS OF
LYS-998.
PLASMID=F;
PubMed=15629940; DOI=10.1128/JB.187.2.697-706.2005;
Matson S.W., Ragonese H.;
"The F-plasmid TraI protein contains three functional domains required
for conjugative DNA strand transfer.";
J. Bacteriol. 187:697-706(2005).
[15]
CHARACTERIZATION OF HELICASE ACTIVITY, AND SUBUNIT.
PLASMID=F;
PubMed=16984922; DOI=10.1074/jbc.M604412200;
Sikora B., Eoff R.L., Matson S.W., Raney K.D.;
"DNA unwinding by Escherichia coli DNA helicase I (TraI) provides
evidence for a processive monomeric molecular motor.";
J. Biol. Chem. 281:36110-36116(2006).
[16]
INTERACTION WITH TRAM; TRAY AND IHF, AND SUBUNIT.
PLASMID=F;
PubMed=17238924; DOI=10.1111/j.1365-2958.2006.05576.x;
Ragonese H., Haisch D., Villareal E., Choi J.H., Matson S.W.;
"The F plasmid-encoded TraM protein stimulates relaxosome-mediated
cleavage at oriT through an interaction with TraI.";
Mol. Microbiol. 63:1173-1184(2007).
[17]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-330 IN COMPLEX WITH
MAGNESIUM.
PLASMID=F;
PubMed=14604527; DOI=10.1016/j.str.2003.10.001;
Datta S., Larkin C., Schildbach J.F.;
"Structural insights into single-stranded DNA binding and cleavage by
F factor TraI.";
Structure 11:1369-1379(2003).
[18]
X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 1-330 BOUND TO SS-DNA AND
MAGNESIUM, CHARACTERIZATION OF RELAXASE CATALYTIC RESIDUE, AND
MUTAGENESIS OF MET-1; SER-3; TYR-16; LYS-88; ARG-237 AND ILE-241.
PLASMID=F;
PubMed=16216584; DOI=10.1016/j.str.2005.06.013;
Larkin C., Datta S., Harley M.J., Anderson B.J., Ebie A.,
Hargreaves V., Schildbach J.F.;
"Inter- and intramolecular determinants of the specificity of single-
stranded DNA binding and cleavage by the F factor relaxase.";
Structure 13:1533-1544(2005).
[19]
X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-300 IN COMPLEX WITH SS-DNA
WITH AND WITHOUT INHIBITOR, ACTIVITY REGULATION, AND MUTAGENESIS OF
HIS-159.
PLASMID=F;
PubMed=17630285; DOI=10.1073/pnas.0702760104;
Lujan S.A., Guogas L.M., Ragonese H., Matson S.W., Redinbo M.R.;
"Disrupting antibiotic resistance propagation by inhibiting the
conjugative DNA relaxase.";
Proc. Natl. Acad. Sci. U.S.A. 104:12282-12287(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1476-1628, DNA-BINDING BY
C-TERMINUS, MUTAGENESIS OF 1517-ALA--GLY-1525; 1574-LEU-GLN-1575;
VAL-1603 AND 1721-GLU--ASP-1756, AND DISRUPTION PHENOTYPE.
PLASMID=F;
PubMed=19136009; DOI=10.1016/j.jmb.2008.12.057;
Guogas L.M., Kennedy S.A., Lee J.H., Redinbo M.R.;
"A novel fold in the TraI relaxase-helicase c-terminal domain is
essential for conjugative DNA transfer.";
J. Mol. Biol. 386:554-568(2009).
-!- FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional
transfer of ssDNA plasmid from a donor to a recipient cell. It is
the central mechanism by which antibiotic resistance and virulence
factors are propagated in bacterial populations. Part of the
relaxosome, which facilitates a site- and strand-specific cut in
the origin of transfer by TraI, at the nic site. Relaxosome
formation requires binding of IHF and TraY to the oriT region,
which then facilitates binding of TraI relaxase. TraI forms a
covalent 5'-phosphotyrosine intermediate linkage to the ssDNA. The
transesterified T-strand moves from the donor cell to the
recipient cell in a 5'to 3' direction, with the DNA helicase
activity of TraI unwinding the DNA. DNA transfer occurs via the
conjugative pore (transferosome) an intercellular junction
mediated by a type IV secretion system, with TraD providing the
means to link the relaxosome to the conjugative pore. The relaxase
completes DNA transfer by reversing the covalent phosphotyrosine
linkage and releasing the T-strand.
-!- FUNCTION: TraI has also been identified as DNA helicase I. DNA.
helicase I is a potent, highly processive DNA-dependent ATPase,
able to unwind about 1.1 kb dsDNA per second in a 5' to 3' manner.
-!- CATALYTIC ACTIVITY:
Reaction=ATP-independent breakage of single-stranded DNA, followed
by passage and rejoining.; EC=5.99.1.2;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Nicking activity (relaxase) is inhibited by
bisphosphonates such as the non-competitive inhibitor
imidobisphosphate (PNP), etidronic acid (ETIDRO) and clodronic
acid (CLODRO). The latter 2 are competitive inhibitors, and are
already used clinically to treat bone loss (marketed as Didronel
and Bonefos). All 3 compounds also inhibit conjugation and kill F
plasmid-containing cells. They are specific to dual tyrosine
relaxases such as those found in F and related R conjugative
plasmids. {ECO:0000269|PubMed:17630285}.
-!- SUBUNIT: Monomer. Part of the relaxosome, a complex composed of
plasmid-encodes TraI, TraM, TraY and host-encoded IHF bound to the
F plasmid origin of transfer (oriT). Directly contacts coupling
protein TraD. Seems to directly contact TraM via its C-terminus.
{ECO:0000269|PubMed:12637015, ECO:0000269|PubMed:14604527,
ECO:0000269|PubMed:16984922, ECO:0000269|PubMed:17238924,
ECO:0000269|PubMed:17630285}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=traI;
IsoId=P14565-1; Sequence=Displayed;
Name=traI*;
IsoId=P14565-2; Sequence=VSP_018971;
-!- DOMAIN: Has 4 domains; the relaxase domain (residues 1-330), an
unknown domain (residues 330-990), the helicase domain (residues
990-1450) and the C-terminal domain (1450-1756) which is required
for conjugative DNA transfer, possibly via interaction with TraM.
{ECO:0000269|PubMed:11054423, ECO:0000269|PubMed:15629940}.
-!- DISRUPTION PHENOTYPE: Loss of conjugative DNA transfer.
{ECO:0000269|PubMed:11054423, ECO:0000269|PubMed:19136009}.
-!- SIMILARITY: To TraI of plasmid IncFII R100. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA83930.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M54796; AAA98085.1; -; Genomic_DNA.
EMBL; M54796; AAA98086.1; -; Genomic_DNA.
EMBL; U01159; AAC44186.1; -; Genomic_DNA.
EMBL; AP001918; BAA97974.1; -; Genomic_DNA.
EMBL; M29254; AAA83930.1; ALT_INIT; Genomic_DNA.
EMBL; X57430; CAA40677.1; -; Genomic_DNA.
EMBL; U01159; AAC44187.1; -; Genomic_DNA.
RefSeq; NP_061483.1; NC_002483.1. [P14565-1]
RefSeq; WP_000987005.1; NZ_CP014273.1.
PDB; 1P4D; X-ray; 2.60 A; A/B/C=1-330.
PDB; 2A0I; X-ray; 2.72 A; A=1-330.
PDB; 2L8B; NMR; -; A=381-569.
PDB; 2Q7T; X-ray; 2.42 A; A/B=1-300.
PDB; 2Q7U; X-ray; 3.00 A; A/B=1-300.
PDB; 3FLD; X-ray; 2.40 A; A/B=1476-1628.
PDB; 5N8O; EM; 3.90 A; A=1-1756.
PDBsum; 1P4D; -.
PDBsum; 2A0I; -.
PDBsum; 2L8B; -.
PDBsum; 2Q7T; -.
PDBsum; 2Q7U; -.
PDBsum; 3FLD; -.
PDBsum; 5N8O; -.
ProteinModelPortal; P14565; -.
SMR; P14565; -.
PRIDE; P14565; -.
GeneID; 1263574; -.
PATRIC; fig|83333.107.peg.607; -.
EvolutionaryTrace; P14565; -.
PRO; PR:P14565; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000746; P:conjugation; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
InterPro; IPR014059; Conjug_relaxase_N.
InterPro; IPR014129; Conjug_relaxase_TraI.
InterPro; IPR009767; DNA_helicase_TraI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014862; TrwC.
Pfam; PF07057; TraI; 1.
Pfam; PF08751; TrwC; 1.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR02686; relax_trwC; 1.
TIGRFAMs; TIGR02760; TraI_TIGR; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; ATP-binding; Coiled coil;
Conjugation; Cytoplasm; Direct protein sequencing; DNA-binding;
Helicase; Hydrolase; Isomerase; Magnesium; Metal-binding;
Mobility protein; Multifunctional enzyme; Nucleotide-binding; Plasmid.
CHAIN 1 1756 Multifunctional conjugation protein TraI.
/FTId=PRO_0000024504.
NP_BIND 992 999 ATP. {ECO:0000255}.
REGION 1 330 DNA relaxase.
REGION 950 1500 DNA helicase I.
REGION 1534 1756 Required for DNA transfer, may interact
with TraM.
COILED 1717 1753 {ECO:0000255}.
ACT_SITE 16 16 O-(5'-phospho-DNA)-tyrosine intermediate;
for relaxase activity. {ECO:0000305}.
ACT_SITE 17 17 Relaxase. {ECO:0000255}.
METAL 146 146 Magnesium; via pros nitrogen; catalytic.
{ECO:0000269|PubMed:14604527}.
METAL 157 157 Magnesium; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:14604527}.
METAL 159 159 Magnesium; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:14604527}.
VAR_SEQ 1 954 Missing (in isoform traI*).
{ECO:0000305}.
/FTId=VSP_018971.
MUTAGEN 1 1 Missing: Loss of ssDNA binding.
{ECO:0000269|PubMed:16216584}.
MUTAGEN 3 3 S->A: 1000-fold reduced affinity for
ssDNA. {ECO:0000269|PubMed:16216584}.
MUTAGEN 16 16 Y->F: Loss of DNA nicking ability; still
binds ssDNA.
{ECO:0000269|PubMed:11560509,
ECO:0000269|PubMed:12637015,
ECO:0000269|PubMed:16216584}.
MUTAGEN 17 17 Y->F: Loss of DNA nicking ability; still
binds ssDNA.
{ECO:0000269|PubMed:12637015}.
MUTAGEN 23 23 Y->F: Reduced DNA nicking ability.
{ECO:0000269|PubMed:12637015}.
MUTAGEN 24 24 Y->F: Reduced DNA nicking ability.
{ECO:0000269|PubMed:12637015}.
MUTAGEN 88 88 K->A: 10000-fold reduced affinity for
ssDNA. {ECO:0000269|PubMed:16216584}.
MUTAGEN 159 159 H->E: Loss of oriT cleavage.
{ECO:0000269|PubMed:17630285}.
MUTAGEN 237 237 R->A: 300-fold reduced affinity for
ssDNA. {ECO:0000269|PubMed:16216584}.
MUTAGEN 241 241 I->A: 1500-fold reduced affinity for
ssDNA. {ECO:0000269|PubMed:16216584}.
MUTAGEN 998 998 K->M: No helicase activity, nicks DNA,
loss of DNA transfer activity.
{ECO:0000269|PubMed:11054423,
ECO:0000269|PubMed:15629940}.
MUTAGEN 1517 1525 Missing: 10,000-fold reduction in
conjugative DNA transfer.
{ECO:0000269|PubMed:19136009}.
MUTAGEN 1518 1525 PGRKYPQP->GGRKYGQG: 100,000-fold
reduction in conjugative DNA transfer.
MUTAGEN 1574 1575 LQ->AA: 200-fold reduction in conjugative
DNA transfer; when associated with A-
1603. {ECO:0000269|PubMed:19136009}.
MUTAGEN 1603 1603 V->A: 200-fold reduction in conjugative
DNA transfer; when associated with 1574-
A-A-1575. {ECO:0000269|PubMed:19136009}.
MUTAGEN 1721 1756 Missing: More than 100-fold reduction in
conjugative DNA transfer.
{ECO:0000269|PubMed:19136009}.
CONFLICT 69 74 MQDGSN -> CRMAVT (in Ref. 4; AAA83930).
{ECO:0000305}.
STRAND 2 6 {ECO:0000244|PDB:2Q7T}.
HELIX 10 17 {ECO:0000244|PDB:2Q7T}.
HELIX 20 22 {ECO:0000244|PDB:2Q7T}.
TURN 24 26 {ECO:0000244|PDB:2Q7T}.
STRAND 32 35 {ECO:0000244|PDB:2Q7T}.
HELIX 36 41 {ECO:0000244|PDB:2Q7T}.
HELIX 49 56 {ECO:0000244|PDB:2Q7T}.
STRAND 61 63 {ECO:0000244|PDB:2A0I}.
TURN 71 73 {ECO:0000244|PDB:2A0I}.
STRAND 79 85 {ECO:0000244|PDB:2Q7T}.
HELIX 88 95 {ECO:0000244|PDB:2Q7T}.
HELIX 101 118 {ECO:0000244|PDB:2Q7T}.
STRAND 122 124 {ECO:0000244|PDB:2Q7T}.
STRAND 133 135 {ECO:0000244|PDB:2Q7T}.
STRAND 141 148 {ECO:0000244|PDB:2Q7T}.
STRAND 154 164 {ECO:0000244|PDB:2Q7T}.
STRAND 166 168 {ECO:0000244|PDB:2Q7T}.
STRAND 171 173 {ECO:0000244|PDB:2Q7T}.
TURN 179 181 {ECO:0000244|PDB:2Q7T}.
HELIX 185 190 {ECO:0000244|PDB:2Q7T}.
HELIX 193 210 {ECO:0000244|PDB:2Q7T}.
HELIX 220 222 {ECO:0000244|PDB:2Q7T}.
HELIX 231 234 {ECO:0000244|PDB:2Q7T}.
HELIX 236 244 {ECO:0000244|PDB:2A0I}.
HELIX 251 260 {ECO:0000244|PDB:2A0I}.
HELIX 270 282 {ECO:0000244|PDB:2Q7T}.
TURN 283 285 {ECO:0000244|PDB:2Q7T}.
HELIX 288 296 {ECO:0000244|PDB:2Q7T}.
HELIX 390 403 {ECO:0000244|PDB:2L8B}.
HELIX 409 411 {ECO:0000244|PDB:2L8B}.
HELIX 417 429 {ECO:0000244|PDB:2L8B}.
HELIX 443 458 {ECO:0000244|PDB:2L8B}.
STRAND 463 466 {ECO:0000244|PDB:2L8B}.
HELIX 471 476 {ECO:0000244|PDB:2L8B}.
TURN 479 481 {ECO:0000244|PDB:2L8B}.
STRAND 486 488 {ECO:0000244|PDB:2L8B}.
TURN 489 495 {ECO:0000244|PDB:2L8B}.
STRAND 504 512 {ECO:0000244|PDB:2L8B}.
HELIX 513 527 {ECO:0000244|PDB:2L8B}.
STRAND 532 538 {ECO:0000244|PDB:2L8B}.
TURN 539 541 {ECO:0000244|PDB:2L8B}.
HELIX 544 552 {ECO:0000244|PDB:2L8B}.
HELIX 1477 1487 {ECO:0000244|PDB:3FLD}.
HELIX 1491 1493 {ECO:0000244|PDB:3FLD}.
HELIX 1495 1504 {ECO:0000244|PDB:3FLD}.
STRAND 1514 1516 {ECO:0000244|PDB:3FLD}.
STRAND 1526 1532 {ECO:0000244|PDB:3FLD}.
STRAND 1538 1545 {ECO:0000244|PDB:3FLD}.
STRAND 1547 1549 {ECO:0000244|PDB:3FLD}.
TURN 1550 1552 {ECO:0000244|PDB:3FLD}.
STRAND 1553 1555 {ECO:0000244|PDB:3FLD}.
STRAND 1562 1565 {ECO:0000244|PDB:3FLD}.
STRAND 1571 1576 {ECO:0000244|PDB:3FLD}.
STRAND 1578 1587 {ECO:0000244|PDB:3FLD}.
HELIX 1588 1597 {ECO:0000244|PDB:3FLD}.
STRAND 1601 1608 {ECO:0000244|PDB:3FLD}.
HELIX 1616 1618 {ECO:0000244|PDB:3FLD}.
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


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