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Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase); DNA ligase D (LigD) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]); DNA repair polymerase (Pol) (Polymerase/primase)]

 LIGD_PSEAE              Reviewed;         840 AA.
Q9I1X7;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 110.
RecName: Full=Multifunctional non-homologous end joining protein LigD;
AltName: Full=NHEJ DNA polymerase;
Includes:
RecName: Full=3'-phosphoesterase;
Short=3'-ribonuclease/3'-phosphatase;
Includes:
RecName: Full=DNA ligase D;
Short=LigD;
EC=6.5.1.1;
AltName: Full=Polydeoxyribonucleotide synthase [ATP];
Includes:
RecName: Full=DNA repair polymerase;
Short=Pol;
AltName: Full=Polymerase/primase;
Name=ligD; OrderedLocusNames=PA2138;
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
[2]
FUNCTION AS A LIGASE, FUNCTION AS A DNA POLYMERASE, COFACTOR, SUBUNIT,
DOMAIN, AND MUTAGENESIS OF 669-ASP--ASP-671.
PubMed=15520014; DOI=10.1074/jbc.M410110200;
Zhu H., Shuman S.;
"A primer-dependent polymerase function of pseudomonas aeruginosa ATP-
dependent DNA ligase (LigD).";
J. Biol. Chem. 280:418-427(2005).
[3]
FUNCTION IN RESECTION, COFACTOR, DOMAIN, AND MUTAGENESIS OF ASP-50;
ARG-52; GLU-54; GLU-82 AND HIS-84.
PubMed=15897197; DOI=10.1074/jbc.M504002200;
Zhu H., Shuman S.;
"Novel 3'-ribonuclease and 3'-phosphatase activities of the bacterial
non-homologous end-joining protein, DNA ligase D.";
J. Biol. Chem. 280:25973-25981(2005).
[4]
FUNCTION, COFACTOR, DOMAIN, AND MUTAGENESIS OF ARG-14; ASP-15; GLU-21;
GLN-40; HIS-42; ARG-46; HIS-48; LYS-66; ARG-76; ASP-83 AND TYR-88.
PubMed=16046407; DOI=10.1074/jbc.M506838200;
Zhu H., Wang L.K., Shuman S.;
"Essential constituents of the 3'-phosphoesterase domain of bacterial
DNA ligase D, a nonhomologous end-joining enzyme.";
J. Biol. Chem. 280:33707-33715(2005).
[5]
FUNCTION IN GAP-FILLING, ENZYME REGULATION, AND MUTAGENESIS OF
HIS-553; 553-HIS--LYS-566; ARG-556; LYS-566 AND PHE-603.
PubMed=20018881; DOI=10.1074/jbc.M109.073874;
Zhu H., Shuman S.;
"Gap filling activities of Pseudomonas DNA ligase D (LigD) polymerase
and functional interactions of LigD with the DNA end-binding Ku
protein.";
J. Biol. Chem. 285:4815-4825(2010).
[6]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 533-840 OF APOENZYME AND IN
COMPLEX WITH ATP AND MANGANESE, COFACTOR, ATP-BINDING, AND MUTAGENESIS
OF PHE-604; ASP-669; ASP-671; HIS-710; ARG-752; ASP-759; ARG-776 AND
ARG-778.
PubMed=16446439; DOI=10.1073/pnas.0509083103;
Zhu H., Nandakumar J., Aniukwu J., Wang L.K., Glickman M.S.,
Lima C.D., Shuman S.;
"Atomic structure and nonhomologous end-joining function of the
polymerase component of bacterial DNA ligase D.";
Proc. Natl. Acad. Sci. U.S.A. 103:1711-1716(2006).
[7]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 17-187 IN COMPLEX WITH
MANGANESE, FUNCTION, AND REACTION MECHANISM.
PubMed=20616014; DOI=10.1073/pnas.1005830107;
Nair P.A., Smith P., Shuman S.;
"Structure of bacterial LigD 3'-phosphoesterase unveils a DNA repair
superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 107:12822-12827(2010).
[8]
STRUCTURE BY NMR OF 1-177, AND DNA-BINDING.
PubMed=22084199; DOI=10.1093/nar/gkr950;
Natarajan A., Dutta K., Temel D.B., Nair P.A., Shuman S., Ghose R.;
"Solution structure and DNA-binding properties of the phosphoesterase
domain of DNA ligase D.";
Nucleic Acids Res. 40:2076-2088(2012).
-!- FUNCTION: With Ku probably forms a non-homologous end joining
(NHEJ) repair enzyme, which repairs dsDNA breaks (DSB) with
reduced fidelity. Acts as a DNA ligase on singly nicked dsDNA,
fills dsDNA gaps (3- or 4- nucleotide gaps, prefers a 5'-phosphate
at the gap distal end, prefers dNTPs over rNTPs)
(PubMed:20018881), has DNA-directed DNA polymerase activity
(templated primer extension) and DNA-directed RNA polymerase
activity (PubMed:15897197), adds 1 or 2 non-templated rNTP (or
less well dNTP) to ssDNA or blunt-end dsDNA (primer extension).
Has 3' resection activity, removing 3'-rNMPs from DNA using its
3'-ribonuclease and 3'-phosphatase activities sequentially.
Resection requires a 2'-OH in the penultimate nucleoside position
(i.e. a ribo- not deoxyribonucleoside) (PubMed:15897197), although
the 3'-phosphatase activity does not, and its specific activity is
16-fold higher on a DNA substrate (PubMed:16046407). On
appropriate substrates will extend a DNA primer to the end of the
template strand and then incorporate a non-templated nucleotide.
{ECO:0000269|PubMed:15897197, ECO:0000269|PubMed:16046407,
ECO:0000269|PubMed:20018881}.
-!- FUNCTION: The preference of the polymerase domain for rNTPs over
dNTPs may be advantageous in quiescent cells where the dNTP pool
may be limiting.
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
AMP + diphosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000305|PubMed:15520014,
ECO:0000305|PubMed:15897197, ECO:0000305|PubMed:16046407,
ECO:0000305|PubMed:16446439};
Note=Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1
each for 3-phosphoesterase and ligase.
{ECO:0000305|PubMed:15520014, ECO:0000305|PubMed:15897197,
ECO:0000305|PubMed:16046407, ECO:0000305|PubMed:16446439};
-!- ENZYME REGULATION: rNTP addition and end joining activities are
stimulated by Ku homodimer. {ECO:0000269|PubMed:20018881}.
-!- SUBUNIT: Monomer. Interacts with Ku (By similarity).
{ECO:0000250}.
-!- DOMAIN: The N-terminal 3'-phosphoesterase domain (PE) has 3'-
ribonuclease and 3'-phosphatase activities.
{ECO:0000269|PubMed:15897197}.
-!- DOMAIN: The central ATP-dependent ligase domain (Lig) functions as
an independent domain. {ECO:0000269|PubMed:15520014}.
-!- DOMAIN: The C-terminal polymerase/primase domain (Pol)
(PubMed:15520014) adds up to 4 rNTPs in a DNA template-directed
fashion (PubMed:15897197). {ECO:0000269|PubMed:15520014,
ECO:0000269|PubMed:15897197}.
-!- MISCELLANEOUS: LigD has variable architecture; domain order can be
permutated, domains can be independently encoded, while some
bacteria lack the 3'-phosphoesterase domain entirely.
-!- SIMILARITY: In the N-terminal section; belongs to the LigD 3'-
phosphoesterase family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the ATP-dependent
DNA ligase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the LigD
polymerase family. {ECO:0000305}.
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EMBL; AE004091; AAG05526.1; -; Genomic_DNA.
PIR; C83378; C83378.
RefSeq; NP_250828.1; NC_002516.2.
RefSeq; WP_003113639.1; NC_002516.2.
PDB; 2FAO; X-ray; 1.50 A; A/B=533-840.
PDB; 2FAQ; X-ray; 1.90 A; A/B=533-840.
PDB; 2FAR; X-ray; 1.90 A; A/B=533-840.
PDB; 2LJ6; NMR; -; A=1-177.
PDB; 3N9B; X-ray; 1.92 A; A/B=17-187.
PDB; 3N9D; X-ray; 2.30 A; A=17-187.
PDBsum; 2FAO; -.
PDBsum; 2FAQ; -.
PDBsum; 2FAR; -.
PDBsum; 2LJ6; -.
PDBsum; 3N9B; -.
PDBsum; 3N9D; -.
ProteinModelPortal; Q9I1X7; -.
SMR; Q9I1X7; -.
STRING; 208964.PA2138; -.
PaxDb; Q9I1X7; -.
EnsemblBacteria; AAG05526; AAG05526; PA2138.
GeneID; 880451; -.
KEGG; pae:PA2138; -.
PATRIC; fig|208964.12.peg.2235; -.
PseudoCAP; PA2138; -.
eggNOG; ENOG4105DQE; Bacteria.
eggNOG; COG1793; LUCA.
eggNOG; COG3285; LUCA.
HOGENOM; HOG000222509; -.
InParanoid; Q9I1X7; -.
KO; K01971; -.
OMA; AMMVEDH; -.
PhylomeDB; Q9I1X7; -.
EvolutionaryTrace; Q9I1X7; -.
Proteomes; UP000002438; Chromosome.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:UniProtKB.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
GO; GO:0004532; F:exoribonuclease activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
GO; GO:0071897; P:DNA biosynthetic process; IDA:PseudoCAP.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:PseudoCAP.
CDD; cd04862; PaeLigD_Pol_like; 1.
InterPro; IPR012309; DNA_ligase_ATP-dep_C.
InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
InterPro; IPR014146; LigD_ligase_dom.
InterPro; IPR014144; LigD_PE_domain.
InterPro; IPR014145; LigD_pol_dom.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR014143; NHEJ_ligase_prk.
InterPro; IPR033651; PaeLigD_Pol-like.
Pfam; PF04679; DNA_ligase_A_C; 1.
Pfam; PF01068; DNA_ligase_A_M; 1.
Pfam; PF13298; LigD_N; 1.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR02777; LigD_PE_dom; 1.
TIGRFAMs; TIGR02778; ligD_pol; 1.
TIGRFAMs; TIGR02779; NHEJ_ligase_lig; 1.
TIGRFAMs; TIGR02776; NHEJ_ligase_prk; 1.
PROSITE; PS50160; DNA_LIGASE_A3; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; DNA damage;
DNA recombination; DNA repair; DNA-binding;
DNA-directed DNA polymerase; Exonuclease; Hydrolase; Ligase;
Manganese; Metal-binding; Multifunctional enzyme; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Transferase.
CHAIN 1 840 Multifunctional non-homologous end
joining protein LigD.
/FTId=PRO_0000425950.
NP_BIND 704 710 ATP. {ECO:0000269|PubMed:16446439}.
NP_BIND 776 778 ATP. {ECO:0000269|PubMed:16446439}.
REGION 7 162 3'-phosphoesterase domain (PE).
REGION 219 521 Ligase domain (Lig).
REGION 549 793 DNA repair polymerase domain (Pol).
ACT_SITE 238 238 N6-AMP-lysine intermediate.
{ECO:0000305}.
METAL 42 42 Manganese 1; via pros nitrogen;
catalytic; for 3'-phosphoesterase
activity. {ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
METAL 48 48 Manganese 1; via tele nitrogen;
catalytic; for 3'-phosphoesterase
activity. {ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
METAL 50 50 Manganese 1; catalytic; for 3'-
phosphoesterase activity.
{ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
METAL 240 240 Manganese 2. {ECO:0000250}.
METAL 376 376 Manganese 2. {ECO:0000250}.
METAL 669 669 Manganese 3.
{ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
METAL 669 669 Manganese 4.
{ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
METAL 671 671 Manganese 3.
{ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
METAL 759 759 Manganese 4.
{ECO:0000269|PubMed:16446439,
ECO:0000269|PubMed:20616014}.
BINDING 604 604 ATP. {ECO:0000269|PubMed:16446439}.
BINDING 651 651 ATP. {ECO:0000269|PubMed:16446439}.
BINDING 671 671 ATP. {ECO:0000269|PubMed:16446439}.
BINDING 768 768 ATP. {ECO:0000269|PubMed:16446439}.
SITE 84 84 Transition state stabilizer; for 3'-
phosphoesterase activity. {ECO:0000305}.
MUTAGEN 14 14 R->A: 77% ribonuclease activity, loss of
3'-phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 15 15 D->A: 3% 3'-phosphatase activity (in PE
domain). {ECO:0000269|PubMed:16046407}.
MUTAGEN 21 21 E->A: Loss of 3'-phosphatase activity (in
PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 40 40 Q->A: 41% ribonuclease activity, 7% 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 42 42 H->A: Loss of ribonuclease and 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 46 46 R->A: 16% ribonuclease activity, 20% 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 48 48 H->A: Loss of ribonuclease and 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 50 50 D->A: Loss of nuclease and 3'-phosphatase
activity (in PE domain).
{ECO:0000269|PubMed:15897197}.
MUTAGEN 52 52 R->A: Loss of nuclease and 3'-phosphatase
activity (in PE domain).
{ECO:0000269|PubMed:15897197}.
MUTAGEN 54 54 E->A: Nearly wild-type nuclease and 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:15897197}.
MUTAGEN 66 66 K->A: 3% ribonuclease activity, 28% 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 76 76 R->A: 1% ribonuclease activity, 16% 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 82 82 E->A: Selective loss of 3'-phosphatase
activity (in PE domain).
{ECO:0000269|PubMed:15897197}.
MUTAGEN 83 83 D->A: 57% ribonuclease activity, 50% 3'-
phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 84 84 H->A: Loss of nuclease and 3'-phosphatase
activity (in PE domain).
{ECO:0000269|PubMed:15897197}.
MUTAGEN 88 88 Y->A: 7% ribonuclease activity, loss of
3'-phosphatase activity (in PE domain).
{ECO:0000269|PubMed:16046407}.
MUTAGEN 553 566 HPQRLIDPSIQASK->APQALIDPSIQASA: 5'-
phosphate at distal end of gap no longer
advantageous for rNTP or dNTP addition
(in Pol domain).
{ECO:0000269|PubMed:20018881}.
MUTAGEN 553 566 HPQRLIDPSIQASK->APQRLIDPSIQASA: Addition
of rNTP to gapped molecule decreases to 1
or 2 nucleotides, dNTP addition
decreased, 5'-phosphate at distal end of
gap no longer advantageous (in Pol
domain). {ECO:0000269|PubMed:20018881}.
MUTAGEN 553 553 H->A: Wild-type gap closing by rNTP or
dNTP addition (in Pol domain).
{ECO:0000269|PubMed:20018881}.
MUTAGEN 556 556 R->A: Decreases gap closing efficiency by
rNTP, wild-type by dNTP (in Pol domain).
{ECO:0000269|PubMed:20018881}.
MUTAGEN 566 566 K->A: No change in dNTP addition to
gapped molecule, 5'-phosphate at distal
of the gap no longer advantageous for
rNTP addition (in Pol domain).
{ECO:0000269|PubMed:20018881}.
MUTAGEN 603 603 F->A: Last nucleotide rarely added during
gap closing for dNTP or rNTP addition,
(in Pol domain). Stacks a DNA template
base. {ECO:0000269|PubMed:20018881}.
MUTAGEN 604 604 F->A: Nearly complete loss of templated
dNTP or rNTP addition (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 669 671 DLD->ALA: Loss of templated and non-
templated DNA synthesis (in Pol domain).
{ECO:0000269|PubMed:15520014}.
MUTAGEN 669 669 D->A,N: Loss of templated DNA synthesis
(in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 669 669 D->E: Partial loss of templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 671 671 D->A,E,N: Loss of templated DNA synthesis
(in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 710 710 H->A: Loss of templated DNA synthesis (in
Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 710 710 H->N: Partial loss of templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 710 710 H->Q: Nearly wild-type templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 752 752 R->A,Q: Loss of templated DNA synthesis
(in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 752 752 R->K: Partial loss of templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 759 759 D->A,N: Loss of templated DNA synthesis
(in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 759 759 D->E: Partial loss of templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 776 776 R->A: Loss of templated DNA synthesis (in
Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 776 776 R->K: Nearly wild-type templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 776 776 R->Q: Partial loss of templated DNA
synthesis (in Pol domain).
{ECO:0000269|PubMed:16446439}.
MUTAGEN 778 778 R->A: Nearly wild-type templated dNTP or
rNTP addition (in Pol domain).
{ECO:0000269|PubMed:16446439}.
STRAND 35 55 {ECO:0000244|PDB:3N9B}.
STRAND 58 64 {ECO:0000244|PDB:3N9B}.
STRAND 72 74 {ECO:0000244|PDB:2LJ6}.
STRAND 76 84 {ECO:0000244|PDB:3N9B}.
HELIX 86 90 {ECO:0000244|PDB:3N9B}.
STRAND 91 95 {ECO:0000244|PDB:2LJ6}.
TURN 97 100 {ECO:0000244|PDB:2LJ6}.
STRAND 104 117 {ECO:0000244|PDB:3N9B}.
HELIX 119 125 {ECO:0000244|PDB:3N9B}.
STRAND 127 136 {ECO:0000244|PDB:3N9B}.
STRAND 138 145 {ECO:0000244|PDB:3N9B}.
STRAND 148 153 {ECO:0000244|PDB:2LJ6}.
STRAND 154 159 {ECO:0000244|PDB:3N9B}.
TURN 168 170 {ECO:0000244|PDB:3N9B}.
HELIX 173 176 {ECO:0000244|PDB:3N9B}.
TURN 181 183 {ECO:0000244|PDB:3N9B}.
TURN 544 548 {ECO:0000244|PDB:2FAO}.
STRAND 556 559 {ECO:0000244|PDB:2FAO}.
HELIX 560 562 {ECO:0000244|PDB:2FAO}.
HELIX 566 575 {ECO:0000244|PDB:2FAO}.
HELIX 577 584 {ECO:0000244|PDB:2FAO}.
STRAND 587 593 {ECO:0000244|PDB:2FAO}.
STRAND 603 605 {ECO:0000244|PDB:2FAO}.
HELIX 621 623 {ECO:0000244|PDB:2FAO}.
STRAND 630 632 {ECO:0000244|PDB:2FAO}.
HELIX 636 644 {ECO:0000244|PDB:2FAO}.
STRAND 647 652 {ECO:0000244|PDB:2FAO}.
STRAND 664 672 {ECO:0000244|PDB:2FAO}.
HELIX 678 695 {ECO:0000244|PDB:2FAO}.
STRAND 700 703 {ECO:0000244|PDB:2FAO}.
STRAND 705 714 {ECO:0000244|PDB:2FAO}.
HELIX 721 738 {ECO:0000244|PDB:2FAO}.
TURN 740 742 {ECO:0000244|PDB:2FAO}.
HELIX 749 751 {ECO:0000244|PDB:2FAO}.
STRAND 755 759 {ECO:0000244|PDB:2FAO}.
HELIX 761 763 {ECO:0000244|PDB:2FAO}.
HELIX 789 794 {ECO:0000244|PDB:2FAO}.
TURN 803 805 {ECO:0000244|PDB:2FAO}.
HELIX 806 813 {ECO:0000244|PDB:2FAO}.
TURN 818 824 {ECO:0000244|PDB:2FAO}.
HELIX 831 836 {ECO:0000244|PDB:2FAO}.
SEQUENCE 840 AA; 94030 MW; 5CAE7929CC5F29C7 CRC64;
MPSSKPLAEY ARKRDFRQTP EPSGRKPRKD STGLLRYCVQ KHDASRLHYD FRLELDGTLK
SWAVPKGPCL DPAVKRLAVQ VEDHPLDYAD FEGSIPQGHY GAGDVIVWDR GAWTPLDDPR
EGLEKGHLSF ALDGEKLSGR WHLIRTNLRG KQSQWFLVKA KDGEARSLDR FDVLKERPDS
VLSERTLLPR HGEAATPAAR PARRGKSGGK TPMPEWIAPE LASLVEQPPR GEWAYELKLD
GYRLMSRIED GHVRLLTRNG HDWTERLPHL EKALAGLGLQ RSWLDGELVV LDEEGRPDFQ
ALQNAFEEGR GENILYVLFD LPYHEGEDLR DVALEERRAR LEALLEGRDE DPLRFSATLA
EDPRDLLASA CKLGLEGVIG KRLGSAYRSR RSNDWIKLKC QLRQEFVIVG YTEPKGSRRH
IGALLLGLYS PDEERRLRYA GKVGSGFTAA SLKKVRERLE PLAVRSSPLA KVPPARETGS
VQWVRPQQLC EVSYAQMTRG GIIRQAVFHG LREDKPAREV TGERPAGPPP LRGARKASAG
ASRAATAGVR ISHPQRLIDP SIQASKLELA EFHARYADLL LRDLRERPVS LVRGPDGIGG
ELFFQKHAAR LKIPGIVQLD PALDPGHPPL LQIRSAEALV GAVQMGSIEF HTWNASLANL
ERPDRFVLDL DPDPALPWKR MLEATQLSLT LLDELGLRAF LKTSGGKGMH LLVPLERRHG
WDEVKDFAQA ISQHLARLMP ERFSAVSGPR NRVGKIFVDY LRNSRGASTV AAYSVRAREG
LPVSVPVFRE ELDSLQGANQ WNLRSLPQRL DELAGDDPWA DYAGTRQRIS AAMRRQLGRG


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