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