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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   12-AUG-2020, entry version 121.
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 / JCM
OS   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 / 1C /
RC   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., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   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; ARG-52;
RP   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 non-
RT   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 DNA
RT   ligase D, a nonhomologous end-joining enzyme.";
RL   J. Biol. Chem. 280:33707-33715(2005).
RN   [5]
RP   FUNCTION IN GAP-FILLING, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-553;
RP   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 and
RT   functional interactions of LigD with the DNA end-binding Ku 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 OF
RP   PHE-604; ASP-669; ASP-671; HIS-710; ARG-752; ASP-759; ARG-776 AND ARG-778.
RX   PubMed=16446439; DOI=10.1073/pnas.0509083103;
RA   Zhu H., Nandakumar J., Aniukwu J., Wang L.K., Glickman M.S., Lima C.D.,
RA   Shuman S.;
RT   "Atomic structure and nonhomologous end-joining function of the polymerase
RT   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 MANGANESE,
RP   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 (NHEJ)
CC       repair enzyme, which repairs dsDNA breaks (DSB) with reduced fidelity.
CC       Acts as a DNA ligase on singly nicked dsDNA, fills dsDNA gaps (3- or
CC       4- nucleotide gaps, prefers a 5'-phosphate at the gap distal end,
CC       prefers dNTPs over rNTPs) (PubMed:20018881), has DNA-directed DNA
CC       polymerase activity (templated primer extension) and DNA-directed RNA
CC       polymerase activity (PubMed:15897197), adds 1 or 2 non-templated rNTP
CC       (or less well dNTP) to ssDNA or blunt-end dsDNA (primer extension). Has
CC       3' resection activity, removing 3'-rNMPs from DNA using its 3'-
CC       ribonuclease and 3'-phosphatase activities sequentially. Resection
CC       requires a 2'-OH in the penultimate nucleoside position (i.e. a
CC       ribo- not deoxyribonucleoside) (PubMed:15897197), although the 3'-
CC       phosphatase activity does not, and its specific activity is 16-fold
CC       higher on a DNA substrate (PubMed:16046407). On appropriate substrates
CC       will extend a DNA primer to the end of the template strand and then
CC       incorporate a non-templated nucleotide. {ECO:0000269|PubMed:15897197,
CC       ECO:0000269|PubMed:16046407, ECO:0000269|PubMed:20018881}.
CC   -!- FUNCTION: The preference of the polymerase domain for rNTPs over dNTPs
CC       may be advantageous in quiescent cells where the dNTP pool may be
CC       limiting.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000305|PubMed:15520014, ECO:0000305|PubMed:15897197,
CC         ECO:0000305|PubMed:16046407, ECO:0000305|PubMed:16446439};
CC       Note=Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each
CC       for 3-phosphoesterase and ligase. {ECO:0000305|PubMed:15520014,
CC       ECO:0000305|PubMed:15897197, ECO:0000305|PubMed:16046407,
CC       ECO:0000305|PubMed:16446439};
CC   -!- ACTIVITY 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). {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 an
CC       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 fashion
CC       (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 bacteria
CC       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 DNA
CC       ligase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the LigD polymerase
CC       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; NZ_QZGE01000014.1.
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   SMR; Q9I1X7; -.
DR   PaxDb; Q9I1X7; -.
DR   PRIDE; Q9I1X7; -.
DR   EnsemblBacteria; AAG05526; AAG05526; PA2138.
DR   GeneID; 880451; -.
DR   KEGG; pae:PA2138; -.
DR   PATRIC; fig|208964.12.peg.2235; -.
DR   PseudoCAP; PA2138; -.
DR   HOGENOM; CLU_008325_0_0_6; -.
DR   InParanoid; Q9I1X7; -.
DR   KO; K01971; -.
DR   OMA; YMANLGC; -.
DR   PhylomeDB; Q9I1X7; -.
DR   BioCyc; PAER208964:G1FZ6-2177-MONOMER; -.
DR   EvolutionaryTrace; Q9I1X7; -.
DR   Proteomes; UP000002438; Chromosome.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:PseudoCAP.
DR   CDD; cd04862; PaeLigD_Pol_like; 1.
DR   DisProt; DP01670; -.
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; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; 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
FT                   /note="Multifunctional non-homologous end joining protein
FT                   LigD"
FT                   /id="PRO_0000425950"
FT   NP_BIND         704..710
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   NP_BIND         776..778
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   REGION          7..162
FT                   /note="3'-phosphoesterase domain (PE)"
FT   REGION          219..521
FT                   /note="Ligase domain (Lig)"
FT   REGION          549..793
FT                   /note="DNA repair polymerase domain (Pol)"
FT   ACT_SITE        238
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000305"
FT   METAL           42
FT                   /note="Manganese 1; via pros nitrogen; catalytic; for 3'-
FT                   phosphoesterase activity"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   METAL           48
FT                   /note="Manganese 1; via tele nitrogen; catalytic; for 3'-
FT                   phosphoesterase activity"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   METAL           50
FT                   /note="Manganese 1; catalytic; for 3'-phosphoesterase
FT                   activity"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   METAL           240
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           376
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           669
FT                   /note="Manganese 3"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   METAL           669
FT                   /note="Manganese 4"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   METAL           671
FT                   /note="Manganese 3"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   METAL           759
FT                   /note="Manganese 4"
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:20616014"
FT   BINDING         604
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   BINDING         651
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   BINDING         671
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   BINDING         768
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   SITE            84
FT                   /note="Transition state stabilizer; for 3'-phosphoesterase
FT                   activity"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         14
FT                   /note="R->A: 77% ribonuclease activity, loss of 3'-
FT                   phosphatase activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         15
FT                   /note="D->A: 3% 3'-phosphatase activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         21
FT                   /note="E->A: Loss of 3'-phosphatase activity (in PE
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         40
FT                   /note="Q->A: 41% ribonuclease activity, 7% 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         42
FT                   /note="H->A: Loss of ribonuclease and 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         46
FT                   /note="R->A: 16% ribonuclease activity, 20% 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         48
FT                   /note="H->A: Loss of ribonuclease and 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         50
FT                   /note="D->A: Loss of nuclease and 3'-phosphatase activity
FT                   (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:15897197"
FT   MUTAGEN         52
FT                   /note="R->A: Loss of nuclease and 3'-phosphatase activity
FT                   (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:15897197"
FT   MUTAGEN         54
FT                   /note="E->A: Nearly wild-type nuclease and 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:15897197"
FT   MUTAGEN         66
FT                   /note="K->A: 3% ribonuclease activity, 28% 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         76
FT                   /note="R->A: 1% ribonuclease activity, 16% 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         82
FT                   /note="E->A: Selective loss of 3'-phosphatase activity (in
FT                   PE domain)."
FT                   /evidence="ECO:0000269|PubMed:15897197"
FT   MUTAGEN         83
FT                   /note="D->A: 57% ribonuclease activity, 50% 3'-phosphatase
FT                   activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         84
FT                   /note="H->A: Loss of nuclease and 3'-phosphatase activity
FT                   (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:15897197"
FT   MUTAGEN         88
FT                   /note="Y->A: 7% ribonuclease activity, loss of 3'-
FT                   phosphatase activity (in PE domain)."
FT                   /evidence="ECO:0000269|PubMed:16046407"
FT   MUTAGEN         553..566
FT                   /note="HPQRLIDPSIQASK->APQALIDPSIQASA: 5'-phosphate at
FT                   distal end of gap no longer advantageous for rNTP or dNTP
FT                   addition (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:20018881"
FT   MUTAGEN         553..566
FT                   /note="HPQRLIDPSIQASK->APQRLIDPSIQASA: Addition of rNTP to
FT                   gapped molecule decreases to 1 or 2 nucleotides, dNTP
FT                   addition decreased, 5'-phosphate at distal end of gap no
FT                   longer advantageous (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:20018881"
FT   MUTAGEN         553
FT                   /note="H->A: Wild-type gap closing by rNTP or dNTP addition
FT                   (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:20018881"
FT   MUTAGEN         556
FT                   /note="R->A: Decreases gap closing efficiency by rNTP,
FT                   wild-type by dNTP (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:20018881"
FT   MUTAGEN         566
FT                   /note="K->A: No change in dNTP addition to gapped molecule,
FT                   5'-phosphate at distal of the gap no longer advantageous
FT                   for rNTP addition (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:20018881"
FT   MUTAGEN         603
FT                   /note="F->A: Last nucleotide rarely added during gap
FT                   closing for dNTP or rNTP addition, (in Pol domain). Stacks
FT                   a DNA template base."
FT                   /evidence="ECO:0000269|PubMed:20018881"
FT   MUTAGEN         604
FT                   /note="F->A: Nearly complete loss of templated dNTP or rNTP
FT                   addition (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         669..671
FT                   /note="DLD->ALA: Loss of templated and non-templated DNA
FT                   synthesis (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:15520014"
FT   MUTAGEN         669
FT                   /note="D->A,N: Loss of templated DNA synthesis (in Pol
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         669
FT                   /note="D->E: Partial loss of templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         671
FT                   /note="D->A,E,N: Loss of templated DNA synthesis (in Pol
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         710
FT                   /note="H->A: Loss of templated DNA synthesis (in Pol
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         710
FT                   /note="H->N: Partial loss of templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         710
FT                   /note="H->Q: Nearly wild-type templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         752
FT                   /note="R->A,Q: Loss of templated DNA synthesis (in Pol
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         752
FT                   /note="R->K: Partial loss of templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         759
FT                   /note="D->A,N: Loss of templated DNA synthesis (in Pol
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         759
FT                   /note="D->E: Partial loss of templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         776
FT                   /note="R->A: Loss of templated DNA synthesis (in Pol
FT                   domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         776
FT                   /note="R->K: Nearly wild-type templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         776
FT                   /note="R->Q: Partial loss of templated DNA synthesis (in
FT                   Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   MUTAGEN         778
FT                   /note="R->A: Nearly wild-type templated dNTP or rNTP
FT                   addition (in Pol domain)."
FT                   /evidence="ECO:0000269|PubMed:16446439"
FT   STRAND          35..55
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   STRAND          58..64
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   STRAND          72..74
FT                   /evidence="ECO:0000244|PDB:2LJ6"
FT   STRAND          76..84
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   HELIX           86..90
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   STRAND          91..95
FT                   /evidence="ECO:0000244|PDB:2LJ6"
FT   TURN            97..100
FT                   /evidence="ECO:0000244|PDB:2LJ6"
FT   STRAND          104..117
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   HELIX           119..125
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   STRAND          127..136
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   STRAND          138..145
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   STRAND          148..153
FT                   /evidence="ECO:0000244|PDB:2LJ6"
FT   STRAND          154..159
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   TURN            168..170
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   HELIX           173..176
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   TURN            181..183
FT                   /evidence="ECO:0000244|PDB:3N9B"
FT   TURN            544..548
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          556..559
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           560..562
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           566..575
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           577..584
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          587..593
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          603..605
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           621..623
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          630..632
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           636..644
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          647..652
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          664..672
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           678..695
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          700..703
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          705..714
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           721..738
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   TURN            740..742
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           749..751
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   STRAND          755..759
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           761..763
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           789..794
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   TURN            803..805
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           806..813
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   TURN            818..824
FT                   /evidence="ECO:0000244|PDB:2FAO"
FT   HELIX           831..836
FT                   /evidence="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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