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 03-AUG-2022, entry version 128.
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}.
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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 AlphaFoldDB; Q9I1X7; -.
DR BMRB; Q9I1X7; -.
DR SMR; Q9I1X7; -.
DR STRING; 287.DR97_6291; -.
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 HOGENOM; CLU_008325_0_0_6; -.
DR InParanoid; Q9I1X7; -.
DR OMA; YMANLGC; -.
DR PhylomeDB; Q9I1X7; -.
DR BioCyc; PAER208964:G1FZ6-2177-MON; -.
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 Gene3D; 2.40.50.140; -; 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; 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 REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7..162
FT /note="3'-phosphoesterase domain (PE)"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..521
FT /note="Ligase domain (Lig)"
FT REGION 514..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..793
FT /note="DNA repair polymerase domain (Pol)"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000305"
FT BINDING 42
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for 3'-phosphoesterase activity"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 48
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for 3'-phosphoesterase activity"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for 3'-phosphoesterase activity"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16446439"
FT BINDING 651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16446439"
FT BINDING 669
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 669
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 671
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16446439"
FT BINDING 671
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 704..710
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16446439"
FT BINDING 759
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:16446439,
FT ECO:0000269|PubMed:20616014"
FT BINDING 768
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16446439"
FT BINDING 776..778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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:0007829|PDB:3N9B"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3N9B"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2LJ6"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:3N9B"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:3N9B"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2LJ6"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2LJ6"
FT STRAND 104..117
FT /evidence="ECO:0007829|PDB:3N9B"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3N9B"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:3N9B"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3N9B"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2LJ6"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3N9B"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3N9B"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3N9B"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3N9B"
FT TURN 544..548
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 566..575
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 577..584
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 636..644
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 664..672
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 678..695
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 705..714
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 721..738
FT /evidence="ECO:0007829|PDB:2FAO"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 749..751
FT /evidence="ECO:0007829|PDB:2FAO"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 761..763
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 789..794
FT /evidence="ECO:0007829|PDB:2FAO"
FT TURN 803..805
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 806..813
FT /evidence="ECO:0007829|PDB:2FAO"
FT TURN 818..824
FT /evidence="ECO:0007829|PDB:2FAO"
FT HELIX 831..836
FT /evidence="ECO:0007829|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
