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 27-MAR-2024, entry version 137. 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; Pseudomonadota; 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., 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 208964.PA2138; -. DR PaxDb; 208964-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 OrthoDB; 9802472at2; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB. DR GO; GO:0004532; F:RNA exonuclease 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 CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1. DR CDD; cd07971; OBF_DNA_ligase_LigD; 1. DR CDD; cd04862; PaeLigD_Pol_like; 1. DR DisProt; DP01670; -. DR Gene3D; 3.30.1490.70; -; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 NCBIfam; TIGR02777; LigD_PE_dom; 1. DR NCBIfam; TIGR02778; ligD_pol; 1. DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1. DR NCBIfam; TIGR02776; NHEJ_ligase_prk; 1. DR PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1. DR PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF13298; LigD_N; 1. DR Pfam; PF21686; LigD_Prim-Pol; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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 FT 3'-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 FT 3'-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 //