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Database: UniProt
Entry: Q7Z5Q5
LinkDB: Q7Z5Q5
Original site: Q7Z5Q5 
ID   DPOLN_HUMAN             Reviewed;         900 AA.
AC   Q7Z5Q5; A2A336; B4E158; Q4TTW4; Q6ZNF4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   17-JUN-2020, entry version 142.
DE   RecName: Full=DNA polymerase nu;
DE            EC=2.7.7.7 {ECO:0000269|PubMed:12794064, ECO:0000269|PubMed:16787914};
GN   Name=POLN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, VARIANT
RP   HIS-121, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF ASP-623.
RX   PubMed=12794064; DOI=10.1074/jbc.m305646200;
RA   Marini F., Kim N., Schuffert A., Wood R.D.;
RT   "POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-
RT   link sensitivity protein Mus308.";
RL   J. Biol. Chem. 278:32014-32019(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   CYS-425.
RC   TISSUE=Brain, and Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-121; GLY-201; LEU-310;
RP   SER-315; SER-336; CYS-425; GLY-502 AND LEU-711.
RG   NIEHS SNPs program;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF ASP-623.
RX   PubMed=16787914; DOI=10.1074/jbc.m604317200;
RA   Takata K., Shimizu T., Iwai S., Wood R.D.;
RT   "Human DNA polymerase N (POLN) is a low fidelity enzyme capable of error-
RT   free bypass of 5S-thymine glycol.";
RL   J. Biol. Chem. 281:23445-23455(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=17118716; DOI=10.1016/j.dnarep.2006.09.012;
RA   Arana M.E., Takata K., Garcia-Diaz M., Wood R.D., Kunkel T.A.;
RT   "A unique error signature for human DNA polymerase nu.";
RL   DNA Repair 6:213-223(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=19908865; DOI=10.1021/bi9015346;
RA   Zietlow L., Smith L.A., Bessho M., Bessho T.;
RT   "Evidence for the involvement of human DNA polymerase N in the repair of
RT   DNA interstrand cross-links.";
RL   Biochemistry 48:11817-11824(2009).
RN   [9]
RP   FUNCTION.
RX   PubMed=20102227; DOI=10.1021/tx900449u;
RA   Yamanaka K., Minko I.G., Takata K., Kolbanovskiy A., Kozekov I.D.,
RA   Wood R.D., Rizzo C.J., Lloyd R.S.;
RT   "Novel enzymatic function of DNA polymerase nu in translesion DNA synthesis
RT   past major groove DNA-peptide and DNA-DNA cross-links.";
RL   Chem. Res. Toxicol. 23:689-695(2010).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH FANCD2; FANCI; PCNA; RAD51 AND HELQ.
RX   PubMed=19995904; DOI=10.1128/mcb.01124-09;
RA   Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
RA   Vinciguerra P., D'Andrea A.D.;
RT   "DNA polymerase POLN participates in cross-link repair and homologous
RT   recombination.";
RL   Mol. Cell. Biol. 30:1088-1096(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 194-859, AND MUTAGENESIS OF
RP   GLU-675 AND LYS-679.
RX   PubMed=25775266; DOI=10.1038/nsmb.2985;
RA   Lee Y.S., Gao Y., Yang W.;
RT   "How a homolog of high-fidelity replicases conducts mutagenic DNA
RT   synthesis.";
RL   Nat. Struct. Mol. Biol. 22:298-303(2015).
CC   -!- FUNCTION: DNA polymerase with very low fidelity that catalyzes
CC       considerable misincorporation by inserting dTTP opposite a G template,
CC       and dGTP opposite a T template (PubMed:16787914, PubMed:17118716). Is
CC       the least accurate of the DNA polymerase A family (i.e. POLG, POLN and
CC       POLQ) (PubMed:17118716). Can perform accurate translesion DNA synthesis
CC       (TLS) past a 5S-thymine glycol. Can perform efficient strand
CC       displacement past a nick or a gap and gives rise to an amount of
CC       product similar to that on non-damaged template. Has no exonuclease
CC       activity (PubMed:16787914). Error-prone DNA polymerase that
CC       preferentially misincorporates dT regardless of template sequence
CC       (PubMed:25775266). May play a role in TLS during interstrand cross-link
CC       (ICL) repair (PubMed:19908865). May be involved in TLS when genomic
CC       replication is blocked by extremely large major groove DNA lesions. May
CC       function in the bypass of some DNA-protein and DNA-DNA cross-links. May
CC       have a role in cellular tolerance to DNA cross-linking agents
CC       (PubMed:20102227). Involved in the repair of DNA cross-links and
CC       double-strand break (DSB) resistance. Participates in FANCD2-mediated
CC       repair. Forms a complex with HELQ helicase that participates in
CC       homologous recombination (HR) repair and is essential for cellular
CC       protection against DNA cross-links (PubMed:19995904).
CC       {ECO:0000269|PubMed:16787914, ECO:0000269|PubMed:17118716,
CC       ECO:0000269|PubMed:19908865, ECO:0000269|PubMed:19995904,
CC       ECO:0000269|PubMed:20102227, ECO:0000269|PubMed:25775266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:12794064,
CC         ECO:0000269|PubMed:16787914};
CC   -!- ACTIVITY REGULATION: Inhibited by ddTTP. {ECO:0000269|PubMed:16787914}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.0 uM for dATP:T {ECO:0000269|PubMed:16787914};
CC         KM=8.2 uM for dCTP:G {ECO:0000269|PubMed:16787914};
CC         KM=7.7 uM for dGTP:C {ECO:0000269|PubMed:16787914};
CC         KM=7.3 uM for dTTP:A {ECO:0000269|PubMed:16787914};
CC       pH dependence:
CC         Optimum pH is 8.8. {ECO:0000269|PubMed:16787914};
CC   -!- SUBUNIT: Interacts with FANCD2, FANCI, PCNA, RAD51 and HELQ.
CC       {ECO:0000269|PubMed:19995904}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12794064}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z5Q5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z5Q5-3; Sequence=VSP_054402, VSP_054403;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis and heart. Weakly
CC       expressed in skeletal muscle. {ECO:0000269|PubMed:12794064}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD18421.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/poln/";
DR   EMBL; AY136549; AAN52116.1; -; mRNA.
DR   EMBL; AK131239; BAD18421.1; ALT_SEQ; mRNA.
DR   EMBL; AK303673; BAG64670.1; -; mRNA.
DR   EMBL; DQ060036; AAY43130.1; -; Genomic_DNA.
DR   EMBL; AL136360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471131; EAW82539.1; -; Genomic_DNA.
DR   CCDS; CCDS3360.1; -. [Q7Z5Q5-1]
DR   RefSeq; NP_861524.2; NM_181808.3. [Q7Z5Q5-1]
DR   PDB; 4XVI; X-ray; 3.10 A; A=194-859.
DR   PDB; 4XVK; X-ray; 2.95 A; A=194-859.
DR   PDB; 4XVL; X-ray; 3.30 A; A=194-859.
DR   PDB; 4XVM; X-ray; 3.20 A; A=194-859.
DR   PDBsum; 4XVI; -.
DR   PDBsum; 4XVK; -.
DR   PDBsum; 4XVL; -.
DR   PDBsum; 4XVM; -.
DR   SMR; Q7Z5Q5; -.
DR   BioGRID; 131695; 31.
DR   STRING; 9606.ENSP00000435506; -.
DR   BindingDB; Q7Z5Q5; -.
DR   ChEMBL; CHEMBL2010628; -.
DR   iPTMnet; Q7Z5Q5; -.
DR   PhosphoSitePlus; Q7Z5Q5; -.
DR   BioMuta; POLN; -.
DR   DMDM; 90101282; -.
DR   jPOST; Q7Z5Q5; -.
DR   MassIVE; Q7Z5Q5; -.
DR   PaxDb; Q7Z5Q5; -.
DR   PeptideAtlas; Q7Z5Q5; -.
DR   PRIDE; Q7Z5Q5; -.
DR   ProteomicsDB; 69348; -. [Q7Z5Q5-1]
DR   Antibodypedia; 22333; 70 antibodies.
DR   DNASU; 353497; -.
DR   Ensembl; ENST00000382865; ENSP00000372316; ENSG00000130997. [Q7Z5Q5-1]
DR   Ensembl; ENST00000511885; ENSP00000435506; ENSG00000130997. [Q7Z5Q5-1]
DR   GeneID; 353497; -.
DR   KEGG; hsa:353497; -.
DR   UCSC; uc003ger.3; human. [Q7Z5Q5-1]
DR   CTD; 353497; -.
DR   DisGeNET; 353497; -.
DR   EuPathDB; HostDB:ENSG00000130997.16; -.
DR   GeneCards; POLN; -.
DR   HGNC; HGNC:18870; POLN.
DR   HPA; ENSG00000130997; Low tissue specificity.
DR   MIM; 610887; gene.
DR   neXtProt; NX_Q7Z5Q5; -.
DR   OpenTargets; ENSG00000130997; -.
DR   PharmGKB; PA134979866; -.
DR   eggNOG; ENOG410IPH2; Eukaryota.
DR   eggNOG; COG0749; LUCA.
DR   GeneTree; ENSGT00940000159015; -.
DR   HOGENOM; CLU_015708_0_0_1; -.
DR   InParanoid; Q7Z5Q5; -.
DR   KO; K16618; -.
DR   OMA; PRIHAHD; -.
DR   OrthoDB; 931773at2759; -.
DR   PhylomeDB; Q7Z5Q5; -.
DR   TreeFam; TF337202; -.
DR   Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR   BioGRID-ORCS; 353497; 2 hits in 791 CRISPR screens.
DR   ChiTaRS; POLN; human.
DR   GeneWiki; DNA_polymerase_nu; -.
DR   GenomeRNAi; 353497; -.
DR   Pharos; Q7Z5Q5; Tbio.
DR   PRO; PR:Q7Z5Q5; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q7Z5Q5; protein.
DR   Bgee; ENSG00000130997; Expressed in amniotic fluid and 133 other tissues.
DR   ExpressionAtlas; Q7Z5Q5; baseline and differential.
DR   Genevisible; Q7Z5Q5; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR   GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR   GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR040940; DNA_pol_P_Exo.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF18049; DNA_pol_P_Exo; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..900
FT                   /note="DNA polymerase nu"
FT                   /id="PRO_0000227938"
FT   VAR_SEQ         578..610
FT                   /note="NIQGISKHPIQITTPKNFKGKEDKILTISPRAM -> ICARQVASDFQKCVE
FT                   VSDAMMNSSIFWWLLKLY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054402"
FT   VAR_SEQ         611..899
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054403"
FT   VARIANT         121
FT                   /note="Q -> H (in dbSNP:rs2353552)"
FT                   /evidence="ECO:0000269|PubMed:12794064, ECO:0000269|Ref.3"
FT                   /id="VAR_025647"
FT   VARIANT         201
FT                   /note="R -> G (in dbSNP:rs35884361)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025648"
FT   VARIANT         310
FT                   /note="M -> L (in dbSNP:rs10018786)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025649"
FT   VARIANT         315
FT                   /note="P -> S (in dbSNP:rs11725880)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025650"
FT   VARIANT         336
FT                   /note="G -> S (in dbSNP:rs10011549)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025651"
FT   VARIANT         425
FT                   /note="R -> C (in dbSNP:rs9328764)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT                   /id="VAR_025652"
FT   VARIANT         502
FT                   /note="S -> G (in dbSNP:rs34574483)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025653"
FT   VARIANT         711
FT                   /note="F -> L (in dbSNP:rs34554757)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025654"
FT   MUTAGEN         623
FT                   /note="D->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:12794064,
FT                   ECO:0000269|PubMed:16787914"
FT   MUTAGEN         675
FT                   /note="E->R: Reduces polymerase activity. No effect on
FT                   accuracy."
FT                   /evidence="ECO:0000269|PubMed:25775266"
FT   MUTAGEN         679
FT                   /note="K->A: No effect on polymerase activity. Increases
FT                   accuracy by ten-fold."
FT                   /evidence="ECO:0000269|PubMed:25775266"
FT   CONFLICT        8
FT                   /note="V -> A (in Ref. 2; BAG64670)"
FT                   /evidence="ECO:0000305"
FT   STRAND          196..199
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           200..202
FT                   /evidence="ECO:0000244|PDB:4XVM"
FT   HELIX           205..217
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          219..227
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   TURN            233..235
FT                   /evidence="ECO:0000244|PDB:4XVM"
FT   STRAND          244..253
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          273..275
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          280..284
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           293..311
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          316..320
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           321..332
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           333..335
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           338..340
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           349..356
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          358..360
FT                   /evidence="ECO:0000244|PDB:4XVL"
FT   HELIX           365..372
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           390..417
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           421..426
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   TURN            427..430
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           431..440
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          443..445
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           447..472
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           481..488
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   TURN            489..491
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           494..497
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          500..506
FT                   /evidence="ECO:0000244|PDB:4XVI"
FT   STRAND          508..511
FT                   /evidence="ECO:0000244|PDB:4XVI"
FT   HELIX           516..521
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   TURN            522..525
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           528..545
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           547..550
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          561..566
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          568..570
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          573..577
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   TURN            579..581
FT                   /evidence="ECO:0000244|PDB:4XVM"
FT   STRAND          587..590
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          602..605
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           607..610
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          618..624
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           627..636
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           639..643
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           654..662
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           666..668
FT                   /evidence="ECO:0000244|PDB:4XVM"
FT   HELIX           671..685
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           690..696
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           701..714
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           717..732
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          733..736
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          738..740
FT                   /evidence="ECO:0000244|PDB:4XVL"
FT   STRAND          742..744
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           746..749
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           753..788
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          796..801
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          804..809
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           811..813
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           814..826
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   HELIX           827..829
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          832..834
FT                   /evidence="ECO:0000244|PDB:4XVK"
FT   STRAND          844..853
FT                   /evidence="ECO:0000244|PDB:4XVK"
SQ   SEQUENCE   900 AA;  100307 MW;  D44758D71BCD3F02 CRC64;
     MENYEALVGF DLCNTPLSSV AQKIMSAMHS GDLVDSKTWG KSTETMEVIN KSSVKYSVQL
     EDRKTQSPEK KDLKSLRSQT SRGSAKLSPQ SFSVRLTDQL SADQKQKSIS SLTLSSCLIP
     QYNQEASVLQ KKGHKRKHFL MENINNENKG SINLKRKHIT YNNLSEKTSK QMALEEDTDD
     AEGYLNSGNS GALKKHFCDI RHLDDWAKSQ LIEMLKQAAA LVITVMYTDG STQLGADQTP
     VSSVRGIVVL VKRQAEGGHG CPDAPACGPV LEGFVSDDPC IYIQIEHSAI WDQEQEAHQQ
     FARNVLFQTM KCKCPVICFN AKDFVRIVLQ FFGNDGSWKH VADFIGLDPR IAAWLIDPSD
     ATPSFEDLVE KYCEKSITVK VNSTYGNSSR NIVNQNVREN LKTLYRLTMD LCSKLKDYGL
     WQLFRTLELP LIPILAVMES HAIQVNKEEM EKTSALLGAR LKELEQEAHF VAGERFLITS
     NNQLREILFG KLKLHLLSQR NSLPRTGLQK YPSTSEAVLN ALRDLHPLPK IILEYRQVHK
     IKSTFVDGLL ACMKKGSISS TWNQTGTVTG RLSAKHPNIQ GISKHPIQIT TPKNFKGKED
     KILTISPRAM FVSSKGHTFL AADFSQIELR ILTHLSGDPE LLKLFQESER DDVFSTLTSQ
     WKDVPVEQVT HADREQTKKV VYAVVYGAGK ERLAACLGVP IQEAAQFLES FLQKYKKIKD
     FARAAIAQCH QTGCVVSIMG RRRPLPRIHA HDQQLRAQAE RQAVNFVVQG SAADLCKLAM
     IHVFTAVAAS HTLTARLVAQ IHDELLFEVE DPQIPECAAL VRRTMESLEQ VQALELQLQV
     PLKVSLSAGR SWGHLVPLQE AWGPPPGPCR TESPSNSLAA PGSPASTQPP PLHFSPSFCL
//
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