POLH_ARATH
ID POLH_ARATH Reviewed; 672 AA.
AC Q8H2D5; A4ZYA7; A4ZYA8; O48586; Q8H1C5; Q9C5F5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=DNA polymerase eta;
DE EC=2.7.7.7 {ECO:0000269|PubMed:16857217, ECO:0000269|PubMed:18366182};
DE AltName: Full=Radiation-sensitive protein 30;
DE Short=AtRAD30;
DE AltName: Full=Y-family DNA polymerase H;
DE Short=AtPOLH;
GN Name=POLH; Synonyms=RAD30; OrderedLocusNames=At5g44740;
GN ORFNames=K23L20.8, T19K24.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Alejandre-Duran E., Ariza R.R., Roldan-Arjona T., Ruiz-Rubio M.;
RT "A DNA polymerase homolog in the model plant Arabidopsis thaliana.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION IN UV PROTECTION,
RP MUTAGENESIS OF 120-ASP--VAL-122, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16857217; DOI=10.1016/j.mrfmmm.2006.05.036;
RA Santiago M.J., Alejandre-Duran E., Ruiz-Rubio M.;
RT "Analysis of UV-induced mutation spectra in Escherichia coli by DNA
RT polymerase eta from Arabidopsis thaliana.";
RL Mutat. Res. 601:51-60(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSLESION, DISRUPTION
RP PHENOTYPE, AND INTERACTION WITH PCNA1 AND PCNA2.
RX PubMed=18494853; DOI=10.1111/j.1365-313x.2008.03562.x;
RA Anderson H.J., Vonarx E.J., Pastushok L., Nakagawa M., Katafuchi A.,
RA Gruz P., Di Rubbo A., Grice D.M., Osmond M.J., Sakamoto A.N., Nohmi T.,
RA Xiao W., Kunz B.A.;
RT "Arabidopsis thaliana Y-family DNA polymerase eta catalyses translesion
RT synthesis and interacts functionally with PCNA2.";
RL Plant J. 55:895-908(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP REVIEW.
RX PubMed=15645454; DOI=10.1002/em.20094;
RA Kunz B.A., Anderson H.J., Osmond M.J., Vonarx E.J.;
RT "Components of nucleotide excision repair and DNA damage tolerance in
RT Arabidopsis thaliana.";
RL Environ. Mol. Mutagen. 45:115-127(2005).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=18366182; DOI=10.1021/bi701781p;
RA Hoffman P.D., Curtis M.J., Iwai S., Hays J.B.;
RT "Biochemical evolution of DNA polymerase eta: properties of plant, human,
RT and yeast proteins.";
RL Biochemistry 47:4583-4596(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18339443; DOI=10.1016/j.jplph.2007.11.012;
RA Jesus Santiago M., Alejandre-Duran E., Munoz-Serrano A., Ruiz-Rubio M.;
RT "Two translesion synthesis DNA polymerase genes, AtPOLH and AtREV1, are
RT involved in development and UV light resistance in Arabidopsis.";
RL J. Plant Physiol. 165:1582-1591(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22018494; DOI=10.1016/j.dnarep.2011.10.001;
RA Curtis M.J., Hays J.B.;
RT "Cooperative responses of DNA-damage-activated protein kinases ATR and ATM
RT and DNA translesion polymerases to replication-blocking DNA damage in a
RT stem-cell niche.";
RL DNA Repair 10:1272-1281(2011).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21030509; DOI=10.1104/pp.110.166082;
RA Nakagawa M., Takahashi S., Tanaka A., Narumi I., Sakamoto A.N.;
RT "Role of AtPolzeta, AtRev1, and AtPoleta in UV light-induced mutagenesis in
RT Arabidopsis.";
RL Plant Physiol. 155:414-420(2011).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21455019; DOI=10.4161/psb.6.5.15124;
RA Nakagawa M., Takahashi S., Narumi I., Sakamoto A.N.;
RT "Role of AtPolzeta, AtRev1 and AtPoleta in gamma ray-induced mutagenesis.";
RL Plant Signal. Behav. 6:728-731(2011).
CC -!- FUNCTION: Error-free DNA polymerase specifically involved in DNA
CC repair. Plays an important role in translesion synthesis (TLS), where
CC the normal high fidelity DNA polymerases cannot proceed and DNA
CC synthesis stalls. Plays an important role in the repair of UV-induced
CC pyrimidine dimers and confers resistance to ultraviolet light.
CC Depending on the context, it inserts the correct base, but may cause
CC base transitions and transversions. Forms a Schiff base with 5'-
CC deoxyribose phosphate at abasic sites, but does not have lyase
CC activity. Targets POLI to replication foci. Exhibits cyclobutane dimer
CC nonmutagenic bypass activity in vitro. {ECO:0000269|PubMed:16857217,
CC ECO:0000269|PubMed:18339443, ECO:0000269|PubMed:18366182,
CC ECO:0000269|PubMed:18494853, ECO:0000269|PubMed:21030509,
CC ECO:0000269|PubMed:21455019, ECO:0000269|PubMed:22018494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:16857217, ECO:0000269|PubMed:18366182};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC Note=Binds 2 Mg(2+). Prefers Mg(2+), but can also use Mn(2+). In vitro,
CC can also utilize other divalent cations such as Ca(2+).
CC {ECO:0000250|UniProtKB:Q9Y253};
CC -!- ACTIVITY REGULATION: The enzyme in complex with the DNA substrate binds
CC a third divalent metal cation. The binding of this third divalent
CC cation, which is coordinated by water molecules and two oxygen atoms
CC from DNA and dNTP, is essential for catalyzing the DNA synthesis.
CC {ECO:0000250|UniProtKB:Q9Y253}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 22 degrees Celsius.
CC {ECO:0000269|PubMed:18366182};
CC -!- SUBUNIT: Interacts with PCNA1 and PCNA2. The interaction with PCNA2 is
CC required for translesion synthesis (TLS) to repair UV photoproducts.
CC {ECO:0000269|PubMed:18494853}.
CC -!- INTERACTION:
CC Q8H2D5; Q9M7Q7: PCNA; NbExp=2; IntAct=EBI-1810451, EBI-1810458;
CC Q8H2D5; Q9ZW35: PCNA2; NbExp=2; IntAct=EBI-1810451, EBI-1810473;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Accumulates at
CC replication forks after DNA damage. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8H2D5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H2D5-2; Sequence=VSP_046623;
CC Name=3;
CC IsoId=Q8H2D5-3; Sequence=VSP_046626, VSP_046627;
CC Name=4;
CC IsoId=Q8H2D5-4; Sequence=VSP_046624, VSP_046625;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, stems, leaves,
CC flowers and siliques. {ECO:0000269|PubMed:16857217}.
CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC subdomains, but the fingers and thumb subdomains are much smaller than
CC in high-fidelity polymerases; residues from five sequence motifs of the
CC Y-family cluster around an active site cleft that can accommodate DNA
CC and nucleotide substrates with relaxed geometric constraints, with
CC consequently higher rates of misincorporation and low processivity.
CC {ECO:0000250|UniProtKB:Q9Y253}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to UV radiation accompanied
CC by an increased mutation frequency. Shorter root and stem growth.
CC {ECO:0000269|PubMed:18339443, ECO:0000269|PubMed:18494853,
CC ECO:0000269|PubMed:21030509, ECO:0000269|PubMed:21455019,
CC ECO:0000269|PubMed:22018494}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79146.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB08827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ416380; CAC94893.1; -; mRNA.
DR EMBL; EF495196; ABP49608.1; -; mRNA.
DR EMBL; EF495197; ABP49609.1; -; mRNA.
DR EMBL; AY151396; AAN39011.1; -; mRNA.
DR EMBL; AB016874; BAB08827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002342; AAC79146.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95154.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95155.1; -; Genomic_DNA.
DR EMBL; AF360283; AAK25993.1; -; mRNA.
DR EMBL; AY113879; AAM44927.1; -; mRNA.
DR RefSeq; NP_568638.2; NM_123841.5. [Q8H2D5-1]
DR RefSeq; NP_851130.1; NM_180799.2. [Q8H2D5-2]
DR AlphaFoldDB; Q8H2D5; -.
DR SMR; Q8H2D5; -.
DR BioGRID; 19753; 3.
DR IntAct; Q8H2D5; 3.
DR STRING; 3702.AT5G44740.2; -.
DR PaxDb; Q8H2D5; -.
DR PRIDE; Q8H2D5; -.
DR ProteomicsDB; 234857; -. [Q8H2D5-1]
DR EnsemblPlants; AT5G44740.1; AT5G44740.1; AT5G44740. [Q8H2D5-2]
DR EnsemblPlants; AT5G44740.2; AT5G44740.2; AT5G44740. [Q8H2D5-1]
DR GeneID; 834503; -.
DR Gramene; AT5G44740.1; AT5G44740.1; AT5G44740. [Q8H2D5-2]
DR Gramene; AT5G44740.2; AT5G44740.2; AT5G44740. [Q8H2D5-1]
DR KEGG; ath:AT5G44740; -.
DR Araport; AT5G44740; -.
DR TAIR; locus:2156309; AT5G44740.
DR eggNOG; KOG2095; Eukaryota.
DR HOGENOM; CLU_012348_7_2_1; -.
DR InParanoid; Q8H2D5; -.
DR OMA; YARACKK; -.
DR OrthoDB; 1593931at2759; -.
DR PhylomeDB; Q8H2D5; -.
DR PRO; PR:Q8H2D5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H2D5; baseline and differential.
DR Genevisible; Q8H2D5; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:TAIR.
DR GO; GO:0009314; P:response to radiation; IBA:GO_Central.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0009650; P:UV protection; IGI:UniProtKB.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; DNA replication;
KW DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Magnesium;
KW Manganese; Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Schiff base; Transferase.
FT CHAIN 1..672
FT /note="DNA polymerase eta"
FT /id="PRO_0000422771"
FT DOMAIN 14..254
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 318..325
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 362..383
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 521..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 18
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 18
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 23
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT SITE 23
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT VAR_SEQ 1..103
FT /note="MPVARPEASDARVIAHVDMDCFYVQVEQRKQPELRGLPSAVVQYNEWQGGGL
FT IAVSYEARKCGVKRSMRGDEAKAACPQIQLVQVPVARGKADLNLYRSAGSE -> MRLK
FT LLVLRFNWFKFLWLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_046623"
FT VAR_SEQ 333..350
FT /note="QHWLNQLSEELSERLGSD -> RVESQQCTSFPFAISCSS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16857217"
FT /id="VSP_046624"
FT VAR_SEQ 351..672
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16857217"
FT /id="VSP_046625"
FT VAR_SEQ 442
FT /note="G -> E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16857217"
FT /id="VSP_046626"
FT VAR_SEQ 443..672
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16857217"
FT /id="VSP_046627"
FT MUTAGEN 120..122
FT /note="DEV->AAA: Loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:16857217"
FT CONFLICT 205
FT /note="F -> L (in Ref. 3; AAN39011)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="F -> V (in Ref. 3; AAN39011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 73985 MW; DBE48E35014680BD CRC64;
MPVARPEASD ARVIAHVDMD CFYVQVEQRK QPELRGLPSA VVQYNEWQGG GLIAVSYEAR
KCGVKRSMRG DEAKAACPQI QLVQVPVARG KADLNLYRSA GSEVVSILAK SGKCERASID
EVYLDLTDAA ESMLADAPPE SLELIDEEVL KSHILGMNRE DGDDFKESVR NWICREDADR
RDKLLSCGII IVAELRKQVL KETEFTCSAG IAHNKMLAKL ASGMNKPAQQ TVVPYAAVQE
LLSSLPIKKM KQLGGKLGTS LQTDLGVDTV GDLLQFSETK LQEHYGVNTG TWLWNIARGI
SGEEVQGRLL PKSHGSGKTF PGPRALKSLS TVQHWLNQLS EELSERLGSD LEQNKRIAST
LTLHASAFRS KDSDSHKKFP SKSCPMRYGV TKIQEDAFNL FQAALREYMG SFGIKPQGNK
LETWRITGLS VSASKIVDIP SGTSSIMRYF QSQPTVPSRS ADGCVQGNVA MTASASEGCS
EQRSTETQAA MPEVDTGVTY TLPNFENQDK DIDLVSEKDV VSCPSNEATD VSTQSESNKG
TQTKKIGRKM NNSKEKNRGM PSIVDIFKNY NATPPSKQET QEDSTVSSAS KRAKLSSSSH
NSQVNQEVEE SRETDWGYKT DEIDQSVFDE LPVEIQRELR SFLRTNKQFN TGKSKGDGST
SSIAHYFPPL NR
