DPOLL_ARATH
ID DPOLL_ARATH Reviewed; 529 AA.
AC Q9FNY4; Q9XIK1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=DNA polymerase lambda {ECO:0000305};
DE Short=Pol Lambda {ECO:0000305};
DE EC=2.7.7.7 {ECO:0000305};
DE EC=4.2.99.- {ECO:0000305};
GN Name=POLL {ECO:0000305};
GN OrderedLocusNames=At1g10520 {ECO:0000312|Araport:AT1G10520};
GN ORFNames=T10O24.13 {ECO:0000312|EMBL:AAD39573.1};
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].
RX PubMed=10966791; DOI=10.1006/jmbi.2000.4005;
RA Garcia-Diaz M., Dominguez O., Lopez-Fernandez L.A., Lain de Lera T.,
RA Saniger M.L., Ruiz J.F., Parraga M., Garcia M.J., Kirchhoff T.,
RA del Mazo J., Bernad A., Blanco L.;
RT "DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with
RT a potential role in meiosis.";
RL J. Mol. Biol. 301:851-867(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Roy S., Roy Choudhury S., Singh S.K., Das K.P.;
RT "Arabidopsis thaliana DNA pol lambda (Poll) mRNA.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION.
RX PubMed=21889425; DOI=10.1016/j.dnarep.2011.07.011;
RA Huefner N.D., Mizuno Y., Weil C.F., Korf I., Britt A.B.;
RT "Breadth by depth: expanding our understanding of the repair of transposon-
RT induced DNA double strand breaks via deep-sequencing.";
RL DNA Repair 10:1023-1033(2011).
RN [8]
RP FUNCTION, AND INDUCTION BY UV-B.
RX PubMed=21227935; DOI=10.1093/pcp/pcr002;
RA Roy S., Choudhury S.R., Singh S.K., Das K.P.;
RT "AtPollambda, a homolog of mammalian DNA polymerase lambda in Arabidopsis
RT thaliana, is involved in the repair of UV-B induced DNA damage through the
RT dark repair pathway.";
RL Plant Cell Physiol. 52:448-467(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH XRCC4 AND LIG4.
RX PubMed=23660835; DOI=10.1104/pp.113.219022;
RA Roy S., Choudhury S.R., Sengupta D.N., Das K.P.;
RT "Involvement of AtPollambda in the repair of high salt- and DNA cross-
RT linking agent-induced double strand breaks in Arabidopsis.";
RL Plant Physiol. 162:1195-1210(2013).
RN [10]
RP INTERACTION WITH HSP90-1.
RX PubMed=26230318; DOI=10.1371/journal.pone.0133843;
RA Roy S., Banerjee V., Das K.P.;
RT "Understanding the physical and molecular basis of stability of Arabidopsis
RT DNA Pol lambda under UV-B and high NaCl stress.";
RL PLoS ONE 10:E0133843-E0133843(2015).
CC -!- FUNCTION: Repair polymerase involved in base excision repair (BER) and
CC responsible for repair of lesions that give rise to abasic (AP) sites
CC in DNA. Has both DNA polymerase and terminal transferase activities.
CC Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity (By
CC similarity). Involved in the repair of transposon-induced DNA double
CC strand breaks (DSBs) (PubMed:21889425). Involved in repair of UV-B-
CC mediated DNA damage during seedling development through an excision
CC repair mechanism (PubMed:21227935). Involved the repair of DSBs induced
CC by high salinity and DNA cross-linking agent. Functions via the DNA
CC non-homologous end joining (NHEJ) pathway.
CC {ECO:0000250|UniProtKB:Q67VC8, ECO:0000269|PubMed:21227935,
CC ECO:0000269|PubMed:21889425}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- SUBUNIT: Interacts with the DNA repair proteins XRCC4 and LIG4
CC (PubMed:23660835). Interacts with HSP90-1 (PubMed:26230318).
CC {ECO:0000269|PubMed:23660835, ECO:0000269|PubMed:26230318}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Induced by UV-B. {ECO:0000269|PubMed:21227935}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ289628; CAC21394.1; -; mRNA.
DR EMBL; HQ009888; ADM33939.1; -; mRNA.
DR EMBL; AC007067; AAD39573.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28588.1; -; Genomic_DNA.
DR EMBL; DQ446242; ABE65612.1; -; mRNA.
DR PIR; G86238; G86238.
DR RefSeq; NP_172522.2; NM_100926.3.
DR AlphaFoldDB; Q9FNY4; -.
DR SMR; Q9FNY4; -.
DR STRING; 3702.AT1G10520.1; -.
DR iPTMnet; Q9FNY4; -.
DR PaxDb; Q9FNY4; -.
DR PRIDE; Q9FNY4; -.
DR ProteomicsDB; 224290; -.
DR EnsemblPlants; AT1G10520.1; AT1G10520.1; AT1G10520.
DR GeneID; 837592; -.
DR Gramene; AT1G10520.1; AT1G10520.1; AT1G10520.
DR KEGG; ath:AT1G10520; -.
DR Araport; AT1G10520; -.
DR TAIR; locus:2194610; AT1G10520.
DR eggNOG; KOG2534; Eukaryota.
DR HOGENOM; CLU_008698_6_2_1; -.
DR InParanoid; Q9FNY4; -.
DR OMA; CMRSAPL; -.
DR OrthoDB; 1328151at2759; -.
DR PhylomeDB; Q9FNY4; -.
DR PRO; PR:Q9FNY4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FNY4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IEP:TAIR.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW DNA-directed DNA polymerase; Lyase; Manganese; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..529
FT /note="DNA polymerase lambda"
FT /id="PRO_0000438212"
FT DOMAIN 14..109
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 119..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..227
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT REGION 295..298
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT REGION 370..379
FT /note="Involved in primer binding"
FT /evidence="ECO:0000250"
FT REGION 418..459
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT COMPBIAS 126..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 260
FT /evidence="ECO:0000305"
FT BINDING 336
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 367..370
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 376..379
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 377
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 444
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 467
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
SQ SEQUENCE 529 AA; 59588 MW; 976083F9906BB618 CRC64;
MAAKRGRNRS PSPDPEGMFA GMVVFMVEIG VQRRRLQIWK QKLVQMGAVI EEDRVTKKVT
HVLAMNLEAL LHKFGKERLS HFTARLMLYQ WLEDSLTSGE KANEDLYVLK IDSEEVDKPK
KSLPAISGSE DQSSPQKRTR YSPDAGDFKG VESHSNTQGS PDSPTSCSVP STSASPGEGI
AETPTSPQSE STSVYKPPDL NRNITEIFGK LINIYRALGE DRRSFSYYKA IPVIEKFPTR
IESVDQLKHL PGIGKAMRDH IQEIVTTGKL SKLEHFETDE KVRTISLFGE VWGVGPATAL
KLYEKGHRTL EDLKNEDSLT HAQKLGLKYF DDIKTRIPRQ EVQEMEQLLQ RVGEETLPGV
NIVCGGSYRR GKATCGDLDI VVTHPDGQSH KGFLTKFVKR LKEMNFLRED LIFSTHSEEG
TDSGVDTYFG LCTYPGQELR RRIDFKVYPR DIYSFGLIAW TGNDVLNRRL RLLAESKGYR
LDDTGLFPAT HSSSGNRGAR GTASLKLSTE KQVFDFLGFP WLEPHERNL
