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DNA polymerase lambda (Pol Lambda) (EC 2.7.7.7) (EC 4.2.99.-)

 DPOLL_ARATH             Reviewed;         529 AA.
Q9FNY4; Q9XIK1;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 119.
RecName: Full=DNA polymerase lambda {ECO:0000305};
Short=Pol Lambda {ECO:0000305};
EC=2.7.7.7 {ECO:0000305};
EC=4.2.99.- {ECO:0000305};
Name=POLL {ECO:0000305};
OrderedLocusNames=At1g10520 {ECO:0000312|Araport:AT1G10520};
ORFNames=T10O24.13 {ECO:0000312|EMBL:AAD39573.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10966791; DOI=10.1006/jmbi.2000.4005;
Garcia-Diaz M., Dominguez O., Lopez-Fernandez L.A., Lain de Lera T.,
Saniger M.L., Ruiz J.F., Parraga M., Garcia M.J., Kirchhoff T.,
del Mazo J., Bernad A., Blanco L.;
"DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase
with a potential role in meiosis.";
J. Mol. Biol. 301:851-867(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Roy S., Roy Choudhury S., Singh S.K., Das K.P.;
"Arabidopsis thaliana DNA pol lambda (Poll) mRNA.";
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading
frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[7]
FUNCTION.
PubMed=21889425; DOI=10.1016/j.dnarep.2011.07.011;
Huefner N.D., Mizuno Y., Weil C.F., Korf I., Britt A.B.;
"Breadth by depth: expanding our understanding of the repair of
transposon-induced DNA double strand breaks via deep-sequencing.";
DNA Repair 10:1023-1033(2011).
[8]
FUNCTION, AND INDUCTION BY UV-B.
PubMed=21227935; DOI=10.1093/pcp/pcr002;
Roy S., Choudhury S.R., Singh S.K., Das K.P.;
"AtPollambda, a homolog of mammalian DNA polymerase lambda in
Arabidopsis thaliana, is involved in the repair of UV-B induced DNA
damage through the dark repair pathway.";
Plant Cell Physiol. 52:448-467(2011).
[9]
FUNCTION, AND INTERACTION WITH XRCC4 AND LIG4.
PubMed=23660835; DOI=10.1104/pp.113.219022;
Roy S., Choudhury S.R., Sengupta D.N., Das K.P.;
"Involvement of AtPollambda in the repair of high salt- and DNA cross-
linking agent-induced double strand breaks in Arabidopsis.";
Plant Physiol. 162:1195-1210(2013).
[10]
INTERACTION WITH HSP90-1.
PubMed=26230318; DOI=10.1371/journal.pone.0133843;
Roy S., Banerjee V., Das K.P.;
"Understanding the physical and molecular basis of stability of
Arabidopsis DNA Pol lambda under UV-B and high NaCl stress.";
PLoS ONE 10:E0133843-E0133843(2015).
-!- FUNCTION: Repair polymerase involved in base excision repair (BER)
and responsible for repair of lesions that give rise to abasic
(AP) sites in DNA. Has both DNA polymerase and terminal
transferase activities. Has a 5'-deoxyribose-5-phosphate lyase
(dRP lyase) activity (By similarity). Involved in the repair of
transposon-induced DNA double strand breaks (DSBs)
(PubMed:21889425). Involved in repair of UV-B-mediated DNA damage
during seedling development through an excision repair mechanism
(PubMed:21227935). Involved the repair of DSBs induced by high
salinity and DNA cross-linking agent. Functions via the DNA non-
homologous end joining (NHEJ) pathway.
{ECO:0000250|UniProtKB:Q67VC8, ECO:0000269|PubMed:21227935,
ECO:0000269|PubMed:21889425}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- SUBUNIT: Interacts with the DNA repair proteins XRCC4 and LIG4
(PubMed:23660835). Interacts with HSP90-1 (PubMed:26230318).
{ECO:0000269|PubMed:23660835, ECO:0000269|PubMed:26230318}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- INDUCTION: Induced by UV-B. {ECO:0000269|PubMed:21227935}.
-!- SIMILARITY: Belongs to the DNA polymerase type-X family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD39573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ289628; CAC21394.1; -; mRNA.
EMBL; HQ009888; ADM33939.1; -; mRNA.
EMBL; AC007067; AAD39573.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28588.1; -; Genomic_DNA.
EMBL; DQ446242; ABE65612.1; -; mRNA.
PIR; G86238; G86238.
RefSeq; NP_172522.2; NM_100926.3.
UniGene; At.10195; -.
ProteinModelPortal; Q9FNY4; -.
SMR; Q9FNY4; -.
STRING; 3702.AT1G10520.1; -.
iPTMnet; Q9FNY4; -.
PaxDb; Q9FNY4; -.
EnsemblPlants; AT1G10520.1; AT1G10520.1; AT1G10520.
GeneID; 837592; -.
Gramene; AT1G10520.1; AT1G10520.1; AT1G10520.
KEGG; ath:AT1G10520; -.
Araport; AT1G10520; -.
TAIR; locus:2194610; AT1G10520.
eggNOG; KOG2534; Eukaryota.
eggNOG; COG1796; LUCA.
HOGENOM; HOG000030669; -.
KO; K03512; -.
OMA; PKRKKIH; -.
OrthoDB; EOG0936076R; -.
PhylomeDB; Q9FNY4; -.
PRO; PR:Q9FNY4; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9FNY4; baseline and differential.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IEA:EnsemblPlants.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0030145; F:manganese ion binding; IEA:EnsemblPlants.
GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IEA:EnsemblPlants.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
GO; GO:0006289; P:nucleotide-excision repair; IMP:TAIR.
GO; GO:0010224; P:response to UV-B; IEP:TAIR.
CDD; cd00141; NT_POLXc; 1.
Gene3D; 1.10.150.110; -; 1.
Gene3D; 3.30.210.10; -; 1.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR002054; DNA-dir_DNA_pol_X.
InterPro; IPR019843; DNA_pol-X_BS.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR028207; DNA_pol_B_palm_palm.
InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
InterPro; IPR037160; DNA_Pol_thumb_sf.
InterPro; IPR022312; DNA_pol_X.
InterPro; IPR002008; DNA_pol_X_beta-like.
InterPro; IPR029398; PolB_thumb.
Pfam; PF14792; DNA_pol_B_palm; 1.
Pfam; PF14791; DNA_pol_B_thumb; 1.
Pfam; PF10391; DNA_pol_lambd_f; 1.
Pfam; PF14716; HHH_8; 1.
PRINTS; PR00869; DNAPOLX.
PRINTS; PR00870; DNAPOLXBETA.
SMART; SM00483; POLXc; 1.
SUPFAM; SSF47802; SSF47802; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS00522; DNA_POLYMERASE_X; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA repair; DNA replication;
DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Lyase;
Manganese; Metal-binding; Nucleotidyltransferase; Nucleus;
Reference proteome; Transferase.
CHAIN 1 529 DNA polymerase lambda.
/FTId=PRO_0000438212.
DOMAIN 14 109 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
NP_BIND 367 370 dCTP binding.
{ECO:0000250|UniProtKB:Q9UGP5}.
NP_BIND 376 379 dCTP binding.
{ECO:0000250|UniProtKB:Q9UGP5}.
REGION 213 227 DNA binding.
{ECO:0000250|UniProtKB:Q9UGP5}.
REGION 295 298 DNA binding.
{ECO:0000250|UniProtKB:Q9UGP5}.
REGION 370 379 Involved in primer binding.
{ECO:0000250}.
REGION 418 459 DNA binding.
{ECO:0000250|UniProtKB:Q9UGP5}.
ACT_SITE 260 260 {ECO:0000305}.
METAL 377 377 Manganese.
{ECO:0000250|UniProtKB:Q9UGP5}.
METAL 379 379 Manganese.
{ECO:0000250|UniProtKB:Q9UGP5}.
METAL 444 444 Manganese.
{ECO:0000250|UniProtKB:Q9UGP5}.
BINDING 336 336 dCTP. {ECO:0000250|UniProtKB:Q9UGP5}.
BINDING 467 467 dCTP. {ECO:0000250|UniProtKB:Q9UGP5}.
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


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