DPOLQ_MOUSE
ID DPOLQ_MOUSE Reviewed; 2544 AA.
AC Q8CGS6; Q3UTE0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA polymerase theta {ECO:0000312|MGI:MGI:2155399};
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:O75417};
DE AltName: Full=Chromosome aberrations occurring spontaneously protein 1 {ECO:0000303|PubMed:12663541, ECO:0000303|PubMed:15542845};
DE AltName: Full=DNA polymerase eta;
GN Name=Polq {ECO:0000312|MGI:MGI:2155399};
GN Synonyms=Chaos1 {ECO:0000303|PubMed:12663541, ECO:0000303|PubMed:15542845};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN64234.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAN64234.1};
RX PubMed=12663541; DOI=10.1093/genetics/163.3.1031;
RA Shima N., Hartford S.A., Duffy T., Wilson L.A., Schimenti K.J.,
RA Schimenti J.C.;
RT "Phenotype-based identification of mouse chromosome instability mutants.";
RL Genetics 163:1031-1040(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2246-2544.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE24040.1};
RC TISSUE=Egg {ECO:0000312|EMBL:BAE24040.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1932.
RX PubMed=15542845; DOI=10.1128/mcb.24.23.10381-10389.2004;
RA Shima N., Munroe R.J., Schimenti J.C.;
RT "The mouse genomic instability mutation chaos1 is an allele of Polq that
RT exhibits genetic interaction with Atm.";
RL Mol. Cell. Biol. 24:10381-10389(2004).
RN [5]
RP FUNCTION.
RX PubMed=16222339; DOI=10.1038/sj.emboj.7600833;
RA Zan H., Shima N., Xu Z., Al-Qahtani A., Evinger Iii A.J., Zhong Y.,
RA Schimenti J.C., Casali P.;
RT "The translesion DNA polymerase theta plays a dominant role in
RT immunoglobulin gene somatic hypermutation.";
RL EMBO J. 24:3757-3769(2005).
RN [6]
RP FUNCTION.
RX PubMed=16172387; DOI=10.1073/pnas.0505636102;
RA Masuda K., Ouchida R., Takeuchi A., Saito T., Koseki H., Kawamura K.,
RA Tagawa M., Tokuhisa T., Azuma T., O-Wang J.;
RT "DNA polymerase theta contributes to the generation of C/G mutations during
RT somatic hypermutation of Ig genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13986-13991(2005).
RN [7]
RP FUNCTION.
RX PubMed=16890500; DOI=10.1016/j.dnarep.2006.06.006;
RA Masuda K., Ouchida R., Hikida M., Nakayama M., Ohara O., Kurosaki T.,
RA O-Wang J.;
RT "Absence of DNA polymerase theta results in decreased somatic hypermutation
RT frequency and altered mutation patterns in Ig genes.";
RL DNA Repair 5:1384-1391(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17449470; DOI=10.1074/jbc.m611849200;
RA Masuda K., Ouchida R., Hikida M., Kurosaki T., Yokoi M., Masutani C.,
RA Seki M., Wood R.D., Hanaoka F., O-Wang J.;
RT "DNA polymerases eta and theta function in the same genetic pathway to
RT generate mutations at A/T during somatic hypermutation of Ig genes.";
RL J. Biol. Chem. 282:17387-17394(2007).
RN [9]
RP FUNCTION.
RX PubMed=18485835; DOI=10.1016/j.dnarep.2008.04.002;
RA Martomo S.A., Saribasak H., Yokoi M., Hanaoka F., Gearhart P.J.;
RT "Reevaluation of the role of DNA polymerase theta in somatic hypermutation
RT of immunoglobulin genes.";
RL DNA Repair 7:1603-1608(2008).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=19630521; DOI=10.1667/rr1598.1;
RA Goff J.P., Shields D.S., Seki M., Choi S., Epperly M.W., Dixon T., Wang H.,
RA Bakkenist C.J., Dertinger S.D., Torous D.K., Wittschieben J., Wood R.D.,
RA Greenberger J.S.;
RT "Lack of DNA polymerase theta (POLQ) radiosensitizes bone marrow stromal
RT cells in vitro and increases reticulocyte micronuclei after total-body
RT irradiation.";
RL Radiat. Res. 172:165-174(2009).
RN [11]
RP FUNCTION.
RX PubMed=21883722; DOI=10.1111/j.1365-2443.2011.01550.x;
RA Li Y., Gao X., Wang J.Y.;
RT "Comparison of two POLQ mutants reveals that a polymerase-inactive POLQ
RT retains significant function in tolerance to etoposide and gamma-
RT irradiation in mouse B cells.";
RL Genes Cells 16:973-983(2011).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF LYS-120 AND 2494-ASP-GLU-2495.
RX PubMed=25275444; DOI=10.1371/journal.pgen.1004654;
RA Yousefzadeh M.J., Wyatt D.W., Takata K., Mu Y., Hensley S.C., Tomida J.,
RA Bylund G.O., Doublie S., Johansson E., Ramsden D.A., McBride K.M.,
RA Wood R.D.;
RT "Mechanism of suppression of chromosomal instability by DNA polymerase
RT POLQ.";
RL PLoS Genet. 10:E1004654-E1004654(2014).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=25642963; DOI=10.1038/nature14184;
RA Ceccaldi R., Liu J.C., Amunugama R., Hajdu I., Primack B., Petalcorin M.I.,
RA O'Connor K.W., Konstantinopoulos P.A., Elledge S.J., Boulton S.J.,
RA Yusufzai T., D'Andrea A.D.;
RT "Homologous-recombination-deficient tumours are dependent on Poltheta-
RT mediated repair.";
RL Nature 518:258-262(2015).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF 2494-ASP-GLU-2495.
RX PubMed=25642960; DOI=10.1038/nature14157;
RA Mateos-Gomez P.A., Gong F., Nair N., Miller K.M., Lazzerini-Denchi E.,
RA Sfeir A.;
RT "Mammalian polymerase theta promotes alternative NHEJ and suppresses
RT recombination.";
RL Nature 518:254-257(2015).
CC -!- FUNCTION: DNA polymerase that promotes microhomology-mediated end-
CC joining (MMEJ), an alternative non-homologous end-joining (NHEJ)
CC machinery triggered in response to double-strand breaks in DNA. MMEJ is
CC an error-prone repair pathway that produces deletions of sequences from
CC the strand being repaired and promotes genomic rearrangements, such as
CC telomere fusions, some of them leading to cellular transformation
CC (PubMed:25275444, PubMed:25642963). POLQ acts as an inhibitor of
CC homology-recombination repair (HR) pathway by limiting RAD51
CC accumulation at resected ends (PubMed:25642963). POLQ-mediated MMEJ may
CC be required to promote the survival of cells with a compromised HR
CC repair pathway, thereby preventing genomic havoc by resolving
CC unrepaired lesions (PubMed:25642963). The polymerase acts by binding
CC directly the 2 ends of resected double-strand breaks, allowing
CC microhomologous sequences in the overhangs to form base pairs. It then
CC extends each strand from the base-paired region using the opposing
CC overhang as a template. Requires partially resected DNA containing 2 to
CC 6 base pairs of microhomology to perform MMEJ. The polymerase activity
CC is highly promiscuous: unlike most polymerases, promotes extension of
CC ssDNA and partial ssDNA (pssDNA) substrates. Also exhibits low-fidelity
CC DNA synthesis, translesion synthesis and lyase activity, and it is
CC implicated in interstrand-cross-link repair, base excision repair and
CC DNA end-joining (By similarity). Involved in somatic hypermutation of
CC immunoglobulin genes, a process that requires the activity of DNA
CC polymerases to ultimately introduce mutations at both A/T and C/G base
CC pairs (PubMed:16222339, PubMed:16172387, PubMed:16890500,
CC PubMed:17449470). However, POLQ does not play a major role in somatic
CC hypermutation (PubMed:18485835). {ECO:0000250|UniProtKB:O75417,
CC ECO:0000269|PubMed:16172387, ECO:0000269|PubMed:16222339,
CC ECO:0000269|PubMed:16890500, ECO:0000269|PubMed:17449470,
CC ECO:0000269|PubMed:18485835, ECO:0000269|PubMed:21883722,
CC ECO:0000269|PubMed:25275444, ECO:0000269|PubMed:25642963}.
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:0000250|UniProtKB:O75417};
CC -!- SUBUNIT: Homomultimer; forms dimers and multimers. Interacts with
CC RAD51. Interacts with ORC2 and ORC4. {ECO:0000250|UniProtKB:O75417}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O18475}.
CC Chromosome {ECO:0000250|UniProtKB:O75417}. Note=Enriched in chromatin
CC in response to ultaviolet (UV) light. Binds to chromatin during early
CC G1. {ECO:0000250|UniProtKB:O75417}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CGS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGS6-2; Sequence=VSP_057561;
CC -!- DOMAIN: The loop 2 region is involved in the binding of the 2 ends of
CC resected double-strand breaks and homomultimerization.
CC {ECO:0000250|UniProtKB:O75417}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, but show elevated
CC frequencies of spontaneous and radiation-induced micronuclei, due to an
CC increased frequency of chromosomal breakage (PubMed:12663541,
CC PubMed:15542845, PubMed:19630521). Mice display a 20% reduction of both
CC A/T and C/G mutations during somatic hypermutation of immunoglobulin
CC genes (PubMed:17449470). Mice lacking both Polh and Polq do not show a
CC further decrease of A/T mutations as compared with mice lacking only
CC Polh (PubMed:17449470). Mice lacking both Fancd2 and Polq die during
CC embryogenesis (PubMed:25642960). {ECO:0000269|PubMed:12663541,
CC ECO:0000269|PubMed:15542845, ECO:0000269|PubMed:17449470,
CC ECO:0000269|PubMed:19630521, ECO:0000269|PubMed:25642960}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; AY147862; AAN64234.1; -; mRNA.
DR EMBL; AC154763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK139505; BAE24040.1; -; mRNA.
DR CCDS; CCDS28158.1; -. [Q8CGS6-1]
DR CCDS; CCDS49845.1; -. [Q8CGS6-2]
DR RefSeq; NP_001152841.1; NM_001159369.1. [Q8CGS6-2]
DR RefSeq; NP_084253.1; NM_029977.2. [Q8CGS6-1]
DR AlphaFoldDB; Q8CGS6; -.
DR SMR; Q8CGS6; -.
DR STRING; 10090.ENSMUSP00000059757; -.
DR iPTMnet; Q8CGS6; -.
DR PhosphoSitePlus; Q8CGS6; -.
DR MaxQB; Q8CGS6; -.
DR PaxDb; Q8CGS6; -.
DR PRIDE; Q8CGS6; -.
DR ProteomicsDB; 277597; -. [Q8CGS6-1]
DR ProteomicsDB; 277598; -. [Q8CGS6-2]
DR Antibodypedia; 32825; 77 antibodies from 23 providers.
DR DNASU; 77782; -.
DR Ensembl; ENSMUST00000054034; ENSMUSP00000059757; ENSMUSG00000034206. [Q8CGS6-1]
DR Ensembl; ENSMUST00000071452; ENSMUSP00000071396; ENSMUSG00000034206. [Q8CGS6-2]
DR GeneID; 77782; -.
DR KEGG; mmu:77782; -.
DR UCSC; uc007zdo.2; mouse. [Q8CGS6-1]
DR UCSC; uc007zdr.2; mouse.
DR CTD; 10721; -.
DR MGI; MGI:2155399; Polq.
DR VEuPathDB; HostDB:ENSMUSG00000034206; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000158694; -.
DR HOGENOM; CLU_000818_0_1_1; -.
DR OMA; NVSFCAE; -.
DR PhylomeDB; Q8CGS6; -.
DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
DR BioGRID-ORCS; 77782; 22 hits in 108 CRISPR screens.
DR ChiTaRS; Polq; mouse.
DR PRO; PR:Q8CGS6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CGS6; protein.
DR Bgee; ENSMUSG00000034206; Expressed in embryonic post-anal tail and 66 other tissues.
DR ExpressionAtlas; Q8CGS6; baseline and differential.
DR Genevisible; Q8CGS6; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chromosome; Coiled coil;
KW DNA damage; DNA repair; DNA-directed DNA polymerase; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..2544
FT /note="DNA polymerase theta"
FT /id="PRO_0000432702"
FT DOMAIN 101..285
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 320..551
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..890
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000250|UniProtKB:O75417"
FT REGION 896..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2097..2132
FT /note="Loop 1"
FT /evidence="ECO:0000250|UniProtKB:O75417"
FT REGION 2104..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2212..2276
FT /note="Loop 2"
FT /evidence="ECO:0000250|UniProtKB:O75417"
FT REGION 2445..2489
FT /note="Loop 3"
FT /evidence="ECO:0000250|UniProtKB:O75417"
FT MOTIF 215..218
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 924..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 983
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75417"
FT VAR_SEQ 210..488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12663541"
FT /id="VSP_057561"
FT MUTAGEN 120
FT /note="K->M: Abolishes ATP-binding in the helicase domain
FT without affecting the ability to confer resistance to DNA
FT damage."
FT /evidence="ECO:0000269|PubMed:25275444"
FT MUTAGEN 1932
FT /note="S->P: In chaos1; mice display higher frequencies of
FT spontaneous and radiation- or mitomycin C-induced
FT micronucleated erythrocytes."
FT /evidence="ECO:0000269|PubMed:15542845"
FT MUTAGEN 2494..2495
FT /note="DE->AA: Abolishes DNA polymerase activity and
FT ability to confer resistance to DNA damage."
FT /evidence="ECO:0000269|PubMed:25275444,
FT ECO:0000269|PubMed:25642960"
SQ SEQUENCE 2544 AA; 280714 MW; D9E007BEE5033F65 CRC64;
MSLPRRSRKR RRSSSGSDTF SGDGDSFVSP QLRCGPVLSP PPGLGRGRRL TGTGTNKRRV
SDDQIDQLLL ANWGLPKAVL EKYHSFGVRK MFEWQAECLL LGHVLEGKNL VYSAPTSAGK
TLVAELLILK RVLETRKKAL FILPFVSVAK EKKCYLQSLF QEVGLKVDGY MGSTSPTGQF
SSLDIAVCTI ERANGLVNRL IEENKMDLLG MVVVDELHML GDSHRGYLLE LLLTKICYVT
RKSASHQAES ASTLSNAVQI VGMSATLPNL QLVASWLNAE LYHTDFRPVP LLESIKIGNS
IYDSSMKLVR EFQPLLQVKG DEDHIVSLCY ETIQDNHSVL IFCPSKKWCE KVADIIAREF
YNLHHQPEGL VKSSEFPPVI LDQKSLLEVM DQLKRSPSGL DSVLKNTVPW GVAFHHAGLT
FEERDIIEGA FRQGFIRVLA ATSTLSSGVN LPARRVIIRT PIFSGQPLDI LTYKQMVGRA
GRKGVDTMGE SILVCKNSEK SKGIALLQGS LEPVHSCLQR QGEVTASMIR AILEIIVGGV
ASTSQDMQTY AACTFLAAAI QEGKQGMQRN QDDAQLGAID ACVTWLLENE FIQVAEPGDG
TGGKVYHPTH LGSATLSSSL SPTDTLDIFA DLQRAMKGFV LENDLHIVYL VTPVFEDWIS
IDWYRFFCLW EKLPTSMKRV AELVGVEEGF LARCVKGKVV ARTERQHRQM AIHKRFFTSL
VLLDLISEIP LKDINQKYGC NRGQIQSLQQ SAAVYAGMIT VFSNRLGWHN MELLLSQFQK
RLTFGIQREL CDLIRVSLLN AQRARFLYAS GFLTVADLAR ADSAEVEVAL KNSLPFKSAR
KAVDEEEEAA EERRSMRTIW VTGKGLSARE AAALIVEEAK MILQQDLIEM GVRWDPKSPL
SSSTHSRTST SEVKEHTFKS QTKSSHKRLA SMGRNSIRAS GSNDKPSPDA ERGIDDCSEH
ADSLCKFQGN FEPQTPSICT ARKRTSLGIN KEMLRKSLKE GKPSTKEVLQ TFSSEKTRKT
ALSFSSEQVN NTLPSGRDRK YQKKSWGSSP VRDSGMHRGD LQGQTMCTSA LCEDSQKSLE
EQNAEFRSPG LFAKHLPSCA KEKCKKPSLP LQRQQACSRR STESCAAVGH PAAGSSPAAA
RDRRGLAARE TEKGNEALTE NGGESQLQDT YPVSQYLEYH SEKHTNTCTR QKTLTEGQAG
SSYVARDSND AAPIKCERMK LNSKDRDSNP CRQALGSYTG RTEALQSTAK LGQAGGQCEN
LLNSSGVQGK TGAHATNRTE HSHASNPAFC DFGDSLDLDT QSEEIIEQMA TENTMQGAKA
VVIMEEGSAM QNKCHSTPGD QHVPGAANTD HVDSKKVESV KANTEKNINR GAPVSLIFHT
QGENGACFKG NEHSVTDSQL NSFLQGFETQ EIVKPIIPLA PQMRTPTGVE EESLPETSLN
MSDSILFDSF GEDGFGQGQS PDIKANQPLL SEMTPNHFSN PPHPQEDPVM TPTVSEPQGT
QQQGVCLSGE SIIFSDIDSA QVIEALDNMA AFHVQENCNS VALKTLEPSD SAVLGNECPQ
GKLVRGDQNE GSPKPKLTET NQDNSFTWSG ASFNLSPELQ RILDKVSSPR ENEKPKMIHV
NLSSFEGNSK ESHEREEINS DLGTVQRTSV FPSNEVKNRT EGLESKARHG GASSPLPRKE
SAAADDNGLI PPTPVPASAS KVAFPEILGT SVKRQKASSA LQPGESCLFG SPSDNQNQDL
SQELRDSLKD YDGSVADTSF FLQSQDGLLL TQASCSSESL AIIDVASDQI LFQTFVKEWQ
CQKRFSISLA CEKMTSSMSS KTATIGGKLK QVSLPQEATV EDAGFPVRGC DGAVVVGLAV
CWGAKDAYYL SLQKEQKQSE ISPSLAPPPL DATLTVKERM ECLQSCLQKK SDRERSVVTY
DFIQTYKVLL LSCGISLEPS YEDPKVACWL LDPDSKEPTL HSIVTSFLPH ELALLEGMET
GPGIQSLGLN VNTEHSGRYR ASVESVLIFN SMNQLNSLLQ KENLHDIFCK VEMPSQYCLA
LLELNGIGFS TAECESQKHV MQAKLDAIET QAYQLAGHSF SFTSADDIAQ VLFLELKLPP
NGEMKTQGSK KTLGSTRRGN ESGRRMRLGR QFSTSKDILN KLKGLHPLPG LILEWRRISN
AITKVVFPLQ REKHLNPLLR MERIYPVSQS HTATGRITFT EPNIQNVPRD FEIKMPTLVR
ESPPSQAPKG RFPMAIGQDK KVYGLHPGHR TQMEEKASDR GVPFSVSMRH AFVPFPGGLI
LAADYSQLEL RILAHLSRDC RLIQVLNTGA DVFRSIAAEW KMIEPDAVGD DLRQHAKQIC
YGIIYGMGAK SLGEQMGIKE NDAASYIDSF KSRYKGINHF MRDTVKNCRK NGFVETILGR
RRYLPGIKDD NPYHKAHAER QAINTTVQGS AADIVKIATV NIQKQLETFR STFKSHGHRE
SMLQNDRTGL LPKRKLKGMF CPMRGGFFIL QLHDELLYEV AEEDVVQVAQ IVKNEMECAI
KLSVKLKVKV KIGASWGELK DFDV
