WRN_MOUSE
ID WRN_MOUSE Reviewed; 1401 AA.
AC O09053; O09050; Q80YP9; Q9JKD4; Q9Z241; Q9Z242;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN {ECO:0000305};
DE AltName: Full=Werner syndrome protein homolog {ECO:0000305};
DE Includes:
DE RecName: Full=3'-5' exonuclease;
DE EC=3.1.-.- {ECO:0000269|PubMed:17229737};
DE Includes:
DE RecName: Full=ATP-dependent helicase;
DE EC=3.6.4.12 {ECO:0000269|PubMed:17229737};
GN Name=Wrn;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen, and Testis;
RX PubMed=9143515; DOI=10.1006/geno.1997.4661;
RA Imamura O., Ichikawa K., Yamabe Y., Goto M., Sugawara M., Furuichi Y.;
RT "Cloning of a mouse homologue of the human Werner syndrome gene and
RT assignment to 8A4 by fluorescence in situ hybridization.";
RL Genomics 41:298-300(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Paeper B.W., Gayle M., Brady W., Swartz A., Gillett L.A., Alisch R.S.,
RA Mulligan J., Galas D., Fu Y.-H.;
RT "Genomic structure of the human Werner's gene and cloning of its mouse
RT homolog.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lymph node, and Spleen;
RX PubMed=10757812; DOI=10.1128/mcb.20.9.3286-3291.2000;
RA Lombard D.B., Beard C., Johnson B., Marciniak R.A., Dausman J., Bronson R.,
RA Buhlmann J.E., Lipman R., Curry R., Sharpe A., Jaenisch R., Guarente L.;
RT "Mutations in the WRN Gene in mice accelerate mortality in a p53-null
RT background.";
RL Mol. Cell. Biol. 20:3286-3291(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9618508; DOI=10.1073/pnas.95.12.6887;
RA Marciniak R.A., Lombard D.B., Johnson F.B., Guarente L.;
RT "Nucleolar localization of the Werner syndrome protein in human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6887-6892(1998).
RN [7]
RP INTERACTION WITH WRNIP1.
RX PubMed=11301316; DOI=10.1074/jbc.c100035200;
RA Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F.,
RA Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.;
RT "A novel protein interacts with the Werner's syndrome gene product
RT physically and functionally.";
RL J. Biol. Chem. 276:20364-20369(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-238 IN COMPLEX WITH ZINC IONS
RP AND SULFATE, SUBUNIT, FUNCTION, EXONUCLEASE ACTIVITY, ACTIVITY REGULATION,
RP CIRCULAR DICHROISM, AND MUTAGENESIS OF LYS-185; ARG-190 AND TYR-206.
RX PubMed=17229737; DOI=10.1074/jbc.m609657200;
RA Choi J.M., Kang S.Y., Bae W.J., Jin K.S., Ree M., Cho Y.;
RT "Probing the roles of active site residues in the 3'-5' exonuclease of the
RT Werner syndrome protein.";
RL J. Biol. Chem. 282:9941-9951(2007).
CC -!- FUNCTION: Multifunctional enzyme that has both magnesium and ATP-
CC dependent DNA-helicase activity and 3'->5' exonuclease activity towards
CC double-stranded DNA with a 5'-overhang. Has no nuclease activity
CC towards single-stranded DNA or blunt-ended double-stranded DNA. Binds
CC preferentially to DNA substrates containing alternate secondary
CC structures, such as replication forks and Holliday junctions. May play
CC an important role in the dissociation of joint DNA molecules that can
CC arise as products of homologous recombination, at stalled replication
CC forks or during DNA repair. Alleviates stalling of DNA polymerases at
CC the site of DNA lesions. Important for genomic integrity. Plays a role
CC in the formation of DNA replication focal centers; stably associates
CC with foci elements generating binding sites for RP-A (By similarity).
CC Plays a role in double-strand break repair after gamma-irradiation (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:10757812,
CC ECO:0000269|PubMed:17229737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:17229737};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17229737};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17229737};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17229737};
CC Note=Binds 2 magnesium ions per subunit. Has high activity with
CC manganese and zinc ions (in vitro). {ECO:0000269|PubMed:17229737};
CC -!- ACTIVITY REGULATION: Zinc ions stimulate the exonuclease activity.
CC {ECO:0000269|PubMed:17229737}.
CC -!- SUBUNIT: Monomer, and homooligomer. May exist as homodimer, homotrimer,
CC homotetramer and/or homohexamer. Homotetramer, or homohexamer, when
CC bound to DNA (By similarity). Interacts via its N-terminal domain with
CC WRNIP1 (PubMed:11301316). Interacts with EXO1, PCNA and SUPV3L1.
CC Interacts with PML (isoform PML-4) (By similarity). Interacts (via KBM
CC motif) with XRCC5 and XRCC6; promoting recruitment to DNA damage sites
CC (By similarity). Interacts with RECQL5; this interaction stimulates WRN
CC helicase activity on DNA fork duplexes (By similarity).
CC {ECO:0000250|UniProtKB:Q14191, ECO:0000269|PubMed:11301316}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q14191}. Nucleus {ECO:0000269|PubMed:9618508}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14191}. Chromosome
CC {ECO:0000250|UniProtKB:Q14191}. Note=Gamma-irradiation leads to its
CC translocation from nucleoli to nucleoplasm and PML regulates the
CC irradiation-induced WRN relocation. Localizes to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q14191}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in most organs at a low
CC level, highly expressed in testis, ovary and spleen.
CC {ECO:0000269|PubMed:10757812, ECO:0000269|PubMed:9143515}.
CC -!- DOMAIN: The KBM 2 (Ku-binding motif 2) and XLM (XLF-like motif) mediate
CC cooperative interaction with XRCC5/Ku80 and XRCC6/Ku70 and recruitment
CC to DNA damage sites. {ECO:0000250|UniProtKB:Q14191}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:Q14191}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; D86527; BAA20270.1; -; mRNA.
DR EMBL; D86526; BAA20269.1; -; mRNA.
DR EMBL; AF091215; AAC78077.1; -; mRNA.
DR EMBL; AF091216; AAC72359.1; -; Genomic_DNA.
DR EMBL; AF241636; AAF64490.1; -; mRNA.
DR EMBL; AC153789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050921; AAH50921.1; -; mRNA.
DR EMBL; BC060700; AAH60700.1; -; mRNA.
DR CCDS; CCDS22229.1; -.
DR PIR; T17452; T17452.
DR PIR; T30247; T30247.
DR RefSeq; NP_001116294.1; NM_001122822.1.
DR RefSeq; NP_035851.3; NM_011721.4.
DR RefSeq; XP_006509154.1; XM_006509091.3.
DR RefSeq; XP_017168151.1; XM_017312662.1.
DR PDB; 2E6L; X-ray; 2.20 A; A=31-238.
DR PDB; 2E6M; X-ray; 2.00 A; A=31-238.
DR PDBsum; 2E6L; -.
DR PDBsum; 2E6M; -.
DR AlphaFoldDB; O09053; -.
DR SMR; O09053; -.
DR BioGRID; 204584; 7.
DR DIP; DIP-27642N; -.
DR STRING; 10090.ENSMUSP00000033990; -.
DR iPTMnet; O09053; -.
DR PhosphoSitePlus; O09053; -.
DR EPD; O09053; -.
DR MaxQB; O09053; -.
DR PaxDb; O09053; -.
DR PeptideAtlas; O09053; -.
DR PRIDE; O09053; -.
DR ProteomicsDB; 297858; -.
DR Antibodypedia; 10619; 303 antibodies from 40 providers.
DR DNASU; 22427; -.
DR Ensembl; ENSMUST00000033990; ENSMUSP00000033990; ENSMUSG00000031583.
DR Ensembl; ENSMUST00000033991; ENSMUSP00000033991; ENSMUSG00000031583.
DR GeneID; 22427; -.
DR KEGG; mmu:22427; -.
DR UCSC; uc009ljw.1; mouse.
DR CTD; 7486; -.
DR MGI; MGI:109635; Wrn.
DR VEuPathDB; HostDB:ENSMUSG00000031583; -.
DR eggNOG; KOG0351; Eukaryota.
DR eggNOG; KOG4373; Eukaryota.
DR GeneTree; ENSGT00940000159168; -.
DR HOGENOM; CLU_001103_11_1_1; -.
DR InParanoid; O09053; -.
DR OMA; TSQDFGP; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; O09053; -.
DR TreeFam; TF312852; -.
DR Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 22427; 7 hits in 111 CRISPR screens.
DR ChiTaRS; Wrn; mouse.
DR EvolutionaryTrace; O09053; -.
DR PRO; PR:O09053; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O09053; protein.
DR Bgee; ENSMUSG00000031583; Expressed in embryonic post-anal tail and 225 other tissues.
DR ExpressionAtlas; O09053; baseline and differential.
DR Genevisible; O09053; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0000781; C:chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005657; C:replication fork; IMP:BHF-UCL.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISO:MGI.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:MGI.
DR GO; GO:0070337; F:3'-flap-structured DNA binding; ISO:MGI.
DR GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0000405; F:bubble DNA binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0004527; F:exonuclease activity; ISO:MGI.
DR GO; GO:0061749; F:forked DNA-dependent helicase activity; ISO:MGI.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0009378; F:four-way junction helicase activity; ISO:MGI.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0032405; F:MutLalpha complex binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061821; F:telomeric D-loop binding; ISO:MGI.
DR GO; GO:0000403; F:Y-form DNA binding; ISO:MGI.
DR GO; GO:0006284; P:base-excision repair; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0090398; P:cellular senescence; ISO:MGI.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0006259; P:DNA metabolic process; IMP:MGI.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IMP:BHF-UCL.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISO:MGI.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:BHF-UCL.
DR GO; GO:0010259; P:multicellular organism aging; IGI:MGI.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:MGI.
DR GO; GO:0098530; P:positive regulation of strand invasion; ISO:MGI.
DR GO; GO:1902570; P:protein localization to nucleolus; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0040009; P:regulation of growth rate; IMP:MGI.
DR GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR GO; GO:0090399; P:replicative senescence; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0010225; P:response to UV-C; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029491; Helicase_HTH.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF14493; HTH_40; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding;
KW Exonuclease; Helicase; Hydrolase; Isopeptide bond; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..1401
FT /note="Bifunctional 3'-5' exonuclease/ATP-dependent
FT helicase WRN"
FT /id="PRO_0000205046"
FT DOMAIN 51..223
FT /note="3'-5' exonuclease"
FT DOMAIN 522..688
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 713..866
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1115..1194
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 1..271
FT /note="Interaction with WRNIP1"
FT /evidence="ECO:0000269|PubMed:11301316"
FT REGION 401..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..958
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT REGION 1041..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..18
FT /note="KBM 1"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOTIF 632..635
FT /note="DEAH box"
FT MOTIF 1367..1376
FT /note="KBM 2"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOTIF 1388..1401
FT /note="XLM"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT COMPBIAS 401..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17229737,
FT ECO:0007744|PDB:2E6L"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17229737,
FT ECO:0007744|PDB:2E6L"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17229737,
FT ECO:0007744|PDB:2E6L"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17229737,
FT ECO:0007744|PDB:2E6L"
FT BINDING 535..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 139
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT SITE 1002
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14191"
FT MUTAGEN 185
FT /note="K->A: Loss of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:17229737"
FT MUTAGEN 190
FT /note="R->A: Strongly reduced exonuclease activity."
FT /evidence="ECO:0000269|PubMed:17229737"
FT MUTAGEN 206
FT /note="Y->F: Loss of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:17229737"
FT CONFLICT 101
FT /note="S -> N (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="A -> V (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="S -> L (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="V -> M (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="T -> K (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="R -> C (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="Q -> K (in Ref. 1; BAA20269/BAA20270, 2; AAC72359
FT and 3; AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="K -> Q (in Ref. 1; BAA20270/BAA20269)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="L -> H (in Ref. 2; AAC72359)"
FT /evidence="ECO:0000305"
FT CONFLICT 955..988
FT /note="NSQRLPDKYRGHRLFGAGKEQAESWWKTLSHHLI -> VSVSVIAPGTVSDS
FT AFHCVAMALAFFRWLTSNPC (in Ref. 2; AAC72359)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="S -> L (in Ref. 1; BAA20269/BAA20270 and 3;
FT AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 1145
FT /note="T -> A (in Ref. 1; BAA20270/BAA20269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="L -> V (in Ref. 1; BAA20270/BAA20269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="E -> G (in Ref. 1; BAA20269/BAA20270 and 3;
FT AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="A -> V (in Ref. 1; BAA20269/BAA20270 and 3;
FT AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 1308
FT /note="L -> I (in Ref. 1; BAA20269/BAA20270 and 3;
FT AAF64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 1356
FT /note="A -> V (in Ref. 1; BAA20269/BAA20270 and 3;
FT AAF64490)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2E6M"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2E6M"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2E6M"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:2E6M"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:2E6M"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2E6M"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2E6M"
FT HELIX 201..222
FT /evidence="ECO:0007829|PDB:2E6M"
SQ SEQUENCE 1401 AA; 157204 MW; 66DF2252B17C24C3 CRC64;
METTSLQRKF PEWMSMQSQR CATEEKACVQ KSVLEDNLPF LEFPGSIVYS YEASDCSFLS
EDISMRLSDG DVVGFDMEWP PIYKPGKRSR VAVIQLCVSE SKCYLFHISS MSVFPQGLKM
LLENKSIKKA GVGIEGDQWK LLRDFDVKLE SFVELTDVAN EKLKCAETWS LNGLVKHVLG
KQLLKDKSIR CSNWSNFPLT EDQKLYAATD AYAGLIIYQK LGNLGDTAQV FALNKAEENL
PLEMKKQLNS ISEEMRDLAN RFPVTCRNLE TLQRVPVILK SISENLCSLR KVICGPTNTE
TRLKPGSSFN LLSSEDSAAA GEKEKQIGKH STFAKIKEEP WDPELDSLVK QEEVDVFRNQ
VKQEKGESEN EIEDNLLRED MERTCVIPSI SENELQDLEQ QAKEEKYNDV SHQLSEHLSP
NDDENDSSYI IESDEDLEME MLKSLENLNS DVVEPTHSTW LEMGTNGRLP PEEEDGHGNE
AIKEEQEEED HLLPEPNAKQ INCLKTYFGH SSFKPVQWKV IHSVLEERRD NVVVMATGYG
KSLCFQYPPV YTGKIGIVIS PLISLMEDQV LQLELSNVPA CLLGSAQSKN ILGDVKLGKY
RVIYITPEFC SGNLDLLQQL DSSIGITLIA VDEAHCISEW GHDFRSSFRM LGSLKTALPL
VPVIALSATA SSSIREDIIS CLNLKDPQIT CTGFDRPNLY LEVGRKTGNI LQDLKPFLVR
KASSAWEFEG PTIIYCPSRK MTEQVTAELG KLNLACRTYH AGMKISERKD VHHRFLRDEI
QCVVATVAFG MGINKADIRK VIHYGAPKEM ESYYQEIGRA GRDGLQSSCH LLWAPADFNT
SRNLLIEIHD EKFRLYKLKM MVKMEKYLHS SQCRRRIILS HFEDKCLQKA SLDIMGTEKC
CDNCRPRLNH CLTANNSEDA SQDFGPQAFQ LLSAVDILQE KFGIGIPILF LRGSNSQRLP
DKYRGHRLFG AGKEQAESWW KTLSHHLIAE GFLVEVPKEN KYIKTCSLTK KGRKWLGEAS
SQSPPSLLLQ ANEEMFPRKV LLPSSNPVSP ETTQHSSNQN PAGLTTKQSN LERTHSYKVP
EKVSSGTNIP KKSAVMPSPG TSSSPLEPAI SAQELDARTG LYARLVEARQ KHANKMDVPP
AILATNKVLL DMAKMRPTTV ENMKQIDGVS EGKAALLAPL LEVIKHFCQV TSVQTDLLSS
AKPHKEQEKS QEMEKKDCSL PQSVAVTYTL FQEKKMPLHS IAENRLLPLT AAGMHLAQAV
KAGYPLDMER AGLTPETWKI IMDVIRNPPI NSDMYKVKLI RMLVPENLDT YLIHMAIEIL
QSGSDSRTQP PCDSSRKRRF PSSAESCESC KESKEAVTET KASSSESKRK LPEWFAKGNV
PSADTGSSSS MAKTKKKGLF S
