GEN_HUMAN
ID GEN_HUMAN Reviewed; 908 AA.
AC Q17RS7; Q17RS9; Q6ZN37;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Flap endonuclease GEN homolog 1;
DE EC=3.1.-.-;
GN Name=GEN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-92; ASN-310;
RP ILE-680 AND CYS-898.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-92; ASN-310 AND
RP ILE-680.
RC 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=19020614; DOI=10.1038/nature07470;
RA Ip S.C., Rass U., Blanco M.G., Flynn H.R., Skehel J.M., West S.C.;
RT "Identification of Holliday junction resolvases from humans and yeast.";
RL Nature 456:357-361(2008).
RN [5]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF 134-GLU--GLU-136, AND DNA-BINDING.
RX PubMed=26578604; DOI=10.1093/nar/gkv1207;
RA Chan Y.W., West S.;
RT "GEN1 promotes Holliday junction resolution by a coordinated nick and
RT counter-nick mechanism.";
RL Nucleic Acids Res. 43:10882-10892(2015).
RN [6]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=28049850; DOI=10.1073/pnas.1619790114;
RA Shah Punatar R., Martin M.J., Wyatt H.D., Chan Y.W., West S.C.;
RT "Resolution of single and double Holliday junction recombination
RT intermediates by GEN1.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:443-450(2017).
RN [7] {ECO:0007744|PDB:5T9J}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-505 OF MUTATED AT ASP-30 IN
RP COMPLEX WITH DNA AND MAGNESIUM, COFACTOR, DOMAIN, MUTAGENESIS OF ASP-30;
RP CYS-36; ARG-54; ARG-89; ARG-93; HIS-109; PHE-110; THR-380; LYS-404; ARG-406
RP AND THR-438, FUNCTION, SUBUNIT, AND DNA-BINDING.
RX PubMed=26682650; DOI=10.7554/elife.12256;
RA Lee S.H., Princz L.N., Klugel M.F., Habermann B., Pfander B.,
RA Biertumpfel C.;
RT "Human Holliday junction resolvase GEN1 uses a chromodomain for efficient
RT DNA recognition and cleavage.";
RL Elife 4:0-0(2015).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-275.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [9]
RP VARIANT ARG-766.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Endonuclease which resolves Holliday junctions (HJs) by the
CC introduction of symmetrically related cuts across the junction point,
CC to produce nicked duplex products in which the nicks can be readily
CC ligated. Four-way DNA intermediates, also known as Holliday junctions,
CC are formed during homologous recombination and DNA repair, and their
CC resolution is necessary for proper chromosome segregation
CC (PubMed:19020614, PubMed:26682650). Cleaves HJs by a nick and counter-
CC nick mechanism involving dual coordinated incisions that lead to the
CC formation of ligatable nicked duplex products. Cleavage of the first
CC strand is rate limiting, while second strand cleavage is rapid. Largely
CC monomeric, dimerizes on the HJ and the first nick occurs upon
CC dimerization at the junction (PubMed:26578604). Efficiently cleaves
CC both single and double HJs contained within large recombination
CC intermediates. Exhibits a weak sequence preference for incision between
CC two G residues that reside in a T-rich region of DNA (PubMed:28049850).
CC Has also endonuclease activity on 5'-flap and replication fork (RF) DNA
CC substrates (PubMed:26578604). {ECO:0000269|PubMed:19020614,
CC ECO:0000269|PubMed:26578604, ECO:0000269|PubMed:26682650,
CC ECO:0000269|PubMed:28049850}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:26682650};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000305|PubMed:26682650};
CC -!- SUBUNIT: Largely monomeric, dimerizes on the Holliday junction and the
CC first nick occurs upon dimerization at the junction.
CC {ECO:0000269|PubMed:26578604, ECO:0000269|PubMed:26682650}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:26578604,
CC ECO:0000305|PubMed:28049850}.
CC -!- DOMAIN: XPG-N, XPG-I,5'-3' exonuclease domains interact with DNA.
CC Contains a chromodomain that acts as additional DNA interaction site
CC and is required for efficient DNA recognition and cleavage.
CC {ECO:0000269|PubMed:26682650}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
CC {ECO:0000305}.
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DR EMBL; AK131387; BAD18538.1; -; mRNA.
DR EMBL; AC093731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117204; AAI17205.1; -; mRNA.
DR EMBL; BC117206; AAI17207.1; -; mRNA.
DR CCDS; CCDS1691.1; -.
DR RefSeq; NP_001123481.2; NM_001130009.2.
DR RefSeq; NP_872431.4; NM_182625.4.
DR RefSeq; XP_005262670.1; XM_005262613.4.
DR RefSeq; XP_006712068.1; XM_006712005.3.
DR RefSeq; XP_011531122.1; XM_011532820.2.
DR RefSeq; XP_011531123.1; XM_011532821.2.
DR RefSeq; XP_011531124.1; XM_011532822.2.
DR PDB; 5T9J; X-ray; 3.00 A; A/B=1-505.
DR PDBsum; 5T9J; -.
DR AlphaFoldDB; Q17RS7; -.
DR SMR; Q17RS7; -.
DR BioGRID; 131526; 26.
DR IntAct; Q17RS7; 4.
DR MINT; Q17RS7; -.
DR STRING; 9606.ENSP00000318977; -.
DR iPTMnet; Q17RS7; -.
DR PhosphoSitePlus; Q17RS7; -.
DR BioMuta; GEN1; -.
DR DMDM; 290457644; -.
DR EPD; Q17RS7; -.
DR jPOST; Q17RS7; -.
DR MassIVE; Q17RS7; -.
DR MaxQB; Q17RS7; -.
DR PaxDb; Q17RS7; -.
DR PeptideAtlas; Q17RS7; -.
DR PRIDE; Q17RS7; -.
DR ProteomicsDB; 61166; -.
DR Antibodypedia; 56005; 102 antibodies from 21 providers.
DR DNASU; 348654; -.
DR Ensembl; ENST00000317402.11; ENSP00000318977.7; ENSG00000178295.15.
DR Ensembl; ENST00000381254.7; ENSP00000370653.2; ENSG00000178295.15.
DR GeneID; 348654; -.
DR KEGG; hsa:348654; -.
DR MANE-Select; ENST00000381254.7; ENSP00000370653.2; NM_001130009.3; NP_001123481.3.
DR UCSC; uc002rct.3; human.
DR CTD; 348654; -.
DR DisGeNET; 348654; -.
DR GeneCards; GEN1; -.
DR HGNC; HGNC:26881; GEN1.
DR HPA; ENSG00000178295; Low tissue specificity.
DR MIM; 612449; gene.
DR neXtProt; NX_Q17RS7; -.
DR OpenTargets; ENSG00000178295; -.
DR PharmGKB; PA162389359; -.
DR VEuPathDB; HostDB:ENSG00000178295; -.
DR eggNOG; KOG2519; Eukaryota.
DR GeneTree; ENSGT00940000159266; -.
DR HOGENOM; CLU_013777_0_0_1; -.
DR InParanoid; Q17RS7; -.
DR OMA; CKSDRYC; -.
DR OrthoDB; 1094524at2759; -.
DR PhylomeDB; Q17RS7; -.
DR TreeFam; TF323403; -.
DR BRENDA; 3.1.21.10; 2681.
DR PathwayCommons; Q17RS7; -.
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR SignaLink; Q17RS7; -.
DR BioGRID-ORCS; 348654; 55 hits in 1084 CRISPR screens.
DR ChiTaRS; GEN1; human.
DR GenomeRNAi; 348654; -.
DR Pharos; Q17RS7; Tbio.
DR PRO; PR:Q17RS7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q17RS7; protein.
DR Bgee; ENSG00000178295; Expressed in bone marrow cell and 157 other tissues.
DR ExpressionAtlas; Q17RS7; baseline and differential.
DR Genevisible; Q17RS7; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR GO; GO:0071140; P:resolution of mitotic recombination intermediates; IMP:UniProtKB.
DR GO; GO:0071139; P:resolution of recombination intermediates; IMP:UniProtKB.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR041012; GEN_chromo.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR Pfam; PF18704; Chromo_2; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..908
FT /note="Flap endonuclease GEN homolog 1"
FT /id="PRO_0000314146"
FT REGION 2..96
FT /note="XPG-N domain"
FT /evidence="ECO:0000269|PubMed:26682650"
FT REGION 122..208
FT /note="XPG-I domain"
FT /evidence="ECO:0000269|PubMed:26682650"
FT REGION 208..384
FT /note="5'-3' exonuclease domain"
FT /evidence="ECO:0000269|PubMed:26682650"
FT REGION 390..464
FT /note="Chromodomain"
FT /evidence="ECO:0000269|PubMed:26682650"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26682650,
FT ECO:0007744|PDB:5T9J"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26682650,
FT ECO:0007744|PDB:5T9J"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI4"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI4"
FT VARIANT 92
FT /note="S -> T (in dbSNP:rs1812152)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037844"
FT VARIANT 143
FT /note="N -> S (in dbSNP:rs16981869)"
FT /id="VAR_037845"
FT VARIANT 203
FT /note="I -> V (in dbSNP:rs10177628)"
FT /id="VAR_037846"
FT VARIANT 275
FT /note="R -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037847"
FT VARIANT 310
FT /note="S -> N (in dbSNP:rs300175)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037848"
FT VARIANT 680
FT /note="T -> I (in dbSNP:rs300169)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037849"
FT VARIANT 766
FT /note="C -> R (found in a renal cell carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064715"
FT VARIANT 898
FT /note="R -> C (in dbSNP:rs17315702)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037850"
FT MUTAGEN 30
FT /note="D->N: Abolishes endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 36
FT /note="C->E: Abolishes endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 54
FT /note="R->E: Reduces by 50% endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 89
FT /note="R->E: No effect on endonuclease activity on Hollyday
FT junctions. Slightly reduces endonuclease activity on 5'
FT flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 93
FT /note="R->E: No effect on endonuclease activity on Hollyday
FT junctions. Slightly reduces endonuclease activity on 5'
FT flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 109
FT /note="H->E: Strongly reduces endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 110
FT /note="F->E: Reduces by 25% endonuclease activity on
FT Hollyday junctions and by 65% on 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 134..136
FT /note="EAE->AAA: Abolishes endonuclease activity."
FT /evidence="ECO:0000269|PubMed:26578604"
FT MUTAGEN 380
FT /note="T->E: No effect on endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 404
FT /note="K->E: No effect on endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 406
FT /note="R->E: No effect on endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 438
FT /note="T->E: No effect on endonuclease activity on both
FT Hollyday junctions and 5' flap substrates."
FT /evidence="ECO:0000269|PubMed:26682650"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:5T9J"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 101..124
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5T9J"
FT TURN 158..162
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 368..389
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:5T9J"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:5T9J"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:5T9J"
FT HELIX 450..466
FT /evidence="ECO:0007829|PDB:5T9J"
SQ SEQUENCE 908 AA; 102884 MW; 3C9DB87DDBD0C58F CRC64;
MGVNDLWQIL EPVKQHIPLR NLGGKTIAVD LSLWVCEAQT VKKMMGSVMK PHLRNLFFRI
SYLTQMDVKL VFVMEGEPPK LKADVISKRN QSRYGSSGKS WSQKTGRSHF KSVLRECLHM
LECLGIPWVQ AAGEAEAMCA YLNAGGHVDG CLTNDGDTFL YGAQTVYRNF TMNTKDPHVD
CYTMSSIKSK LGLDRDALVG LAILLGCDYL PKGVPGVGKE QALKLIQILK GQSLLQRFNR
WNETSCNSSP QLLVTKKLAH CSVCSHPGSP KDHERNGCRL CKSDKYCEPH DYEYCCPCEW
HRTEHDRQLS EVENNIKKKA CCCEGFPFHE VIQEFLLNKD KLVKVIRYQR PDLLLFQRFT
LEKMEWPNHY ACEKLLVLLT HYDMIERKLG SRNSNQLQPI RIVKTRIRNG VHCFEIEWEK
PEHYAMEDKQ HGEFALLTIE EESLFEAAYP EIVAVYQKQK LEIKGKKQKR IKPKENNLPE
PDEVMSFQSH MTLKPTCEIF HKQNSKLNSG ISPDPTLPQE SISASLNSLL LPKNTPCLNA
QEQFMSSLRP LAIQQIKAVS KSLISESSQP NTSSHNISVI ADLHLSTIDW EGTSFSNSPA
IQRNTFSHDL KSEVESELSA IPDGFENIPE QLSCESERYT ANIKKVLDED SDGISPEEHL
LSGITDLCLQ DLPLKERIFT KLSYPQDNLQ PDVNLKTLSI LSVKESCIAN SGSDCTSHLS
KDLPGIPLQN ESRDSKILKG DQLLQEDYKV NTSVPYSVSN TVVKTCNVRP PNTALDHSRK
VDMQTTRKIL MKKSVCLDRH SSDEQSAPVF GKAKYTTQRM KHSSQKHNSS HFKESGHNKL
SSPKIHIKET EQCVRSYETA ENEESCFPDS TKSSLSSLQC HKKENNSGTC LDSPLPLRQR
LKLRFQST
