ID   MUTS2_AQUAE             Reviewed;         762 AA.
AC   O67287;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN   Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; Synonyms=mutSB;
GN   OrderedLocusNames=aq_1242;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Endonuclease that is involved in the suppression of
CC       homologous recombination and may therefore have a key role in the
CC       control of bacterial genetic diversity. {ECO:0000255|HAMAP-
CC       Rule:MF_00092}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
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DR   EMBL; AE000657; AAC07247.1; -; Genomic_DNA.
DR   PIR; D70407; D70407.
DR   RefSeq; NP_213851.1; NC_000918.1.
DR   RefSeq; WP_010880789.1; NC_000918.1.
DR   AlphaFoldDB; O67287; -.
DR   SMR; O67287; -.
DR   STRING; 224324.aq_1242; -.
DR   EnsemblBacteria; AAC07247; AAC07247; aq_1242.
DR   KEGG; aae:aq_1242; -.
DR   PATRIC; fig|224324.8.peg.968; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_0; -.
DR   InParanoid; O67287; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro.
DR   CDD; cd03280; ABC_MutS2; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00092; MutS2; 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR005747; MutS2.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   PANTHER; PTHR11361:SF14; PTHR11361:SF14; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF01713; Smr; 1.
DR   PIRSF; PIRSF005814; MutS_YshD; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF160443; SSF160443; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01069; mutS2; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..762
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115215"
FT   DOMAIN          682..757
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         329..336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   762 AA;  87538 MW;  3A7D977DC2EB01BC CRC64;
     MREKDLIKLE FDKVKEVLAS YAHSPATKEK IQNLKPYTNK EKVKEEIELS KAFFDIAENV
     RLFEFEDIRE LLKKAKLQGA ILGVEDILKI LNVINLTKEI RRVLSSHVQR LEPLRKVYKK
     LYTFSPLENL IIGSIDPRGF VKDEASEELL RVRKSIRAVE EEIKKRLDNL INRPDSAKFL
     SDRIVTIRNG RYVIPVKTSH VKKIFGIVHG TSSSGYTTYV EPQFVIHLNN KLTELKQKEE
     EEVRKVLQRI TEYIGDYAKE LLESFEACVE VDFQQCKYRF SKLVEGSFPD FGEWVELYEA
     RHPVLVLVKE DVVPVGILLK EKKGLILTGP NTGGKTVALK TLGLSVLMFQ SAIPVPASPN
     SKLPLFEKVF TDIGDEQSIE QNLSTFSAHV KNMAEFLPKS DENTLVLIDE LGAGTDPIEG
     SALGIGILEY LKKKKAWVFV TTHHTPIKLY STNSDYYTPA SVLFDRETLK PLYKIAYNTV
     GESMAFYIAQ KYGIPSEVIE IAKRHVGEFG EQYIKAMEKL SDYVKKYEEE FRKLEELRKE
     LQKEKEEVEK LRKEYEEAKR KGWKEAYKEA REYLRKLVQE SEEIFKKAKE KKEIKEFVSK
     KREEIENLAP QKPQKLEVGD LVEFMGKKGK VLEVKGNKAL VLVDHLRMWL DTRELQKVGK
     AEPQKETKVT VQTPVMEKRD TLNLIGKDVE TAVRELEKFI EEAYSAGYKV VKVIHGIGSG
     KLKSAVREAL SKNEKVKFFR DAYPKEGGSG VTVVYLEYGE ET