MUTS2_EXIS2
ID MUTS2_EXIS2 Reviewed; 788 AA.
AC B1YJY5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
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}; OrderedLocusNames=Exig_2171;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001022; ACB61623.1; -; Genomic_DNA.
DR RefSeq; WP_012371040.1; NC_010556.1.
DR AlphaFoldDB; B1YJY5; -.
DR SMR; B1YJY5; -.
DR STRING; 262543.Exig_2171; -.
DR EnsemblBacteria; ACB61623; ACB61623; Exig_2171.
DR KEGG; esi:Exig_2171; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000001681; 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: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..788
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093357"
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT REGION 688..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 87208 MW; 75056A8A1618CB7A CRC64;
MNANALRVLE YDKLKELLAK QTASSLGAQF VRKMEPAEDF EQVKALLALT TEATTVYRLR
DRYPFGGLTD VRSEVKRAEI GSVLSTSELL AVADVVYSGR QVKAFQERLH EDHPDLRLPA
LDSRIEQITK LVEIEQGIRH AIDDQGTVQD SASDKLRALR SQLRSLEGQV RSKIDGVLRN
KSKMLSDAIV TMRNDRYCVP VKQEYRQAFG GIVHDQSASG ATLFIEPQAV VAANNEIQEA
RLKERAEIER ILAQLSALVG SVGDSLRINV DVLAELDFIM AKALYGHTIR AVEPRLNENR
HIVLKEARHP FIPDDEVVPI TVSLGGEFTS LVITGPNTGG KTVTLKTIGL LQLMVQSGLY
VPAADETELS VFDAIYADIG DEQSIEQNLS TFSSHMTNIV SMMGKIDFMS LVLFDELGAG
TDPTEGAALA IAILDEVKRR GARVAATTHY SELKAYGYNR EGVVNASMEF DVESLSPTYR
LLIGVPGRSN AFEISKRLGL EDRVIDAARD QVGTDAQSVE TMIGRLEEAK QRAESLEREL
LQEQQRLVEE REEFEREQAE IHQEKNEILA KAEEKATRAV ERAQKEAEAV IKRLKELRDA
GAVKEHELIE ARKQLEQAKP SLQDQRIAKV KAKTNQAPVF AKGEEVKVTT FNQKGYIINQ
NSNGEYTVQV GIMKVNVKPS DLAKVGEVKS ASKTKKRSGG TSITKQSAAS AELDLRGVRV
EEGLAKLDRF MDQALLSNYE QIRVIHGLGT GAMRQGVQEY LRGNRHVKTH RLGGQGEGGH
GVTIIELK