ID R6DS96_9FIRM Unreviewed; 789 AA.
AC R6DS96;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Endonuclease MutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00092};
GN Name=mutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
GN ORFNames=BN553_02009 {ECO:0000313|EMBL:CDA91348.1};
OS Firmicutes bacterium CAG:238.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263011 {ECO:0000313|EMBL:CDA91348.1, ECO:0000313|Proteomes:UP000018260};
RN [1] {ECO:0000313|EMBL:CDA91348.1, ECO:0000313|Proteomes:UP000018260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:238 {ECO:0000313|Proteomes:UP000018260};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:0000256|HAMAP-
CC Rule:MF_00092}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDA91348.1}.
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DR EMBL; CBCS010000148; CDA91348.1; -; Genomic_DNA.
DR AlphaFoldDB; R6DS96; -.
DR Proteomes; UP000018260; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis 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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR046893; MSSS.
DR InterPro; IPR005747; MutS2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR NCBIfam; TIGR01069; mutS2; 1.
DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48378:SF2; SMR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF20297; MSSS; 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; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF160443; SMR domain-like; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR PROSITE; PS50828; SMR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00092}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00092};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00092}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00092};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00092};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00092}; Reference proteome {ECO:0000313|Proteomes:UP000018260}.
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 520..627
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 332..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 789 AA; 87609 MW; 5347C0E48CBA0BCA CRC64;
MNKKALKVLE YNKIIDMLKA QASSQMAKER LAALLPETEI HRIRDGLEET SEAMQVIVKK
GALPLGEIYD ISNSLHFARK GGTLTMRQLL QVLYNMKVTG NVVPFLKNDI EDIPVIRGMS
DLLVVFRELA DRIDRCILSE DEMADSASAE LKNIRRSIAR QNEAIRSKLN HILNSSDNKS
LLQDAIVTMR DGRYVVPVKA EHRAKVPGII HDQSSSGATL FVEPQAVVNL NNELRELELA
ERAEIERILG ELSSAVAEHF HDLLNNQKIL IELDVIFAKG KLSACMHGEE PQINDEGILD
LKLARHPLID AKKVVPINVS IGKEYRTLVI TGPNTGGKTV TLKTVGLLAM MVQSGLHIPA
AATSSMPIYK NIFADIGDEQ SIEQSLSTFS SHMKNTVYLV EKARMGSLVL LDELGAGTDP
TEGAALAISI LERLAAQGAH TIATTHYNEL KKYAIATPGV ENASMEFDVE TLSPTYRLSI
GVPGKSNAFE ISRKLGLPSE IIDRANDLIE KGDLEFEDVL SAIEEDKKKA REERDEAERL
AYEIKKQREE LDQRQLELEK RESKAIKDAK EEARAIIKEA KQTAAEVQKE LKELSKIQSL
GERIGRLEKS KKRIKESENR YADGLEKQTN ANPIEPDELA VGDRVKILTL DQNGEVLTLP
DDKGDLTVKV GIMKINVNLA DLMLINDGSK KKQKNRGYAN MYRMKAQTIS MSVNVQGQNL
EEALMNVDKY IDDAYMAGLK EVTVIHGNGT GVLKEGLRRS FKKHKLVASY RKGAYNEGGD
GVTIVKLKE
//
