ID E2ZE60_9FIRM Unreviewed; 787 AA.
AC E2ZE60;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=HMPREF9429_01762 {ECO:0000313|EMBL:EFQ03440.1};
OS Megasphaera micronuciformis F0359.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ03440.1, ECO:0000313|Proteomes:UP000003195};
RN [1] {ECO:0000313|EMBL:EFQ03440.1, ECO:0000313|Proteomes:UP000003195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0359 {ECO:0000313|EMBL:EFQ03440.1,
RC ECO:0000313|Proteomes:UP000003195};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ03440.1}.
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DR EMBL; AECS01000043; EFQ03440.1; -; Genomic_DNA.
DR RefSeq; WP_006943169.1; NZ_GL538212.1.
DR AlphaFoldDB; E2ZE60; -.
DR STRING; 706434.HMPREF9429_01762; -.
DR GeneID; 78569617; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000003195; 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 CDD; cd06503; ATP-synt_Fo_b; 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; 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:UP000003195}.
FT DOMAIN 713..787
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 144..171
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 521..602
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 787 AA; 87912 MW; 3C3989155CE01BF8 CRC64;
MNKRSMRILG FSQIRDMLVR LAPSRLSKEA ARALKPDTDE DTVVKSLTDT EEAVVCLEKE
GQIPLGGITD IRPFLEKAKR EVTLSADECI AVWENAQRYG QIQDFFAPKE AEYPQLSQRA
ETLGDFSLLV QRVGAVFDEN HQVRDNASVE LARLRTRIAE LERRTKRYIQ QILADKSYQK
YFQDTLVTVR NNRSVIPVKQ EYRHAFPGIV HDMSASGATL YVEPLAVVDA NNDLQTAKLA
EEKEIERIYR RLTALIAGQY EDLYKSTMTT GELEFALTKG RLALQMKATR PQLTSERIIK
LYDARHPLIK ADKVVANTII LGGDYSILLI TGSNTGGKTV SMKTLGLLVL MYQSGLFIPV
SDGSQLPLFG DVFADIGDEQ DIAQNLSTFS SHMKQIVYIL KHASACDLIL TDELGSGTDP
GEGGALAIAI LDEFRRKGSL AMVTTHYNDL KNYAYRTEGV ENGHVEFDTE TLRPTYKLRI
GSAGSSHALA ISERLGMPEA VLEEAHRLRN EAQDADVEAV LTRLNTQLRK IDEERELLAT
RLKEAKAHEE ALRKEKEKVT AKRQDIVDAS RREANELKRK LRLEAEQIIR ELKRQSSDAL
DREKAKAIDQ ARRAIQQISV PELSGPKRDP VDVKRLKQGQ SVFVNSLNSI GTVDDIRGKK
LTVSVRGMTI RVDVSDISAP YADELSRQKV AEKRENTSST YRPARTGQVA TELNVIGKRG
NEAIPDISRF LDQALAAGFS PVRIIHGKGS GALRKQVHEY LDTLPFVTSY TLDDARNGGD
GVTLVYF
//
