MUTS2_ANADF
ID MUTS2_ANADF Reviewed; 805 AA.
AC A7HAB8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=Anae109_1457;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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; CP000769; ABS25664.1; -; Genomic_DNA.
DR RefSeq; WP_011985770.1; NC_009675.1.
DR AlphaFoldDB; A7HAB8; -.
DR SMR; A7HAB8; -.
DR STRING; 404589.Anae109_1457; -.
DR EnsemblBacteria; ABS25664; ABS25664; Anae109_1457.
DR KEGG; afw:Anae109_1457; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_0_7; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000006382; 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 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 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..805
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093340"
FT DOMAIN 729..804
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT REGION 705..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 805 AA; 84747 MW; F008351F931A98DD CRC64;
MTDRTQRELG WPEILNALAA RCRLPAGRNR ALALPFQPTA EAAREALALV GEARRLSELA
LALPLGGVGD VEGHLERASK GGVLEPLALR ECAALARAAA RTRGLLEARA SETPRLWALA
EPLSPSAALA DRIERAIEPS GAISDRASAE LAQARERSRG LHRALKAQVE TLLADADMQR
HLRDTYFTIR NERYVLPVLA SARRAVPGIV HNASQSGQTL FVEPDSMVEL GNELSIANAV
AAEEEQRILR ELTGALMADS GALARDLGIL AALDVLEGSA LLASDLDAHA PEVLSPFDGL
RVGGAGAGFE LLSLRHPLLV LQGKKVVPSH VRLDAPARAL IVSGPNGGGK TVAITAVGLS
ALMLRAGLPV AAAEGSRLPF FLEVKAAVDE RGDLAKDLST FTAHLAAVKE MLAGAVPGSL
ILVDEIAADT DPREGAALAA AILESLVERG AAVLVTTHLD ELKALALTDP RYANARVGFD
AERLAPTYQL HLGSPGSSSA IEVAARVGLP APLVERARAA LTGHGGALGQ ALRALDDERA
RLAEERRAAE SARDAARKAE ERARAAEEVA RRAQREAAAR MGEALADELE AARAEVAELL
AGLQARPTVK AATDAARQLD AWRATVAQAA KATQARADAG AEALPGGEVR PGVRVRIVSL
GQEGEVVEVD GKDALVRAGP LKVRRPVADL VPLLGKAKDA AKLGRSRSEK LQAASEARPS
APPGLERRLD VRGLRVEELL REVERFLDRL YSDGEADCLI LHGHGTGALK QALRDHLSAS
PYVGAFRAGD RHEGGDAVTV VSLRR