ID E3DR71_HALPG Unreviewed; 791 AA.
AC E3DR71;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Hprae_0823 {ECO:0000313|EMBL:ADO76977.1};
OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO76977.1, ECO:0000313|Proteomes:UP000006866};
RN [1] {ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Halanaerobium praevalens DSM 2228.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO76977.1, ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RX PubMed=21886858;
RA Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the extremely halophilic Halanaerobium
RT praevalens type strain (GSL).";
RL Stand. Genomic Sci. 4:312-321(2011).
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}.
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DR EMBL; CP002175; ADO76977.1; -; Genomic_DNA.
DR RefSeq; WP_014553010.1; NC_017455.1.
DR AlphaFoldDB; E3DR71; -.
DR STRING; 572479.Hprae_0823; -.
DR KEGG; hpk:Hprae_0823; -.
DR PATRIC; fig|572479.3.peg.832; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000006866; Chromosome.
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:SF1; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 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:UP000006866}.
FT DOMAIN 716..791
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 146..180
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 510..638
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 791 AA; 89239 MW; 987CC1668ED2BB42 CRC64;
MKEHSLEVLE YKKIIKMTAQ RAATKIGKEI IQNLEPVNNA EYIKDRLEKV SALKSMIVEF
SNPPFGGARD IREDLKKAAK GSVLSTTAIS RVRNTIRAVF ELKRYLNGIK SNLDPRIIER
EYQKIYDLCS DLQTTPSLAR EIDRCLNEYN EVADEASNKL RSLRAQIESI ENSIRDKLDS
IIKSKKYQDI LQENIVTRRE NRYVVPVKQE KRNSFDGIVH GQSASGLTLF MEPMAVVRLN
NQLREVQAKE NVEIQRILQM LSSKIAQSEN IIKRNLMIIS NLDSLAAAAK FSLDFDCNQP
EVNESGIIEL KKARHPLLGE EPVPIDLKLG NDIATLVITG PNTGGKTVAL KTVGLLTLMT
QTGLHIPAAA NSTISIFNKI FADIGDEQSI EQSLSTFSSH MHRIRKFLAE SDNSTLVLMD
ELGVGTDPEE GAALGISILE KLQEKKATTI ATTHYSQLKS YAYGTEEVEN ASVEFDLDTL
KPTYKLIMGV PGGSNAFEIA LRLGIPEEII DRARSLLSEE EIKVEDIINE LNQERNRYQK
LRHEMEAYRN REKELKEKYE KMIKEQQQKH EEEIQAARKE AEAIVTETKK EAKRIISNLK
GKNYNQRSEV DRAQTSANQD LKELSQVLEA ENEKEEAKIS ASKFEVGDQV RVHSIGRKGE
IINIDQDKKE AKIQAGIMQV TASLADLVKV DIPTENEEKQ LKNYRVQKSQ HVSPKLDLRG
ERYEAAQYKV DKYLDDAFLA GLNEVEIVHG KGTGALRQAV EEVLEKSSHA KDYRLGRQKE
GGMGVTIVKI K
//
