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Database: UniProt
Entry: A0A166CUE3_9EURY
LinkDB: A0A166CUE3_9EURY
Original site: A0A166CUE3_9EURY 
ID   A0A166CUE3_9EURY        Unreviewed;       646 AA.
AC   A0A166CUE3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=DNA-binding protein MutS2 {ECO:0000256|HAMAP-Rule:MF_00971};
GN   Name=mutS2 {ECO:0000256|HAMAP-Rule:MF_00971,
GN   ECO:0000313|EMBL:KZX16897.1};
GN   ORFNames=MBCUT_04450 {ECO:0000313|EMBL:KZX16897.1};
OS   Methanobrevibacter cuticularis.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX16897.1, ECO:0000313|Proteomes:UP000077275};
RN   [1] {ECO:0000313|EMBL:KZX16897.1, ECO:0000313|Proteomes:UP000077275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX16897.1,
RC   ECO:0000313|Proteomes:UP000077275};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has ATPase and non-specific DNA-binding activities.
CC       {ECO:0000256|HAMAP-Rule:MF_00971}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00971};
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. Archaeal
CC       Muts2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00971}.
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:KZX16897.1}.
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DR   EMBL; LWMW01000084; KZX16897.1; -; Genomic_DNA.
DR   RefSeq; WP_067258378.1; NZ_LWMW01000084.1.
DR   AlphaFoldDB; A0A166CUE3; -.
DR   STRING; 47311.MBCUT_04450; -.
DR   PATRIC; fig|47311.3.peg.516; -.
DR   OrthoDB; 15514at2157; -.
DR   Proteomes; UP000077275; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00971; MutS2_archaea; 1.
DR   InterPro; IPR012401; DNA-bd_MutS2_arc.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010994; RuvA_2-like.
DR   PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR   PANTHER; PTHR11361:SF125; DNA-BINDING PROTEIN MUTS2; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   PIRSF; PIRSF029254; MutS_C_archaeal; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00971};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00971}; Endonuclease {ECO:0000313|EMBL:KZX16897.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00971, ECO:0000313|EMBL:KZX16897.1};
KW   Nuclease {ECO:0000313|EMBL:KZX16897.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00971}; Reference proteome {ECO:0000313|Proteomes:UP000077275}.
FT   DOMAIN          461..644
FT                   /note="DNA mismatch repair proteins mutS family"
FT                   /evidence="ECO:0000259|SMART:SM00534"
FT   BINDING         468..475
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00971"
SQ   SEQUENCE   646 AA;  73643 MW;  FCF80C1D72A00C49 CRC64;
     MNDKRQIKVR QQVDLQEIKG IGDRLSEKIL KAVGGKEKLK KIVQDLDLEK ITSIEGISQR
     KAIEIMNQLL GNPTQKFLKS ERAVQLYEEI IQKMIAYSNT KYAENRILLL SPSKDKLAIE
     KQVMSVMKAK EKVSKLPIIK LRGLMKNLQL PVQVKPKYDP SKAILVETDE DGDYLIDIGL
     NQYYTIINAS SSMIEEEIRG YELVYYVYSE GFLDIGEMSN LIMINKEAPE HEIVPEIILD
     YFNANQGLFK KVGEIRKILN EKTILEDIPP LLEEVNSLKK QDVDLEKVVN SIKETLDKEI
     KESIKNIDLE GDEVLDLLNN SFPPKIEKIF EEIIQKGKIS IKEETGIDFD PFLKKYPLEI
     DEKEIERIKL MESSKKENNI FDKKVTAASQ LASIKSLAEQ EVKETLKFDY EFTLGSFAYE
     YDLMPAKIAN EFKLEGALHL ELGLEKGDHI QRIDYDLSYP QNVALLTGAN SGGKTTLLET
     IGQISIMSQM GLPVCAKNAE VKLLDEIYHF SKKRSLDAGA FESFLNVFMP IVTTDSEKLV
     LLDELEGITE LEAAVKIISS FIEMIKDSNS YAIIVTHMAK ELMDYTDVRV DGIEAKGLDK
     NYNLIVDRTP KMNCLARSTP EFILKRIYEN SDGRLKEVYG EILKKF
//
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