ID K9UCG4_CHAP6 Unreviewed; 843 AA.
AC K9UCG4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, 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=Cha6605_0627 {ECO:0000313|EMBL:AFY91904.1};
OS Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC Chamaesiphon.
OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY91904.1, ECO:0000313|Proteomes:UP000010366};
RN [1] {ECO:0000313|EMBL:AFY91904.1, ECO:0000313|Proteomes:UP000010366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL Submitted (MAY-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}.
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DR EMBL; CP003600; AFY91904.1; -; Genomic_DNA.
DR RefSeq; WP_015158098.1; NC_019697.1.
DR AlphaFoldDB; K9UCG4; -.
DR STRING; 1173020.Cha6605_0627; -.
DR KEGG; cmp:Cha6605_0627; -.
DR PATRIC; fig|1173020.3.peg.736; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_0_1_3; -.
DR Proteomes; UP000010366; 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 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; 2.
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; 2.
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};
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:UP000010366}.
FT DOMAIN 770..843
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 416..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 843 AA; 91776 MW; 5C69BEC806FCC32B CRC64;
MTIQAETLEL LEWSRLCQQV ATFAATKLGT IAARNLVIPQ SPSVSLNLLA QTKEVYDLET
RLTGGLSLDG IEDFGDALER AAVQGMLSGK ELHEIATTLA GMRKLRRTID SEENIPVLQG
LVADVRTYPE LEQDIYHCID DRGDVTDRSS EKLAQVRVQL KGLRDRIYKF LNSLIQRQSN
AIQQPLITQR GDRFVIPVKA SHKDAIPGVV HDSSGSGSTL YVEPQQIINL GNQLRQLQRQ
EQREIEAVLM ALTAKVTEVV EDLEHLLVVA TTIDLATAKA RYSLWLEANP PRFVDRAASE
YITLRQLRHP LLIWKHRHEE GSPVVPIDLS IRPDIRVVTI TGPNTGGKTV TLKTLAIVAL
MAKVGLFIPA REPVEIPWFD LILADIGDEQ SLQQSLSTFS GHIRRIGRIL DAIGEEGGER
GAGSTSTTLS VSGGDEEMGS VRDDEETIDL QVSHSPIHPS TPSSLILLDE VGAGTDPAEG
SALAIALLQY LADRAMLTIA STHYGELKAL KYQDSRFENA SVEFDDVNLA PTYRLLWGIP
GRSNALSIAQ RLGLNPEVIE NAKSQVILGA TQEVNEVIAG LEAQRRTQET KASEAANVLK
QAEAFYLEVS QKAAQLQARE QELKVNQERA VQAAIAEAKG EIAQVIRQLQ QGPQTAQAAQ
QATSELDGVS SRRLPAKSTP KPPVGFNPKV GDRIRIPKIG QKAEVLSEVD DNGNLNVKFG
IMKMNVALAD IESLTGEKAT PPPKKSGAKV PGTAAPAAPP VAIRTSTNTV DVRGQRVMNA
ETEIERAIGR AYQSGIMWVI HGKGTGKLRE GVHEFLSHHP QVLRFELAGE KDGGGGVTIA
YLK
//
