ID A0A364XX55_9BACT Unreviewed; 790 AA.
AC A0A364XX55;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DQQ10_22460 {ECO:0000313|EMBL:RAV98783.1};
OS Pseudochryseolinea flava.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Pseudochryseolinea.
OX NCBI_TaxID=2059302 {ECO:0000313|EMBL:RAV98783.1, ECO:0000313|Proteomes:UP000251889};
RN [1] {ECO:0000313|EMBL:RAV98783.1, ECO:0000313|Proteomes:UP000251889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDU1-6 {ECO:0000313|EMBL:RAV98783.1,
RC ECO:0000313|Proteomes:UP000251889};
RA Li Y., Wang J.;
RT "Chryseolinea flavus sp. nov., a member of the phylum Bacteroidetes
RT isolated from soil.";
RL Submitted (JUN-2018) 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:RAV98783.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QMFY01000015; RAV98783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364XX55; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000251889; 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 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; 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}; 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:UP000251889}.
FT DOMAIN 715..790
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 522..606
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 341..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 790 AA; 89347 MW; E662A362C828E84A CRC64;
MIYPETFEQK LGFDQIRQKL VAYCLSPAGA AWVDKMRFSS EVDFVKILLK QNLEFRQILE
KGEPFPSQHF FDATDWIKKI SLEGNWLEAE EFLHLAYGLE TILACKTFLV KSAELYPELH
KLSQPVTITS QLSQKIFTTI DDKAQVKDSA SADLGKIRKR LRDEQSRLRR LAEQIFRMAV
QESWVPEGAL PTIREGRLVI PIQAEHKRKV KGFILDESAT GQTVFMEPTE MLDANNEIRD
LEHAEKREVI RILRDLTGDF RTQLPVLNAA FQFLAQIDFI RAKAKFSLEI GGDHPVIEKH
PELIWYQAKH PLLFLSLKGK RDVVPLNIEL DQQDRLLLVS GPNAGGKSVT LKTVGLLQYM
LQCGMLIPLS DRSRVGIFKD IFIDIGDQQS IENDLSTYSS HLRNMNAFIQ HAGDRSLVLM
DELGSGTDPN FGGAIAQAIL ESLLKKRVWG VATTHYYNLK LFAGQRQGVK NAAMRFDDKN
LVPLYVLDIG KPGSSFALEI ARKTGLPQSV LMEAEKLVGK DLAGFETLVR SLEKERVQLA
EKIKKMERQE ADLKQSLAKY QTLSSELETK KKEIIGKAKE EAANLLKDTN REIEKTIRHI
RENQAQKTET LRVRKGLENL TKKVNTQQVQ KEKPVQQKEE LKEGDRVKLL GQDSSGVILA
IQGKNATVQF GELKSVTKLD RLEKITGAVA KEMASRLTTS SLNVHEKRST FSNTLDIRGR
RVDEVLSLVD QFMDTAILLG QSELKVLHGK GEGVLRKVVR DHLRRYKEVA SISDEHIERG
GDGITVVVLK
//
