GenomeNet

Database: UniProt
Entry: A0A401UP73_9CLOT
LinkDB: A0A401UP73_9CLOT
Original site: A0A401UP73_9CLOT 
ID   A0A401UP73_9CLOT        Unreviewed;       787 AA.
AC   A0A401UP73;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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   ECO:0000313|EMBL:GCD11330.1};
GN   ORFNames=Ctaglu_29530 {ECO:0000313|EMBL:GCD11330.1};
OS   Clostridium tagluense.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=360422 {ECO:0000313|EMBL:GCD11330.1, ECO:0000313|Proteomes:UP000287872};
RN   [1] {ECO:0000313|EMBL:GCD11330.1, ECO:0000313|Proteomes:UP000287872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A121 {ECO:0000313|EMBL:GCD11330.1,
RC   ECO:0000313|Proteomes:UP000287872};
RA   Murakami T., Segawa T., Shcherbakova V.A., Mori H., Yoshimura Y.;
RT   "Genome sequencing and assembly of Clostridium tagluense strain A121.";
RL   Submitted (NOV-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:GCD11330.1}.
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; BHYK01000017; GCD11330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401UP73; -.
DR   OrthoDB; 9808166at2; -.
DR   Proteomes; UP000287872; 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   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; 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:UP000287872}.
FT   DOMAIN          712..787
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   COILED          501..623
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         331..338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   787 AA;  88079 MW;  9EBFE84161A5BB9A CRC64;
     MNTKSLKVLE YYKIKDKIKE YTHTTAGKDI IEKLEPYTNM YEVREHLQET NEALLLLSKK
     GSAPFEGIYD VRDAISRASK GACLMPTQLL RIAQMLRCAR LFQNYVGSKG GETSRVLEDI
     CIGIVPIKKL EDEIFIAIIG DDEISDRASS LLFNLRKSLK EKNSSVKEKV NSLVRSNAKY
     LQESLYTIRG DRYVIPVKIE HKSSVPGIVH DQSSSGATLF IEPMSLVNLN NEIKEIMLKE
     KAEVERILAE LSYKIYENIN IVDSNANIVW ELDFIFAKAK YAIEINAIIP SVNDEGVIDI
     IEARHPLIDP KVVVPSNIYL GRGFTSLVIT GPNTGGKTVT LKTVGLIQLM AMSGILIPAR
     DGSVVSFFNE IFADIGDEQS IEQSLSTFSS HMTNIVNIIE KADKKTLALF DELGAGTDPT
     EGAALAVSIL ENLRSRGTKV VATTHYSELK GYALKTTGVE NASVEFNVDT LSPTYRLIIG
     VPGKSNAFEI SKRLGLPDYI IKNARENISS ETLEFEELVQ SLQEKSIKAE KDARTAEGLK
     LEASKLKDKY QEKLYKLENI RENAMYEAQR EAKMLVRNAK EESDVILKNM RELEKLGFPS
     EARQMLEEER MKIKDKLESL DKHVQKNNED LGEKLKTVKE GQEVYLPSLD QKVIVISKPD
     SRGEVQVQAG IMKINVKVDD LRKSKVTQEE KKKAKINKRE LKLNLRNVST SVDLRGMDAQ
     EAVYTVDKYL DDAYLGGLKE VTIIHGKGTG VLRNTITDML KRHGHSKAYR LGNYGEGGSG
     VTVVELK
//
DBGET integrated database retrieval system