ID A0A0J9X637_GEOCN Unreviewed; 958 AA.
AC A0A0J9X637;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Similar to Saccharomyces cerevisiae YOL090W MSH2 Protein that forms heterodimers with Msh3p and Msh6p that bind to DNA mismatches to initiate the mismatch repair process {ECO:0000313|EMBL:CDO52918.1};
GN ORFNames=BN980_GECA04s01550g {ECO:0000313|EMBL:CDO52918.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO52918.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO52918.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO52918.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). {ECO:0000256|RuleBase:RU003756}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000256|ARBA:ARBA00006271, ECO:0000256|RuleBase:RU003756}.
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DR EMBL; CCBN010000004; CDO52918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9X637; -.
DR STRING; 1173061.A0A0J9X637; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd03285; ABC_MSH2_euk; 1.
DR Gene3D; 1.10.1420.10; -; 2.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR011184; DNA_mismatch_repair_Msh2.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR032642; Msh2_ATP-bd.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF35; DNA MISMATCH REPAIR PROTEIN MSH2; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF005813; MSH2; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003756};
KW DNA repair {ECO:0000256|RuleBase:RU003756};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003756};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003756}; Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 741..757
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT COILED 469..496
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 958 AA; 107500 MW; ACB4C9CA853139CB CRC64;
MSSSRPELKF SDKGEEAGFL SFYKSLPSKP ASLIRLFERG DYYSAHGDDA QFIAQSVYRT
TSVIKYLEKP GTPRLPSVTL AQAVFNNFLK DALLNKSLKI EIYGCKMGRN WTLLKKASPG
NLQDVEDLLG NQIDQNPVVL AVKVQSKAEQ KSIGICFIDA SARKIGISEF ADNELFSNFE
SMLIQLGVKE CVLQGSNHSN ENGDSTKTDF DAVKIIELLE RCDIPYTERK SSDFNTRDIE
QDLARLLPKD VVVSALPQLN SQLAMASTAA LIKYLGLMTH PDSFNRFELI QHDLGQYMRL
DSSAMKALNL MPGPRDGVKT MSLFGLLNHC KTVAGTRLLA RWLKQPLMNI DEIETRHLLV
EAFVENSIVC QTLREDQLQV IPDINRLVKK LQRGVASLED VVRLYQMVIR LPDLVESLEN
IIDEKYQPTL TKIYVDKIKE SHLNLEKLQE LVETTVDLQA LDNHEFIIKP DFDDRLREIR
TRLEELKDDI SREHLNSSDD LNMDPEKKLK LENHNIYGWC MRVTRTDGGC LRNKREYIEL
STQKAGIYFT TRNLRSLGQE FTELTSEYNK TQSMLVKEVV GITSTYCPVL EELSMTLAHL
DVIVSFAHVS SYAPTPYVRP KMHPRMTGNT ILKEARHPCL EMQADITFIP NDVSLVRDES
EFLIITGPNM GGKSTYIRQI GVIALMAQIG CFVPCTEAEL TIFDSILARV GAGDSQLKGV
STFMAEMLET ATILKSATKE SLIVIDELGR GTSTYDGFGL AWAISEHIIN EIGCFSMFAT
HFHELTALAD KYPTKVCNLH VVAHVGEIDS KIELDYSHSA APAPVQDITL LYKVERGVSS
QSFGIHVAEV VQFPPKVVRM AKRKALELED FSEPAEVSSD DAASRAKHVK LTTQEIREGS
GLLDRVLKKW ATNVKAEGDF ETLSSTVILQ KLKDVIDASS EKAELESNKF IKSLMAEL
//
