MSH3_KLULA
ID MSH3_KLULA Reviewed; 1029 AA.
AC Q6CSR1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=KLLA0C18590g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA
CC mismatches thereby initiating DNA repair. MSH3 provides substrate-
CC binding and substrate specificity to the complex. When bound, the MutS
CC beta heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC 13 nucleotides in size, but can also repair base-base and single
CC insertion-deletion mismatches that occur during replication. After
CC mismatch binding, forms a ternary complex with the MutL alpha
CC heterodimer, which is thought to be responsible for directing the
CC downstream MMR events, including strand discrimination, excision, and
CC resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC repair functions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382123; CAH01879.1; -; Genomic_DNA.
DR RefSeq; XP_453028.1; XM_453028.1.
DR AlphaFoldDB; Q6CSR1; -.
DR SMR; Q6CSR1; -.
DR STRING; 28985.XP_453028.1; -.
DR EnsemblFungi; CAH01879; CAH01879; KLLA0_C18590g.
DR GeneID; 2892153; -.
DR KEGG; kla:KLLA0_C18590g; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR InParanoid; Q6CSR1; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0032302; C:MutSbeta complex; IEA:EnsemblFungi.
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:0000406; F:double-strand/single-strand DNA junction binding; IEA:EnsemblFungi.
DR GO; GO:0000404; F:heteroduplex DNA loop binding; IEA:EnsemblFungi.
DR GO; GO:0000403; F:Y-form DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000710; P:meiotic mismatch repair; IEA:EnsemblFungi.
DR GO; GO:0006312; P:mitotic recombination; IEA:EnsemblFungi.
DR GO; GO:0000735; P:removal of nonhomologous ends; IEA:EnsemblFungi.
DR GO; GO:0043111; P:replication fork arrest; IEA:EnsemblFungi.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
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; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361; PTHR11361; 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; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1029
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338522"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..270
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 802..809
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1029 AA; 118522 MW; 240FFB8C8B61359E CRC64;
MYQPTISHFF KSSQPSSQTD TRQDEDQRLD IESHEQRGGA NMNKDELINI LGSDSESDQD
LDEDLDQDQN NNQDQDQEQD RDLASKANNG RSTLSAERIE RRPDFNEKLK TIMRKRNAGS
MINTGSDDEN DDNDDVKSTK RTKANNKKLT ELDQQFKELK LKHMDTILCV RVGYKYKFFA
KDAEIVSNIL QIKLVPGKKT LDESDPNDRN YRKFQYCSIP DTRLHVHLQR LVFFNYKVAV
VEQTETSALK KNNNSGSLFT REIKNIFTKV SYGINETFDK SEDRILGDLT SVWAISINET
SKMRKVNLIS VQLNSGEIVH DQFSDDILLN VNLEARIRYL NPTEIITEEE LPPSIRTIFT
KLNQDIQFYQ SHKEACPNLF DALQGLDLNN ELKRLLSVLH SYLSTFENTK VLYFASNYSS
FTAKNFMVLP RNTIESLEIF ENSTTNKTNG SLLWVMDHTR TQFGYRLLRK WISKPLIDLK
SILDRQDAIT CIMKEVHSIF FESFNELLRK SIDLERALNR IAYGSTSRKE VYFFLKQIAT
FASLFKSHHT FIHDQLHKEN SALRKTSCLL FNILQNLDAF FSATDLPLFL QMINVDAALD
KDSHKNVIEF FNLNKYDFPE GLLHKYRDIE EVKTELDDEL QNIKRVLKRP TLSYKDTKDY
LIEVRNTQAK TVPSNWVKVN STKAVSRFRT PKTEELVGKL LYHNDLLNLL AEDEFKRFLQ
RIVDRYAEIK TCINNLATYD CILSLAATSS NVNYVKPKLT ELHQKVKVKN GRNPIIESLD
VNYVPNDVLM SSNSGKINII TGPNMGGKSS YIRQVALLVI MTQIGCYIPA DSAEMSICDR
IFTRIGSHDD LLNAKSTFQV EMSEVLHILN SSTPRSLLLL DEVGRGTGTH DGLSISFAIL
NYFVYLADNC PLVLFITHYS ALCQIDSKLI ANYHMSYIEK HQPGEKWTNV IFLYKLVLGQ
AHNSYGFNVA KLSNIPTEII NRAFEVSEEK ILSSKHHNFL EIMKALKRVN ERKLNKEALK
KIQAFIEDI
