MSH3_DEBHA
ID MSH3_DEBHA Reviewed; 1028 AA.
AC Q6BW83; B5RT01;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=DEHA2B13574g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAR65491.1; -; Genomic_DNA.
DR RefSeq; XP_002770122.1; XM_002770076.1.
DR AlphaFoldDB; Q6BW83; -.
DR SMR; Q6BW83; -.
DR STRING; 4959.XP_002770122.1; -.
DR PRIDE; Q6BW83; -.
DR EnsemblFungi; CAR65491; CAR65491; DEHA2B13574g.
DR GeneID; 8998252; -.
DR KEGG; dha:DEHA2B13574g; -.
DR VEuPathDB; FungiDB:DEHA2B13574g; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q6BW83; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000000599; Chromosome B.
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 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..1028
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338520"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..232
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 798..805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1028 AA; 117540 MW; BFB85E69F4E3DDA7 CRC64;
MAPETKGQRS ISHFFKSQSS SQKLNKDDTE YSGNIIDLTN GDEKVSSRLA NFEHKPNKSS
KSPNELDTSK RKSSKDNEHV DGDPEPVKKK PRTSQSLSRS KSKPQSVGSN SKKLTPLEKQ
FVEMKQSNLD KILAIQVGYK FKFFGEDAVI ASKILSIMLI PGNIKLDEYQ HDRFAYCSIP
DNRLHIHLKR LLNQGLKVGV AKQTETAAIK SIDSTNKSGL FEREITGVYT KATYMGDELL
TGDPNINRTS ITDDEMGDYI FCIDESHSKD IGMIAIQPIT GDIIYDTFND NVTRDELETR
LVYLNPSEIL VINNSTEISK ETIKMINIVN NKVNIIHRPR RQQTDYTNEI YNFFNTIDEG
KYKDLGEHYL LKFPNNIQSC MIELIKYLEE FKLSNIFTII SNVSCFSNSK TCLVLPSSTV
QALEIFQNMT DPNSNKGSLI WLLNHTRTRM GNRLLVKWIS KPLIDKAQIE ERLQGIEDLT
FKFNHFIDSL KNQLDKIGKA SIDLEKNLIK VHYSSTYQLD KISRKEVYLL LKCFDDILSM
IKQFGKPTNN ILESIHSPLL LRIFDELMQL AKEDTVRCLL DMISADALDD SNLNDQKIKF
FNLNYFKDQQ IISQLSEISN VESLLNDELI EIRKMLKRPQ LNYITSSKET YLVEVRNGKM
VDSLPKDWIK INGTKTVSRF RSPEITRLHK QLQYHNDMLI RNCDKAFNAY LFKIDNNYEF
FSKIIRNLST FDCLLSLSAV SSINSNYARP KIVEDKQIIQ MKNSRNPIIE NLSVNYSNYI
SNDINISYDE DRVLIITGPN MGGKSTYVKQ VALLVIMAQI GSYIPCDEAT VGIFDSIFIR
MGARDNILQN QSTFMIEMLE CSHILKNMTS NSLIILDEIG RGTGTNDGIA IAYSILNYLI
EEPRKPLTLF ITHFPSLHVL EDKFKGIATN YHMGFHEVSK SNQEFPEVVF LYNLVRGVVG
NSYGLNVAKL AGIPNSIINN AYTKSTEIRD AIESDWPKKL IKMIKSLREQ NDARVELLEI
EQLCNNID
