MSH3_YEAS7
ID MSH3_YEAS7 Reviewed; 1018 AA.
AC A6ZTR3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=Mismatch-binding protein;
DE Short=MBP;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; ORFNames=SCY_0656;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 either the MutL alpha or
CC MutL beta heterodimer, which is thought to be responsible for directing
CC the downstream MMR events, including strand discrimination, excision,
CC and resynthesis. MutS beta also has a role in regulation of
CC heteroduplex formation during mitotic and meiotic recombination. MutS
CC beta binds to DNA flap structures predicted to form during
CC recombination, and is required for 3' non-homologous tail removal
CC (NHTR). MutS beta-binding alters the DNA conformation of its substrate
CC at the ds/ssDNA junction and may facilitate its recognition and/or
CC cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10
CC endonuclease. ATP binding and hydrolysis play a pivotal role in MMR and
CC NHTR (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with either MutL alpha (MLH1-PMS1) or MutL beta (MLH1-
CC MLH3). MutS beta interacts with proliferating cell nuclear antigen
CC (PCNA/POL30) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The PIP box serves as a PCNA(POL30)-recognition and -binding
CC motif. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN62202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFW02000089; EDN62202.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6ZTR3; -.
DR SMR; A6ZTR3; -.
DR PRIDE; A6ZTR3; -.
DR EnsemblFungi; EDN62202; EDN62202; SCY_0656.
DR HOGENOM; CLU_002472_0_0_1; -.
DR Proteomes; UP000007060; 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 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.
FT CHAIN 1..1018
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338534"
FT REGION 21..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..256
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT MOTIF 4..11
FT /note="PIP box"
FT COMPBIAS 44..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 791..798
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1018 AA; 116534 MW; 1AD91C2E2F2856EF CRC64;
MAGQPTISRF FKKAVKSELT HKQEQEVAVG NGAGSESICL DTDEEDNLSS VASTTVTNDS
FPLKGSVSSK NSKNSEKTSG TSTTFNDIDF AKKLDRIMKR RSDENVEAED DEEEGEEDFV
KKKARKSPTA KLTPLDKQVK DLKMHHRDKV LVIRVGYKYK CFAEDAVTVS RILHIKLVPG
KLTIDESNPQ DCNHRQFAYC SFPDVRLNVH LERLVHHNLK VAVVEQAETS AIKKHDPGAS
KSSVFERKIS NVFTKATFGV NSTFVLRGKR ILGDTNSIWA LSRDVHQGKV AKYSLISVNL
NNGEVVYDEF EEPNLADEKL QIRIKYLQPI EVLVNTDDLP LHVAKFFKDI SCPLIHKQEY
DLEDHVVQAI KVMNEKIQLS PSLIRLVSKL YSHMVEYNNE QVMLIPSIYS PFASKIHMLL
DPNSLQSLDI FTHDGGKGSL FWLLDHTRTS FGLRMLREWI LKPLVDVHQI EERLDAIECI
TSEINNSIFF ESLNQMLNHT PDLLRTLNRI MYGTTSRKEV YFYLKQITSF VDHFKMHQSY
LSEHFKSSDG RIGKQSPLLF RLFSELNELL STTQLPHFLT MINVSAVMEK NSDKQVMDFF
NLNNYDCSEG IIKIQRESES VRSQLKEELA EIRKYLKRPY LNFRDEVDYL IEVKNSQIKD
LPDDWIKVNN TKMVSRFTTP RTQKLTQKLE YYKDLLIRES ELQYKEFLNK ITAEYTELRK
ITLNLAQYDC ILSLAATSCN VNYVRPTFVN GQQAIIAKNA RNPIIESLDV HYVPNDIMMS
PENGKINIIT GPNMGGKSSY IRQVALLTIM AQIGSFVPAE EIRLSIFENV LTRIGAHDDI
INGDSTFKVE MLDILHILKN CNKRSLLLLD EVGRGTGTHD GIAISYALIK YFSELSDCPL
ILFTTHFPML GEIKSPLIRN YHMDYVEEQK TGEDWMSVIF LYKLKKGLTY NSYGMNVAKL
ARLDKDIINR AFSISEELRK ESINEDALKL FSSLKRILKS DNITATDKLA KLLSLDIH
