MSH3_SCLS1
ID MSH3_SCLS1 Reviewed; 1130 AA.
AC A7EC69;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=SS1G_02907;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476623; EDO00048.1; -; Genomic_DNA.
DR RefSeq; XP_001596685.1; XM_001596635.1.
DR AlphaFoldDB; A7EC69; -.
DR SMR; A7EC69; -.
DR STRING; 665079.A7EC69; -.
DR PRIDE; A7EC69; -.
DR EnsemblFungi; EDO00048; EDO00048; SS1G_02907.
DR GeneID; 5492336; -.
DR KEGG; ssl:SS1G_02907; -.
DR VEuPathDB; FungiDB:sscle_04g038050; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; A7EC69; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; 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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IEA:EnsemblFungi.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IEA:EnsemblFungi.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; 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..1130
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338530"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..328
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 890..897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1130 AA; 124780 MW; 5D994C80AE60042E CRC64;
MGKPKSTPVK TQKSISSFFT PKSSQKPQNS SPPPASNAPE NLYDAQSDQE TNETAEITGN
SSKRTLEEDA NGGNTGATER PSKRAKNVDV EEEDGEGSSL PAANARKAPS SSMLGKSKPS
TRTNKYMFSG LSQSVAAEPT IEEELEEESE KARKADLHRK FVKKLGHPDS IKRSIPEDDA
ALEGDEDMED EEEAPAPVKT KKKGAKTGKL TPMELQVLDI KRKHMDTLLI VEVGYKFKFF
GEDARTAAKV LSIVCIPGKF RFDEQAHLNY FASASIPVHR LPIHAKRLVA AGHKIGIVRQ
TETAALKKAG DNRNTPFVRK LTNVYTKGTY IDDIEGLDST DAPSGGAPAT GYLLCITETK
AKGWGTDEKV EVGILAVQPA TGDFIYDNFE DGFMRSEIET RLLHIAPCEF LIVGELTKAT
EKLVQHLSGS TTNVFGDRIR VERVEKPKTM AAESYSRVAQ FYADKLKAHQ SSNNAREQEL
LEKVLRLTEP VTICLSAMIT HMTEYGLEHV FDLTKYFQSF SARSHMLLNG NTLTSLEIYT
NQTDHTEKGS LFWTLDKTQT RFGQRLLRKW VGRPLLDKQR LEERVAAVEE LKDNVNTPKV
DKLNATLREV RSDLERSLLR IYYGKCTRPE LLTVLQTMQR IANEFAHVKI PSDAGFDSVL
LNEAVASLPE IGGVVISFLE KINAQAARKD DKYAFFLEEY ETEEIGEHKC GIGAVEQDLE
AHRKEAASKL SKKTPVTYVT IAGIEYLIEV PNSDLKKVPA SWAKISGTKS NSRFHTPEVI
KFLRERDQHK ESLSSACDTA FLAFLAEIST HYALIRDTIS QLATLDCLLS LAAVASLPGY
CKPTFTSTTE ISVVGGRHPM VEQLLPSTYI PNDTSLSTDP DNTRALLITG PNMGGKSSYV
RQVALISILA QIGSHVPAES ARLGLLDGIY TRMGAYDSLF TAQSTFMVEL SETASILKSA
SPRSLVILDE LGRGTSTHDG VAIAEAVLDW VVRETKCLCL FITHYQTLAS VARGFEKGKE
LRNVHMRFTA ERNGKQVSNA NADKDGEDVN EEITFLYEVG EGVAHRSYGL NVARLARVPK
AVLDTAASKS RELEAEVKQK KLLGLSKMIS NVLENDVDQL EQLIIGMEQL
