MSH3_BOTFB
ID MSH3_BOTFB Reviewed; 1133 AA.
AC A6RPB6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=BC1G_02289;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN31139.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EDN31139.1; Type=Miscellaneous discrepancy; Note=There seems to be an error in the DNA sequence assembly of the genomic region encompassing this gene.; Evidence={ECO:0000305};
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DR EMBL; CH476848; EDN31139.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001559125.1; XM_001559075.1.
DR AlphaFoldDB; A6RPB6; -.
DR SMR; A6RPB6; -.
DR PRIDE; A6RPB6; -.
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..1133
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338514"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..331
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 893..900
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1133 AA; 125120 MW; 602EB37A6896C790 CRC64;
MGKPNSTPAK TQKSISSFFA PKSSQKPQDS SSPPASKAPG NLDDADSNEG TNEDAKITGN
RLKRVLEEDE NGGNTGAKER PSKRAKSVEV EEEDNESYAL PAADSRKTSS SLTRGKSKPS
LRTNKYMFSG SSQRATESLI EEEPEDELEK ARKVELHKKF VKKLGHPDSL RRIIHEDDAA
LEVGDEEGEE DEEAPAPVKT KKKGAKTGKL TPMELQVIDI KRKHMDTLLI VEVGYKFKFF
GEDARTAAKV LSIVCIPGKF RFDEHPSESH LNYFASASIP VHRLPVHAKR LVAAGYKIGI
VRQTETAALK KAGDNRNAPF VRKLTNVYTK GTYIDDIDGL DTTDAPSGGA PATGYLLCIT
ETKAKGWGTD EKVEVGILAV QPATGDVIYD NFEDGFMRGE LETRLLHIAP CELLIVGELT
KATDKLVQHL SGSSTNVFGD RIRVERVGKS KTMAAESYSR VAQFYADKLK AHQSSNNARE
QELLEKVLKL TEPVTICLSA MITHMTEYGL EHVFDLTKYF QSFSARSHML LNGNTLTSLE
IYTNQTDYTQ KGSLFWTLDK TQTKFGQRLL RKWVGRPLLD KQRLEERVAA VEELKDNANT
PKVDKLNATL REVRSDLERS LLRIYYGKCT RPELLTVLQT MQRIANEFAH VKTPSDAGFE
SIALNEAVAS LPAIGEIVIS FLDKINAQAA RNDDKYAFFL EHYETEAIGD HKCGIGAVEQ
DLEAHRMVAA TKLSKKTPVT YVTIAGIEYL IEVPNTDLKN VPASWAKISG TKKMSRFHTP
EVIKFLRERD QHKESLSSAC DAAFSTFLSE ISTHYALIRD TISHLATLDC LLSLATVASL
PGYCKPTFTS STEISVIGGR HPMVEQLLPS AYIPNDTSLS TSPDHTRALL LTGPNMGGKS
SYVRQVALIS ILAQIGSYVP AESARLGLLD GIYTRMGAYD SLFTAQSTFM VELSETASIL
KSAGPRSLVI LDELGRGTST HDGVAIAEAV LDWVVRETKC LCLFITHYQT LASVARGFEK
GKELRNVHMK FTAERNGRRV SNADADKDNE DFDEEITFLY EVGEGVAHRS YGLNVARLAR
VPKSVLDTAA SKSRELETQV KQKKLLGLSN MISNVLENGT DQLDQLIIGM EQL
