MSH3_CHAGB
ID MSH3_CHAGB Reviewed; 1156 AA.
AC Q2HFD4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
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=CHGG_01070;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ92835.1; -; Genomic_DNA.
DR RefSeq; XP_001220291.1; XM_001220290.1.
DR AlphaFoldDB; Q2HFD4; -.
DR SMR; Q2HFD4; -.
DR STRING; 38033.XP_001220291.1; -.
DR EnsemblFungi; EAQ92835; EAQ92835; CHGG_01070.
DR GeneID; 4386506; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q2HFD4; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000001056; 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; 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; 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..1156
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338517"
FT REGION 22..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..345
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT REGION 1125..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 903..910
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1156 AA; 125976 MW; B3A24C65F0ED88C3 CRC64;
MAGPSRAPVK KQASLTSFFT ANISSKKHAN SPGGGSAANR NKDETEDENT QKIIGKGKEK
DESSPITLSV LESNRKRPLQ DNNSNGNGRS SRAAKRAKSV VSEDDSEEVS SPPVQASTGR
TPIPEPPSSS SRTERYAYDA DRLASDPSGL NEDEDAATRR KKEELHRKFV KKLGHPDSLA
SLRRRELLGQ NESPGLDGEG EEEGGDAEED ETPLPSKTKK KGAKTGKLTP MEIQFLDIKR
KHMDTVLVVE VGYKFRFFGE DARIAAKELS IVCIPGKFRY DEPHIDRFAS ASIPVHRLSV
HVKRLVAAGH KVGVVRQLET AALKKAGDNR NAPFVRKLTN IYTKGTYIDE TGELDQPGEG
AGASAGGYLL CLTESPVKGL GTDENVHIGV MAVQPATGDI IYDDFEDGFM RREIETRLLH
ISPCELLVVG ELSKATNKLV QHLAGSSTNV FGDRSRVERV PKSKTMAAEA SSHVTQFYAG
KVKGDDERSA SLLDKVLKLP ESVTVCLSAM ITHLTEYGLE HIFDLTKYFQ SFTTRQHMLI
NGTTLESLEV YRNATDQSEK GSLLWALDKT RTRPGRRLLR KWIGRPLLDR ERLEERVTAV
EELLEHQSNF KVDRLGGVLN SIKADLERSL IRIYYGKCTR PELLSTLQTL QRISIEFSRV
KTPEDTGFNS SLIVEAIYAL PGIGTIVSAY LDKINPEAAR KDDKYTFFRD DEETEDITNH
KLGIAAVEAD LDVHRKDAAT KLSKKTPVTY VTVSGIEYLI EVPNTDLKHV PASWAKISGT
KKLSRFHTPE VMRLMNERDQ HKEALAAACD NAFTDLLKSI ASEYQPLRDA VASLATLDCL
LSLAQVASLP GYSKPTFLPT ATPPTISITS GRHPIAEHTL PDGYIPFTTS LASPSPLAQL
ITGPNMGGKS SYVRAVALLV LLAQIGSYVP AEAMSLTLTD AIYTRMGARD NLFAGESTFM
VEVSETAAIL RGATARSLVV LDELGRGTST HDGAAIAHAV LAHVARETRC LTLFITHYQN
LARVADGLGG AVRCVHMRFE ATGRQRDEAA DGDADAAAAD ADEEITFLYE VADGVAHRSY
GLNVARLARI PRRVLDVAAR KSREMEEGVK ARRLRGAVRL LEDVVAGGGG GGGGGGGDGD
DGEDPLEHLV SSIEQL
