ID   MSH3_AJECN              Reviewed;        1166 AA.
AC   A6R7S1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; ORFNames=HCAG_06362;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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=EDN09195.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476660; EDN09195.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001538757.1; XM_001538707.1.
DR   AlphaFoldDB; A6R7S1; -.
DR   SMR; A6R7S1; -.
DR   STRING; 339724.A6R7S1; -.
DR   EnsemblFungi; EDN09195; EDN09195; HCAG_06362.
DR   GeneID; 5445353; -.
DR   KEGG; aje:HCAG_06362; -.
DR   HOGENOM; CLU_002472_0_0_1; -.
DR   OrthoDB; 138168at2759; -.
DR   Proteomes; UP000009297; 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; 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   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..1166
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000338506"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..373
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         935..942
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1166 AA;  128382 MW;  087C983813751370 CRC64;
     MSSSQSTSQL KRKQQTISSF FSKKPVAPNG STTTTPKDGH VKKTIGHARV HEAPSSEMDV
     VDGAHDAAVR PDEEGDDDYQ IILPSRKRIR SNGEVSTLQR GTLADIDNGH SSKGENELQT
     GIMGSSDSDR AEQPVKIKSG SSRTEKFRFS SSSLPSSSDP KGNGGCDVLY AISADGDASE
     DGDEEQKRKQ ALHQKFVKRL GGPDCLPFSV SRVDAGDAEE AEGAESDAEA EAEIVPVPQK
     GRGGKKTTTG KLTPMERQII DIKKKHMDTL LVVEVGYKFR FFGEDARVAA KELSIVCIPG
     KLRFDEHPSE AHLSRFASAS IPVHRLHVHV KRLVEAGYKV GVVRQLETAA LKAAGENRNA
     PFVRKLTNLY TKGTYIDDVE GLEESSGNSG SASTSTGYLL CMAESNAKGW GNDEKVHVGI
     VAVQPATGDV IYDDFEDGFM RSEIEMRLLH IAPCEFLIVG EMSKATEKLV QHLSGSKTNV
     FGDKIRVERV SKSKTAAAES HSHVSSFYAG RMNAKGTTGD VAASNLLEKV LTLPEDVTIC
     LSSMIKHMSE FGLEYVFDLT KYFQPFSARS HMLLNGNTLT NLEIYQNQTD HTSKGSLFWT
     LDRTKTRFGQ RLLRKWVGRP LLDKTELEER VSAVEELQDP SKTVQIERLK GLLSKIRADL
     EKSLIRIYYG RCTRPELLTV LQTLQLIADE YVHLKSPADL GFSSPTITTA IAALPAIRDD
     VVTYLNKINE EAAKKDDKYC FFREVEETDE ITESNLGIAD VQHRLQEHCA VAAEILGKKK
     VQYTTVAGIE YLIEVENSPY NLKKVPASWR KISGTKKVSR FHTPEVVQYM RERDQYKEAL
     AAACDKAFHA LLADISTKYQ SFRDCILALA TLDCLLSLAN IASQPGYIKP AYTDKTRISV
     QRGRHPMVEQ LLLDTYVPND IELHTDETRA LLVTGPNMGG KSSYVRQVAL ISIMGQIGSY
     VPADSATLGM LDAVYTRMGA FDNMLAGEST FMVELSETAD ILKQATPRSL VILDELGRGT
     STHDGVAIAQ AVLDYMVRNL RSLTLFITHY QNLSSMAREF PKGELRNVHM KFTESGMDGQ
     DITFLYEVGE GVAHRSYGLN VARLANVPDS VLEVARAKSA ELEEKIRKKK MLALAKVAKG
     FINTDGDAGG PAPALLERVM VGLEQL