ID   MSH3_COCIM              Reviewed;        1125 AA.
AC   Q1DQ73; A0A0D6K9M9; J3K482;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; ORFNames=CIMG_07540;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704913; EAS28794.2; -; Genomic_DNA.
DR   RefSeq; XP_001240377.2; XM_001240376.2.
DR   AlphaFoldDB; Q1DQ73; -.
DR   SMR; Q1DQ73; -.
DR   STRING; 246410.Q1DQ73; -.
DR   PRIDE; Q1DQ73; -.
DR   EnsemblFungi; EAS28794; EAS28794; CIMG_07540.
DR   GeneID; 4559896; -.
DR   KEGG; cim:CIMG_07540; -.
DR   VEuPathDB; FungiDB:CIMG_07540; -.
DR   InParanoid; Q1DQ73; -.
DR   OMA; LRNVHMK; -.
DR   OrthoDB; 138168at2759; -.
DR   Proteomes; UP000001261; 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..1125
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000338518"
FT   REGION          1..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..335
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        42..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         898..905
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1125 AA;  124644 MW;  183A382057370B79 CRC64;
     MSQSSSLKRK QQPTISSFFG KTTSSSGEST NKKASLNGLG RAKQRIREEE SNLSPSPEDK
     GEYLDDEDED IVPPSRKRVK SSRISTDGAN AAAKGNDDDL SQSPHRNVPA SSRTERFRFQ
     SSPVSSLDAE GSQVEGREAI DTERERKRKE NLHQKFVRRL GGPGCLPSLE HGSNANTAMT
     EGGEDEDEAL DEEDVAPPPS TKARGARKAA STKLTPLEKQ VIDIKNKHKD AILVVEVGYK
     FRFFGEDARI AAKELSIVCI PGKLRFDEHP SEAHLNRFAS ASIPVHRLHV HVKRLVRAGH
     KVGVVRQLET AALKAAGDNR NAPFERKLTH LYTKGTYIDD TEELEGLNAV GANSAAPATG
     YLLCMTESNA KGWGNDEKVQ VGILAVQPAT GNIIHDSFED GFMRTEIETR LLHIAPCEFL
     LIGDVSRATD KLVQHLSGSK MNVFGDKVRV ERVSKSKTAA AESHSHVSSF YAGRMKATST
     TQDERARDLL DKVLNLPEDV TICLSAMIKH LKEYNLENVF DLTKYFQPFS ARSHMLLNGN
     TLINLEIYQN QTEQTSKGSL FWTLDRTKTR FGQRLLRKWV GRPLLDKQEL EDRVAAVTEL
     KDSDATPRVG RLKTLLSKVK TDLEKNLLRI YYGKCTRPEL LTVLQTLQLI ATEFSHVKSP
     ADAGFDSPVI NEAISQLPVV LDDVVSYLNK INLHSAKADD KFSFFQESEE TDEITEQKLG
     IGSVEHDLEE YRNTAAEILC KKKVCYVTNA GIEYLIEVEN SSLQMKKIPA SWRKISGTKK
     VSRFHPPEVV NLMRERDQHK EALAAACDKA FLGLLADIST KYQPFRDCIQ ALATLDCFMS
     LAAVAAQPGY VRPTYADEAR ISVRGGRHPM VEQLLLDTYV PNDTELGTDG TRALLVTGPN
     MGGKSSYVRQ VALISIMGQI GSYVPAESAT LGMLDAVYTR MGAFDNMLAG ESTFMVELSE
     TSDILKQATP RSLVILDELG RGTSTHDGVA IAQAVLDYMV RDIRSLTLFI THYQHLSNLA
     RTFPNGELRN VHMKFTESGK DGQDITFLYE VGEGVAHRSY GLNVARLANI PSSVLDVAYT
     KSAELEEKIK RKNLEGIAKG LSRVLENGEN EGELMERLLS EVEQL