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 24-JAN-2024, entry version 79.
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.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476660; EDN09195.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A6R7S1; -.
DR SMR; A6R7S1; -.
DR STRING; 339724.A6R7S1; -.
DR HOGENOM; CLU_002472_0_0_1; -.
DR OrthoDB; 168255at2759; -.
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; 1.10.1420.10; -; 2.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF122; DNA MISMATCH REPAIR PROTEIN MSH3; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF01624; MutS_I; 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; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
