ID A0A397HX39_9EURO Unreviewed; 940 AA.
AC A0A397HX39;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=DNA mismatch repair protein MSH3 {ECO:0000256|ARBA:ARBA00019000};
DE AltName: Full=DNA mismatch repair protein msh3 {ECO:0000256|ARBA:ARBA00022151};
GN Name=MSH2 {ECO:0000313|EMBL:RHZ67562.1};
GN ORFNames=CDV56_109628 {ECO:0000313|EMBL:RHZ67562.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ67562.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ67562.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ67562.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025373}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1).
CC {ECO:0000256|ARBA:ARBA00025902}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000256|ARBA:ARBA00006271, ECO:0000256|RuleBase:RU003756}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ67562.1}.
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DR EMBL; NKHU02000006; RHZ67562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HX39; -.
DR STRING; 41047.A0A397HX39; -.
DR VEuPathDB; FungiDB:CDV56_109628; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000215305; 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 CDD; cd03285; ABC_MSH2_euk; 1.
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; IPR011184; DNA_mismatch_repair_Msh2.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
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; IPR032642; Msh2_ATP-bd.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF35; DNA MISMATCH REPAIR PROTEIN MSH2; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 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; PIRSF005813; MSH2; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 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 {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003756};
KW DNA repair {ECO:0000256|RuleBase:RU003756};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003756};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003756}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT DOMAIN 737..753
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
SQ SEQUENCE 940 AA; 105556 MW; 65AA623A9A75E565 CRC64;
MSSRPDLKVD DEVGFIRFYR SLSSDGNDET IRVFDRGDWY SAHGAEAEYI ARTVYKTTSV
LRNLGRSETG GLPSVTMSVT VFRNFLREAL FKLNKRIEIW ASVGAGRGQW KLIKQASPGN
LQDVEEELGS VGGLAMESAP VILAVKISAR ASEARGVGVC FADASVRELG VSEFLDNDVY
SNFESLIIQL GVKECLVQMD SNRKDVELGK IRAIADNCGI AISERPVADF GVKDIEQDLT
RLLRDERSAA TLPQTELKLA MGSASALIKY LGVMSDPSNF GQYHLYQHDL SQFMKLDASA
LRALNLMPGP RDGSRTMSLF GLLNHCKTPV GSRLLAQWLK QPLMDLAEIE KRQQLVEAFV
ENTELRQTMQ EEHLRSIPDL YRLAKRFQRK QANLEDVVRV YQVAIRLPGF VSSLDNVMDE
QYQTPLETEY TSKLRSHSDS LAKLEEMVET TVDLAALENH EFIIKPEFDD SLRIIRKKLD
KLRHDMDVEH RRVARDLDQE VDKKLFLENH RVHGWCFRLT RNEAGCIRNK KEYQECSTQK
NGVYFTTSTM QALRREHDQL SSNYNRIQTG LVNEVVNVAT SYCPVLEQLA GVLAHLDVIV
SFAHAAVHAP TAYVRPKMHP RGTGNTILKE ARHPCMEMQD DISFITNDVS LIRDESSFLI
ITGPNMGGKS TYIRQIGVIA LMAQTGCFVP CSEAEMTIFD CILARVGASD SQLKGVSTFM
AEMLETSNIL KSATSESLII IDELGRGTST YDGFGLAWAI SEHIVTEIRC FGLFATHFHE
LTALADRYPK SVKNLHVVAF IGDGTNDNSE ERKSKKEQVT LLYRVEPGIC DQSFGIHVAE
LVRFPEKVVN MARQKAEELE DFTSAEAQGQ QSSMPIDGYS QEEVEEGSAL LKGMLLKWKA
EIESSDRKLT VEEKRQIMRD LVNADEKLRA NKVFQGIKAL
//
