ID A0A319FGU2_ASPSB Unreviewed; 1007 AA.
AC A0A319FGU2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=DNA mismatch repair protein MSH3 {ECO:0000256|ARBA:ARBA00019000};
DE AltName: Full=DNA mismatch repair protein msh3 {ECO:0000256|ARBA:ARBA00022151};
DE Flags: Fragment;
GN ORFNames=BO78DRAFT_429868 {ECO:0000313|EMBL:PYI06173.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI06173.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI06173.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI06173.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-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}.
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DR EMBL; KZ826351; PYI06173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319FGU2; -.
DR STRING; 1448318.A0A319FGU2; -.
DR Proteomes; UP000248423; 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; -; 1.
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; 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:SF34; DNA MISMATCH REPAIR PROTEIN MSH1, MITOCHONDRIAL; 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; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 3.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 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};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423}.
FT DOMAIN 866..882
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 977..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PYI06173.1"
SQ SEQUENCE 1007 AA; 112001 MW; 894EAC243D570ADC CRC64;
MMRFHVYPRC QRQAVFITRS VPWPYRCQVR TICHHVRPCV PRVTCSPVPR RSAKTQSTVK
LKDLPQGALK LEPYQDAVDD IPKYPVVVQG HWNNMQKFKN CVILTRVGGF YELYFEQAEE
MAPLLNLKLA SKKTSAGPVP MAGFPFFQLD RFLKILVQDL NKYVAVSEEF PIAAEDKLRS
GLLFDRKVAR IITPGTLIDE KFMDPSENNF LLAVYIDKAS LKKQLEQQDG SAAQHALLSA
SQNVGLSWLD LSTGDFFTQV TTAQMLPSAI ARIGAREILV DQGLQDMIGQ ELQLLVGHDH
RLMTFFDFPH KVAPMSRWGT MLEAPVSAAA AASFAADEIA AGYSLLEYIR VQLQGLNMKL
QPPRRRHLDE SMSIDRNSLR GLEIVETARD GFGKGSLLHA VRRTSTKSGA RLLRDRLTSP
STSIPVINER LDLVSVFIDD HELHDSVTQF LKRSYDAQRL VQKFTLGRGD PDDLICLSRA
IEASKEIKRV LSSKIHAASQ QRSLAAMVNR LHMDGPTALA DKILAAIDEE GLLQKQRIED
DTAAEAAMLA QKVTLNEGIP GDMAALPKKV KTKSSDRTAA IDEGSIVDTW IMRRDASPAL
SDLHHELDQL HIGKSELTQR LRDSVGSSAL TLKWTPGLGH ICHVKGAKIT QAALEDLGVT
RNVSTTKSTR SFYLPAWTDL GGQIDQIRSQ IRQEEQVIFE HLRREVILNL VKIRRNASII
DELDVACSFA TLAQEQHLTR PILNTSTTHK ILSGRHPTVK LGLEEQGRHF ISNDCILGSS
SSPTERIWLI TGPNMAGKST FLRQNALITI LAQVGSFVPA AYAELGLVDK IFSRIGAADD
LFRDQSTFMV EMLETAAILK QATERSFVIM DEVGRGTTPE DGTAVGFACL HHLHYRNRCR
TLFATHFHAL ADMTGGFEAL GRYCTDVRES ESEGGTGTFS FVHRLRKGVN RESHALKVAQ
LAGLPREAIE MARRVRGRFT SGEGPRWDGE EGSEPVDGTS HHNQKPS
//
