ID A0A319D7W8_9EURO Unreviewed; 1207 AA.
AC A0A319D7W8;
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 {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=BO71DRAFT_484523 {ECO:0000313|EMBL:PYH93555.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH93555.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH93555.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH93555.1,
RC ECO:0000313|Proteomes:UP000247810};
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|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756}.
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DR EMBL; KZ825891; PYH93555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319D7W8; -.
DR STRING; 1448320.A0A319D7W8; -.
DR Proteomes; UP000247810; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:UniProtKB-UniRule.
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; IPR017261; DNA_mismatch_repair_MutS/MSH.
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; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF148; DNA MISMATCH REPAIR PROTEIN MSH6; 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; PIRSF037677; DNA_mis_repair_Msh6; 1.
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, ECO:0000256|PIRNR:PIRNR037677};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR037677};
KW DNA repair {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037677}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000247810}.
FT DOMAIN 1040..1056
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 135088 MW; 2AD5BF6B6002BBA5 CRC64;
MARGTPAASS PTTATPPSAA LKRATSSVQN MKNQKSILGF FQKSSPSTPS TARNAEPASS
PAERVSERRG GSAKGAMKTD RKKSVPRFKQ DLAPVPSSDL VVPEEDEPLD NTQESPDGKA
ETKTGSPSRR TKKQVSYAES DSEGEDDDEK IFRPGRNARN KRRKMSPDSE DEFKDGGDAE
YSDYDIDDFI VADESEEEVK APQKRKRPSA QPKSKSSSLP PPPPTEEDLD LDIPDASAGT
ALKWTYDPES AEPRQPRAAP VTPKRSNTTK QKAHVTEPEQ RYAWLANIRD IDGHPIGHPE
YDPRTLYIPP LAWSKFSPFE KQYWEIKQKF WDTVVFFKKG KFYELYENDA TVGHQLFDLK
LTDRVNMRMV GVPEMSLDHW ANQFVAKGFK IARVDQAESA LGKEMRERDG KKGGKEDKVI
RRELACVLTA GTLVEGSMLQ DDMSTFCVAI KEALIEDRPA FGIAFVDTAT GQFFLSEFVD
DVDMTKFETF VAQIRPQELL LEKSAVSQKT LRILKNNTGP TTIWNHLKPR KEFWEADITV
KELDASDYFV NEDGDNLQAW PEALRKARDQ ELVMSAFGAL VQYLRVLKIE RDLITIGNFS
TYDPIKKATS LVLDGQTLIN MEIFANSFDG GSDGTLFQLL NRCITPFGKR MFKQWVCHPL
VDAKKINARL DAVDALNADP SVRDQFSSQL TKMPDLERLI SRIHAANCKA QDFLRVLEGF
EQIEYTMSLL KDSGSGEGVI GQLINAMPDL NEQLEYWKTA FDRSKARGNG ILVPKPGVEE
DFDNSQEHIE QIHRDLDNLL KRVRRELGSS AIIYKDNGKE IYQLEVPIKV KNVPKDWDQM
SATKQVKRYY FKELRTLIRQ LQEAQETHSQ IVKEVAGRFY ARFDENYAIW LAAVRIVSQL
DCLISLAKAS SSLGQPSCRP EFVDNDRGVL EFEELRHPCL VSSVGDFIPN DVRLGGTRPN
IDLLTGANAA GKSTVLRMTC VAVIMAQIGC HLPCESARLT PVDRIMSRLG ANDNIFAAQS
TFFVELSETK KILSEATPRS LVILDELGRG TSSYDGVAVA QAVLHHVATH IGALGFFATH
YHSLAAEFEN HPEIAPKRMR IHVDDEERRV TFLYKLEEGV AEGSFGMHCA AMCGIPDKVI
ERAEVAAKQW EHTSRLKESL ERRKGGGLVG MGWWSDVAWA LREASGENAE EVSDRSLDVL
SKAIAAL
//
