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Database: UniProt
Entry: A0A1F8A1P3_9EURO
LinkDB: A0A1F8A1P3_9EURO
Original site: A0A1F8A1P3_9EURO 
ID   A0A1F8A1P3_9EURO        Unreviewed;      1111 AA.
AC   A0A1F8A1P3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN   ORFNames=ABOM_006268 {ECO:0000313|EMBL:OGM45634.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM45634.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM45634.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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. MSH3
CC       subfamily. {ECO:0000256|ARBA:ARBA00007094}.
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:OGM45634.1}.
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DR   EMBL; LYCR01000040; OGM45634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8A1P3; -.
DR   STRING; 109264.A0A1F8A1P3; -.
DR   OrthoDB; 168255at2759; -.
DR   Proteomes; UP000179179; 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; 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: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; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 2.
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 {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};
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:UP000179179}.
FT   DOMAIN          957..973
FT                   /note="DNA mismatch repair proteins mutS family"
FT                   /evidence="ECO:0000259|PROSITE:PS00486"
FT   REGION          1..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1111 AA;  123253 MW;  3FA6320BD15965C7 CRC64;
     MPLSSQPSSS PNLKRKQPTI SSFFTKKPQL SQESTSNDAF KEYERDQEGQ EVTKQEKASR
     GNCSTRSNSV DDEDDVVAPA PKRARINGSY SQNTTESPKE THVERPRLSD NIPKTELSKF
     ASSPATEGET KERTKEREKL HQKFVQRLGG PDCLIGIGRN TATEAVPEEA GEGDEGDEPS
     PPPAAKGKAA TKKGGHKLTP MEKQIIDIKR KHMDTVLVVE VGYKFRFFGE DARTAAKELN
     IVCIPGKFRF DEHPSEAHLD RFASASIPVH RLHVHVKRLV SAGHKVGVVR QMETAALKAA
     GDNRNAPFGR KLTNLYTKGT YIDDMEGLEG STASISAAGT TMATGYMLCI TETNAKGWGN
     DEKVHVGIVA VQPATGDIVY DEFEDGFMRS EIETRLLHLA PCEVLIVGDL SRATEKLVQH
     LSGNKTNAFG DEIRVEKFPK AKTAAAESHS HVSSFYAERM KNANTTDDAQ ASSLLQKVLN
     LSEQVTICLS SMIKHMSEYG LEHVFQLTKY FQHFSSRSHM LLNANTLNSL EIYHNQTDHS
     TKGSLFWTLD RTQTRFGQRM LRKWVGRPLL DKSSLEERVD AVEELKNPER IALVERLKGL
     LGRIKTDLEK SLIRVYYGKC TRPELLTLLQ TLQMIAQEFA GVQSPADTGF SSPLISKAVA
     SLPTILEDVV HFLDKINMHA AKNDDKYEFF RESEETDEIT EHKLGIGAVE HDLEEHRSTV
     GECLGKKKVE YVTVAGIEYL IAVENKSPSI KKVPASWVKI SGTKAVSRFH TPEVIRLLRQ
     RDQHKEALAA GCDKAYASFL GEISASYQSF RDSVQSLATL DCLISLATIA NQPGYVKPEY
     TDHTCIHVDQ GRHPMVEQLL LDSYVPNDID LDSDKTRALL VTGPNMGGKS SYVRQVALIA
     IMGQIGSYVP AQSAKLGMLD AVFTRMGAFD NMLAGESTFM VELSETADIL KQATPRSLVI
     LDELGRGTST HDGVAIAQAV LDYMIRSIRS LTLFITHYQH LSSMTHSFPD HELRNVHMRF
     TESGLTEEEI TFLYEVGEGV AHRSYGLNVA RLANLPAPLI ELAKQKSAEL EQKIRRRRLA
     GLVRTFGDVL SDPAKADETL IEQLISSAEQ L
//
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