ID   MSH3_NEOFI              Reviewed;        1117 AA.
AC   A1DCB2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=DNA mismatch repair protein msh3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=msh3; ORFNames=NFIA_025450;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027695; EAW19472.1; -; Genomic_DNA.
DR   RefSeq; XP_001261369.1; XM_001261368.1.
DR   AlphaFoldDB; A1DCB2; -.
DR   SMR; A1DCB2; -.
DR   STRING; 36630.CADNFIAP00002287; -.
DR   PRIDE; A1DCB2; -.
DR   EnsemblFungi; EAW19472; EAW19472; NFIA_025450.
DR   GeneID; 4588147; -.
DR   KEGG; nfi:NFIA_025450; -.
DR   VEuPathDB; FungiDB:NFIA_025450; -.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_0_1; -.
DR   OMA; LRNVHMK; -.
DR   OrthoDB; 138168at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
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:0007534; P:gene conversion at mating-type locus; IEA:EnsemblFungi.
DR   GO; GO:0043570; P:maintenance of DNA repeat elements; IEA:EnsemblFungi.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; PTHR11361; 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; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55271; SSF55271; 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..1117
FT                   /note="DNA mismatch repair protein msh3"
FT                   /id="PRO_0000338525"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..325
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         888..895
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1117 AA;  123663 MW;  DFA6969F2FFD6AFB CRC64;
     MTLSSSQSSP PSSQNLKRKQ QTISSFFTKR APTAEKRSND LEDGRATTQK GAEMPLRETT
     GDQDDLVDDE DGDIVVRAPK RVKTNRVDPE NGFGRNVTRG PDPPSSSSQR TNLCKFASSP
     ADDAGIEKAD DPEARQRQLE REKLHKLFVK KLGGADCLIG IGRNATTEAP SGTEEVAEGD
     EDDESAPPPR SKGKGASKKG GSKLTPLEKQ VIEIKRKHMD TVLVIEVGYK FRFFGEDARI
     AAKELSIVCI PGKMRFDEHP SEAHLDRFAS ASIPVHRLHV HVKRLVSAGY KVGVVRQLET
     AALKAVGDNR NAPFSRKLTN LYTKGTYVDD VEGLDGATPA ASGGASPATG YMLCITETNA
     KGWGNDEKVH VGIVAVQPNT GDIIYDDFED GFMRSEVEAR LLHIAPCELV IVGELSKATE
     KLVQHLSGSK LNTFGDKVRV DRVAKKKTAV AESHSHVANF YAAKLKAANT ADDAPASNLL
     QKVLNLPEQV TVCLSAMIEH LTEYGLEHIF ELTKYFQHFS SRSHMLLNAN TLVSLEIYQN
     QTDHSAKGSL FWTLDRTQTR FGQRLLRKWV GRPLLDKERL EERVNAVEEL KSPDRTVQVE
     RLKILLGRIK SDLEKNLIRI YYGKCTRPEL LTVLQTLQTI AQEYVDVKTP EDSGFTSPIL
     GEAIARVPSI LEDVVKFLNK INMHAARNDD KYEFFRESEE TEGISEHKCG IASVEHELEE
     HRSVAAGILK WPKVTYVTSS GIEYLIEVEN TAAAIKRVPA SWVKVSGTKK LSRFHTPEVI
     QLLRQRDQHK EALAAACDQA FAALLAEIAT NYQSFRDSVQ SLATLDCLLS LAAIASQPGY
     VKPEYTDQTC IHVEQGRHPM VEQLLLDSYV PNDIDLDSDR TRALLVTGPN MGGKSSYVRQ
     IALIAIMAQI GSYVPARSAK LGMLDAVFTR MGAFDNMLAG ESTFMVELSE TADILKQATP
     RSLVILDELG RGTSTHDGVA IAQAVLDYMV RTIRSLTLFI THYQHLSNMA QSFPNHELRN
     VHMRFTESGS GKDEEITFLY EVGEGVAHRS YGLNVARLAN LPAPLLEVAR QKSSELEERI
     RRRRLAGLRA DVGGLMEDPA KGDEDFFQRL ISNAEQL