MSH3_ASPCL
ID MSH3_ASPCL Reviewed; 1130 AA.
AC A1CDD4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=ACLA_006180;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027051; EAW11861.1; -; Genomic_DNA.
DR RefSeq; XP_001273287.1; XM_001273286.1.
DR AlphaFoldDB; A1CDD4; -.
DR SMR; A1CDD4; -.
DR STRING; 5057.CADACLAP00000673; -.
DR EnsemblFungi; EAW11861; EAW11861; ACLA_006180.
DR GeneID; 4705676; -.
DR KEGG; act:ACLA_006180; -.
DR VEuPathDB; FungiDB:ACLA_006180; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000006701; 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..1130
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338508"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..339
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 901..908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1130 AA; 124666 MW; B5B8C28DF16AD3C1 CRC64;
MPLRSSQSSP PASQSFKRKQ PTISSFFTKK PPTSQEKAQE PEDEPAASRR QFANALDKAT
RVKEHGAPAE RDEEQEEEEE DIVAPAPKRI KTNGVHEKEP ASAAKEVSSA SRPAPPLASS
QRTELYKFAS SPADGAGAGV DRPEDPETKQ RQAERERLHQ LFVKKLGGAD CAVGIGRSAG
GDAPSGAEEA AEGDEDEEVA PAPAAKGRGS KKAGGGKLTP LEKQVIEIKR KHMDTVLVIE
VGYKYRFFGE DARIAAKELS IVCIPGKMRF DEHPSEAHLD RFASASIPVH RLHVHVKRLV
AAGYKVGVVR QLETAALKAA GDNRNAPFSR KLTNLYTKGT YVDDVEGLEG PTPAASGGAS
PATGYLLCIT ETNAKGWGND ERVHVGIVAV QPNTGDIIYD DFEDGFMRSE VETRLLHIAP
CELVIVGELS KATEKLVQHL SGSKLNTFGD KVRVERVGKK KTAVAESHSH VANFYASKLK
AASVDDTQTS NLLQKVLTLP EQVTVCLSAM IEHMTEYGLE HIFQLTKYFQ HFSSRSHMLL
NANTLVSLEI YQNQTDHSTK GSLFWTLDRT QTRFGQRLLR KWVGRPLLDK SRLEERVNAV
EELKNPEKTV QVERLKRLLG RIKSDLEKNL IRIYYGKCTR PELLTVLQTL QTIAQEYADV
KSPEDNGFAS PVLGEAVASL PTILKDVVAF LNKINMHAAR SDDKYEFFRE SEETDEISEH
KLGIASVEHE LEEHRAVAAG ILKWPKVVYV TSSGIEYLIE VENTSNAIKR VPASWVKVSG
TKKLSRFHTP EVIQLLRQRD QHKEALAAAC DKAFAALLAE IAVNYQLFRD CVQALATLDC
LLSLAAIASQ PGYVKPEYTD HTCICVEQGR HPMVEQLLLD SYVPNDTDLD TDQTRALLVT
GPNMGGKSSY VRQVALIAIM GQIGSYVPAR SAKLGMLDAV FTRMGAFDNM LAGESTFMVE
LSETADILKQ ATPRSLVILD ELGRGTSTHD GVAIAQAVLD YMVRTIRSLT LFITHYQHLS
NMTQSFPDHE LRNVHMRFTE SGAGQDEEIT FLYEVGEGVA HRSYGLNVAR LANLPAPLLD
VAKLKSAELE EQIRRRRLAR LLTAVGEVMS DPAKGDEDFL ERLMSTAEQL
