MSH3_ASPNC
ID MSH3_ASPNC Reviewed; 1119 AA.
AC A2R1F6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=An13g01060;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK41506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM270298; CAK41506.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2R1F6; -.
DR SMR; A2R1F6; -.
DR PaxDb; A2R1F6; -.
DR PRIDE; A2R1F6; -.
DR EnsemblFungi; CAK41506; CAK41506; An13g01060.
DR Proteomes; UP000006706; Chromosome 2L.
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; 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; PTHR11361; 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; 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..1119
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338511"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..329
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 892..899
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1119 AA; 123133 MW; BEFF524495F9CD2C CRC64;
MPLPSSQNSS SPGVKRKQST LASFFTKKPQ TAQQASVNVV EEKSPAATFD KADNQERAAK
KDKALTDDEE DDIVAPAPKR VRTNGLYPAS REEIPNSTST TERPPALTSS QRTERFKFSS
SPAVNTGVEG SQAAVELEAG QRQKEREELH HKFVRKLGGA DCLIGIGRNA ISEATPEEGA
EPEDEEEAAP PPPAKGKAAA KKGGSKLTPM EKQVIDIKRK HMDTVLVVEV GYKFRFFGED
ARVAAKELSI VCIPGKLRFD EHPSEASHLD RFASASIPVH RLHVHVKRLV AAGHKVGVVR
QIETAALKAA GDNRNAPFVR KLTNLYTKGT YIDDAEGLGG PMPAASGGAS PATGYLLCIT
ETNAKGWGND EKVQVGIVAV QPATGDIVYD DFEDGFMRSE IETRLLHIAP CELLIVGELS
KATEKLVQHL SGSKLNVFGD KTRVERVLKS KTAAAESHSH VSSFYAGKMK TASAADDAQA
SSLLQKVLNL PEQVTICLSS MIEHMKEYGL EYVFELTKYF QHFSSRSHML LNGNTLMSLE
IYQNQTDHTT KGSLFWTLDR TQTRFGQRML RKWVGRPLLD KSRLEERVNA VEELKNPEKT
VMVERLKGLL GKVKSDLEKS LIRIYYGKCT RPELLTVLQT MQMIAQEFSD VKSPADTGFA
STAINEAITC LPTILEDVVA FLDKINMHAA KSDDKYAFFR EAEETEDISD QKLGIASVEH
ELEEHRSVAG QKLGKKTVEY KSVAGIDYLI EVENSSASIK RVPASWVKVS GTKKVSRFHT
PEVIQLMRQR DQHKEALAAA CDQAFISLLA DIATKYQPFR DSVQALATLD CLIALATIAS
QPGYVKPEYT DHTCIQVDQG RHPMVEQLLL DSYVPNDIDL DSDKTRALLV TGPNMGGKSS
YVRQVALIAI MGQIGSYVPA QSAKLGMLDA VFTRMGAFDN MLAGESTFMV ELSETADILK
QATPRSLVIL DELGRGTSTH DGVAIAQAVL DYMVRSIRSL TLFITHYQHL SSMVHSFADQ
ELRNVHMRFT ESGTGTDEEI TFLYEVGEGV AHRSYGLNVA RLANLPGALL DQARQKSKEL
EEKIRRRKLA GLVTAVGEVI EGSKDENMIE RLISSAEQL
