MSH3_ASPOR
ID MSH3_ASPOR Reviewed; 1111 AA.
AC Q2UT70;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=AO090005000134;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007151; BAE55245.1; -; Genomic_DNA.
DR RefSeq; XP_001817247.1; XM_001817195.1.
DR AlphaFoldDB; Q2UT70; -.
DR SMR; Q2UT70; -.
DR STRING; 510516.Q2UT70; -.
DR PRIDE; Q2UT70; -.
DR EnsemblFungi; BAE55245; BAE55245; AO090005000134.
DR GeneID; 5989192; -.
DR KEGG; aor:AO090005000134; -.
DR VEuPathDB; FungiDB:AO090005000134; -.
DR HOGENOM; CLU_002472_0_0_1; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000006564; Chromosome 1.
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..1111
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338512"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..319
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 883..890
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1111 AA; 123542 MW; 27BCB3328993717C CRC64;
MPLSSQPSSS NLKRKQPTIS SFFTKKPQLS QESISNDVLE KEERDEEREE VAKQEEGLRE
NGGTRSNNVD DDEDDVVAPA SKRARTNGSH SQNTIETPKE KHVERPLPSD SIQKTELSKF
ASSPATEGET KERTKERERL HQKFVRRLGG PDCLIGIGRN TAPEAVPEEV GEGDEDDEPS
PPPAAKGKAT AKKGARKLTP MEKQVIDIKR KHMDTVLVVE VGYKFRFFGE DARTAAKELN
IVCIPGKFRF DEHPSEAHLD RFASASIPVH RLHVHVKRLV SAGHKVGVVR QMETAALKAA
GDNRNAPFGR KLTNLYTKGT YIDDMEGLEG STASMSATGT SMATGYMLCI TETNTKGWGN
DEKVLVGIVA VQPATGDIVY DEFEDGFMRS EIETRLLHLA PCEVLIVGDL SKATEKLVQH
LSGNKTNAFG DEIRVERAPK AKTAAAESHS HVSSFYAERM KKVNATNDVQ ASSLLQKVLN
LSEQATICLS SMIKHMSEYG LEHVFQLTKY FQHFSSRSHM LLNANTLNSL EIYHNQTDHS
TKGSLFWTLD RTQTRFGQRM LRKWVGRPLL NKLGLEERVD AVEELKNLER VALVEQMKCL
LGRIKTDLEK SLIRVYYGKC TRPELLTLLQ TLQMIAQEFA GVQSPADTGF SSPLISKAVA
SLPTILEDVV RFLDKINMHA AKNDDKYEFF RESEETDEIT EHKLGIGAVE HDLEEHRSTA
GEILGKRKVD YVTVAGIEYL IAVENKSPSI KKVPASWVKI SGTKAVSRFH TPEVIRLLRQ
RDQHKEALAA GCDKAYATFL AEISASYQSF RDSVQSLATL DCLISLATIA NQPGYVKPEY
TNHTCIQVDQ GRHPMVEQLL LDSYVPNDID LDSDKTRALL VTGPNMGGKS SYVRQVALIA
IMGQIGSYVP ARSAKLGMLD AVFTRMGAFD NMLAGESTFM VELSETADIL KQATPRSLVI
LDELGRGTST HDGVAIAQAV LDYMIRSIRS LTLFITHYQH LSSMVHSFPD HELRNVHMRF
TESGPTEEEI TFLYEVREGV AHRSYGLNVA RLANLPAPLI ELAKQKSAEL EQKIHRRRLA
GLVRTVGDIL ADSAKADESL IERLISSAEQ L
