MSH3_ASPTN
ID MSH3_ASPTN Reviewed; 1117 AA.
AC Q0CPP9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=ATEG_04335;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476599; EAU34782.1; -; Genomic_DNA.
DR RefSeq; XP_001213513.1; XM_001213513.1.
DR AlphaFoldDB; Q0CPP9; -.
DR SMR; Q0CPP9; -.
DR STRING; 341663.Q0CPP9; -.
DR EnsemblFungi; EAU34782; EAU34782; ATEG_04335.
DR GeneID; 4319891; -.
DR VEuPathDB; FungiDB:ATEG_04335; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000007963; 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_0000338513"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..327
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..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..98
FT /note="Basic and acidic 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; 123742 MW; 84F4BF8DE9A9CD4C CRC64;
MPLSSSQSSP PSSQNLKRKQ QTISSFFTKK PQSTKPEESH GADEKQRTNG AEEVGNENRA
PPHTADAAEE DDDDIVAPAP KRARTNAHRQ KDTDQTSDGP PRIAEPPKSS QRTELAKFAS
SPAGAAEPEE MDEEEAQERK KEREKLHKQF VRRLGGPDCL IGINRHVSGE ADPALEEAAE
ADEDEEAVQA PPAKGKAAAK KGGGKLTPME RQIIDMKRKH MDKILAVQVG YKFRFFGEDA
RVAAKELSIV CIPGKFRFDE HPSEAHLDRF ASASIPVHKL HVHVKRLITA GHKVGIVRQI
ETAALKAAGD NRNAPFVRKL TNVYTKGTYI DDMEGLEGPT AGAGTTAATG YMLCITETNA
KGWGNDEKVH VGIVAVQPAT GDIVFDDFED GFMRSEIETR LLHLAPCELL IVGDLSKASD
KLVQHLAGSK MNVFGDKVRV ERTTKSKTAA AEAHSHVSSF YADKVKSANA SDDTQASNLL
QKVLNLPEQV SICLSSMIKH MTEYGLEHVF DLTKYFQHFS SRSHMLLNGN TLMSLEIYQN
QTDHSSRGSL FWTLDRTQTR FGQRLLRKWV GRPLLDKSKL EERVNAIEEL KSMEKVAMVE
RLKGVLGKAK CDLEKILIRI YYGRCTRPEL LTGLQTLQMI AQEFGDVKSP EDSGFTTPIL
NEAIASLPTI LEDVLSFLNK INLHAARNDD KYEFFREAEE TEDISEHKLG IASVEHELRE
YQSVAGKILG RSKIQYVTVA GIDYLIEVEN NSSYLKRVPA SWVKISGTKK LSRFHSPEVI
KLLRQRDQHK EALAAACDHA YASLLAEIAA NYQPFRDCVQ SLATIDCLLS LSSIANQPGY
VKPEYADNTC IHVEQGRHPM VEQLLLDSYV PNDINLDSEE TRALLVTGPN MGGKSSYVRQ
IALIAIMGQV GSYVPAQSAK LGMLDAVFTR MGAFDNMLAG ESTFMVELSE TADILKQATP
RSLVILDELG RGTSTHDGVA IAQAVLDYMV RSLRSLTLFI THYQHLSSMV HSFPNHELRN
VHMRFTESGS GQDEEITFLY EVGEGVAHRS YGLNVARLAN LPVPLIEVAK QKSAELEQKI
RRRRLAGLMS TVENIMSDSA KNDEGLITRL ISSAEQL
