MSH3_PHANO
ID MSH3_PHANO Reviewed; 1119 AA.
AC Q0UXL8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; ORFNames=SNOG_03496;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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=EAT88701.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAT88701.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH445329; EAT88701.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001794057.1; XM_001794005.1.
DR AlphaFoldDB; Q0UXL8; -.
DR SMR; Q0UXL8; -.
DR STRING; 13684.SNOT_03496; -.
DR GeneID; 5970920; -.
DR KEGG; pno:SNOG_03496; -.
DR eggNOG; KOG0218; Eukaryota.
DR InParanoid; Q0UXL8; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
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; SSF53150; SSF53150; 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_0000338527"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..215
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..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 896..903
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1119 AA; 124391 MW; FE650E301BFF312E CRC64;
MAPKSSQSSQ GLSQRSKQQT ISSFFTPKPS QTPKAPPKPA ALAVPNGADQ DDDDDEDEDI
APPRQLTPAR KRSIDEQHED EEAGRSSPPK RVRVANDEPR PSLGNASATT LNAAKPPKIT
ERTSKFLFSS SPVVRDETDA KDDAAATQKL REKLHEKFVK KLGRPDSFAE LRRRNKVISE
DNGNGEEGEG EEDEEEEEPA PKPTKGRKGA ATKKTSKLTP MELQYLDIKR KHMDTVIVME
VGYKFKFFGE DARTASKELG IVCIPGKFRY DEHPSEAHYD RFASASFPVH RLQVHVKRLV
KANHKVGVVR QLETAALKAA GNNRNTPFVR KLTNLYTKGT YVDDIEGLET PTAGAQATGY
LLCVTETNAK GWGTDEKVQV GLVAVQPATG DIIYDDFEDG FMRSEIETRL LHIAPAEFLI
VGDLSKATDK LIHHLSASKT NVFGDRSRVE RVEKPKTMAA QAYSHISNFY ADKMKSSQEG
GSEQGAILDK VHQLSEHVTI CLSAMITYLS DYALEHVFDL TKYFQPFSAR SYMLLNGNTL
SSLEIYQNQT DYTSKGSLFW TMDRTKTRFG QRLLRKWVGR PLIDKERLEE RIAAVEELKE
GEHTIAVDKV KFLLGKIKTD LEKVLIRIYY KKCSRPELLA ALQILQDIAS QYLSAKTPEQ
SGFSSILLSE AVSNVPKIYE DVNSFLEKIN AKAAKDDDKY GFFREEFEAE DINDLKLSIA
SVEDDLNTHR KDAAAKLGKT KVDYVTVAGI EYLIEVKRKS VEEKKVPASW QQISATKTTL
RFHTPEVKRM LQERDQYKES LAAACDTAFK RLLDDIAAKY QSLRDCVSSL ATLDALLSLA
TLANQPGYVK PTFVETTELD IVGGRHPMVE QLLLDAYVPN DVHLSGDATR ALLVTGPNMG
GKSSYVRSAA LIAIMGQIGS YVPAESAKLG MLDAVFTRMG ALDNMLKGES TFMVELNETA
DILRSATSRS LIILDELGRG TSTFDGVAIA EAVLDYVIRD VGALTLFITH YQHLARLQDR
FNGELKNVHM SFEERDGGKE VVFLYEVAEG TSHRSYGLNV ARLAKVPEKV IETAEVKSSE
LEESMGISRV ANMARMVKGL LEDGGEEGLE RLIEGIEQL
